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Conserved domains on  [gi|767988556|ref|XP_011544153|]
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integrin alpha-M isoform X3 [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 10106982)

integrin alpha forms a heterodimer with integrin beta to mediate cell-extracellular matrix and cell-cell interactions; integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

Graphical summary

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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 2.06e-96

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: 292.72  E-value: 2.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 149 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988556 307 PPRDHVFQVNNFEALKTI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-563 9.55e-11

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: 57.39  E-value: 9.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767988556   517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 563
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 3.20e-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: 50.45  E-value: 3.20e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988556   453 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 495
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 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 2.06e-96

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: 292.72  E-value: 2.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 149 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988556 307 PPRDHVFQVNNFEALKTI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 1.27e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 164.76  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556  150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQL--KKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRT-H 226
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556  227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIAS 305
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 767988556  306 KPPRDHVFQVNNFEALKTIQNQ 327
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-321 1.74e-40

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: 145.29  E-value: 1.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556   150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLL-GRTH 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556   227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsekSRQELNTIASK 306
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                          170
                   ....*....|....*
gi 767988556   307 PPRDHVFQVNNFEAL 321
Cdd:smart00327 157 PGGVYVFLPELLDLL 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-563 9.55e-11

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: 57.39  E-value: 9.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767988556   517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 563
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 3.20e-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: 50.45  E-value: 3.20e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988556   453 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 495
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-304 5.70e-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: 54.17  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 145 PQEDSDIAFLIDGSGSIIPHD-FRRMKEFVSTVMEQLKKsKTLFSLMQYSEEFRIH--FTFkefqnnpNPRSLVKPITQL 221
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLlpLTR-------DREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 222 --LGRTHTATGIRKVVRELfnitNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsEKSRQE 299
Cdd:COG1240  161 ppGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEGL 233


                 ....*
gi 767988556 300 LNTIA 304
Cdd:COG1240  234 LREIA 238
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 2.85e-07

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: 47.12  E-value: 2.85e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988556  521 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNRGAVYLF 556
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 457-493 5.46e-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: 37.88  E-value: 5.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988556  457 FGASLCSVDVDSNGSTDLVlIGAPHYYEQtRGGQVSV 493
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
 
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 2.06e-96

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: 292.72  E-value: 2.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 149 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988556 307 PPRDHVFQVNNFEALKTI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 1.27e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 164.76  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556  150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQL--KKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRT-H 226
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556  227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIAS 305
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 767988556  306 KPPRDHVFQVNNFEALKTIQNQ 327
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-321 1.74e-40

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: 145.29  E-value: 1.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556   150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLL-GRTH 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556   227 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsekSRQELNTIASK 306
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                          170
                   ....*....|....*
gi 767988556   307 PPRDHVFQVNNFEAL 321
Cdd:smart00327 157 PGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-313 2.46e-35

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: 130.49  E-value: 2.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGR-TH 226
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELFNITNgARKNAFKILVVITDGEKFGDPlGYEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIASK 306
Cdd:cd01450   82 TGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPA-----DEEELREIASC 154


                 ....*..
gi 767988556 307 PPRDHVF 313
Cdd:cd01450  155 PSERHVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-313 4.05e-27

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: 107.65  E-value: 4.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPIT-QLLGRTH 226
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELFNITNGARKnafKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDafrsEKSRQELNTIASK 306
Cdd:cd00198   82 IGAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGD----DANEDELKEIADK 154


                 ....*..
gi 767988556 307 PPRDHVF 313
Cdd:cd00198  155 TTGGAVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 150-318 6.46e-26

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: 104.29  E-value: 6.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 227
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 228 ATGIRKVVRELFNITNGARKNAFKILVVITDGeKFGDplgyeDVIPEADR---EGVIRYVIGVGDAFRSeksrqELNTIA 304
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDG-KSQD-----DVELPARVlrnLGVNVFAVGVKDADES-----ELKMIA 150

                        170
                 ....*....|....
gi 767988556 305 SKPPRDHVFQVNNF 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 1.30e-25

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: 103.46  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 227
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGpdGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 228 ATGIRKVVRELFNITNGARKNAFKILVVITDGEKfgdplgYEDVIPEAD---REGVIRYVIGVGDAfrsekSRQELNTIA 304
Cdd:cd01472   82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKS------QDDVEEPAVelkQAGIEVFAVGVKNA-----DEEELKQIA 150

                        170
                 ....*....|....
gi 767988556 305 SKPPRDHVFQVNNF 318
Cdd:cd01472  151 SDPKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 150-332 3.22e-22

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: 95.53  E-value: 3.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSK--TLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 227
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 228 ATGIRKVVRELFNITNGARK---NAFKILVVITDGEKfGDPLGyeDVIPEADREGVIRYVIGVGDAFRSeksrqELNTIA 304
Cdd:cd01475   84 GLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRP-QDDVS--EVAAKARALGIEMFAVGVGRADEE-----ELREIA 155

                        170       180
                 ....*....|....*....|....*...
gi 767988556 305 SKPPRDHVFQVNNFEALKTIQNQLREKI 332
Cdd:cd01475  156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 150-331 3.41e-15

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: 74.08  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIpHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTAT 229
Cdd:cd01474    6 DLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 230 GIRKVVRELFNITNGARKNAfKILVVITDGEKFGDPLGY-EDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIASKPp 308
Cdd:cd01474   85 GLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYpEHEAKLSRKLGAIVYCVGVTDF-----LKSQLINIADSK- 157

                        170       180
                 ....*....|....*....|....
gi 767988556 309 rDHVFQVNN-FEALKTIQNQLREK 331
Cdd:cd01474  158 -EYVFPVTSgFQALSGIIESVVKK 180
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 149-313 2.70e-13

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: 68.19  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 149 SDIAFLIDGSGSIIpHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFR--IHFTFKEFQNNPNPRSLVKPITQLLGR 224
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEigPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 225 THTATGIRKVVrELFNITNGARKNAFKILVVITDGEKFGDPLGyedvIPEADREGVIRYVIGVGDAFRSEKSRQELNTIA 304
Cdd:cd01476   80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEK----QARILRAVPNIETFAVGTGDPGTVDTEELHSIT 154


                 ....*....
gi 767988556 305 SKPprDHVF 313
Cdd:cd01476  155 GNE--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 2.76e-12

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: 65.04  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPItQLLGRTHT 227
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRL-RLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 228 ATG--IRKVVRELFNITNGAR--KNAFKILVVITDGEKFGDplgYEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTI 303
Cdd:cd01481   81 NTGsaLDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDD---VERPAVALKRAGIVPFAIGARNA-----DLAELQQI 152

                        170
                 ....*....|....*
gi 767988556 304 ASKPprDHVFQVNNF 318
Cdd:cd01481  153 AFDP--SFVFQVSDF 165
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 150-297 4.73e-11

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: 62.02  E-value: 4.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSI-IPHDFRRMKEFVSTVMEQLKKSK--TLFSLMQYSEEFRIHFTFKEFqNNPNPRSLVKPITQLL---- 222
Cdd:cd01471    2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPdeINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLslyy 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988556 223 --GRTHTATGIrKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADReGVIRYVIGVGDAFRSEKSR 297
Cdd:cd01471   81 pnGSTNTTSAL-LVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRER-GVIIAVLGVGQGVNHEENR 155
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-563 9.55e-11

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: 57.39  E-value: 9.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767988556   517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 563
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
VWA_2 pfam13519
von Willebrand factor type A domain;
151-256 4.56e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556  151 IAFLIDGSGSI-----IPHDFRRMKEFVSTVMEQLKKSKtlFSLMQYSEEFRIHFTFKefQNNPNPRSLVKPITQLLGRT 225
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPGDR--VGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767988556  226 HTATGIRKVVRELFNITNGARknafKILVVI 256
Cdd:pfam13519  77 NLAAALQLARAALKHRRKNQP----RRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 150-321 4.96e-10

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: 59.32  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTL--------FSLMQYSEEFRIHFTFKEFQNNPNP-RSLVKPITQ 220
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagswrVGVVQYSDQQEVEAGFLRDIRNYTSlKEAVDNLEY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 221 LLGRTHTATGIRKVVRELFNITNGARKnafKILVVITDGEKFG-DPLGYEDVIPEADREGVIRYVIGVGdAFRSEKsrqe 299
Cdd:cd01480   84 IGGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHSDGsPDGGIEKAVNEADHLGIKIFFVAVG-SQNEEP---- 155

                        170       180
                 ....*....|....*....|..
gi 767988556 300 LNTIASKPPRDHvfQVNNFEAL 321
Cdd:cd01480  156 LSRIACDGKSAL--YRENFAEL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 3.20e-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: 50.45  E-value: 3.20e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988556   453 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 495
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-304 5.70e-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: 54.17  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 145 PQEDSDIAFLIDGSGSIIPHD-FRRMKEFVSTVMEQLKKsKTLFSLMQYSEEFRIH--FTFkefqnnpNPRSLVKPITQL 221
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLlpLTR-------DREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 222 --LGRTHTATGIRKVVRELfnitNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsEKSRQE 299
Cdd:COG1240  161 ppGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEGL 233


                 ....*
gi 767988556 300 LNTIA 304
Cdd:COG1240  234 LREIA 238
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 2.85e-07

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: 47.12  E-value: 2.85e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988556  521 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNRGAVYLF 556
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 150-322 1.72e-05

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: 46.13  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 150 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNpNPRSLVKPITQLLGRTH- 226
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISsyEVSPRYEIISYASDPKEIVSIRDFNSN-DADDVIKRLEDFNYDDHg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 --TATGIR---KVVRELFNITNGARKNAFK----ILVVITDGeKF---GDPLGYEDVI---------PEADREGVIR-YV 284
Cdd:cd01470   81 dkTGTNTAaalKKVYERMALEKVRNKEAFNetrhVIILFTDG-KSnmgGSPLPTVDKIknlvyknnkSDNPREDYLDvYV 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767988556 285 IGVGDAFRSEksrqELNTIASKPPRD-HVFQVNNFEALK 322
Cdd:cd01470  160 FGVGDDVNKE----ELNDLASKKDNErHFFKLKDYEDLQ 194
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 149-306 8.17e-05

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 44.71  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 149 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLkKSKTLFSLMQYSEEFRihfTFKEFQNNPNPRSLVKPITQLL--GRTH 226
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDAR---VLLPPTPATDRAKILAAIDRLQagGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 227 TATGIRKVVRELfniTNGARKNAFKILVVITDGE---KFGDPLGYEDVIPEADREGVIRYVIGVGDAFRseksRQELNTI 303
Cdd:COG2304  168 LGAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDYN----EDLLERL 240


                 ...
gi 767988556 304 ASK 306
Cdd:COG2304  241 ADA 243
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 457-493 5.46e-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: 37.88  E-value: 5.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988556  457 FGASLCSVDVDSNGSTDLVlIGAPHYYEQtRGGQVSV 493
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 125-290 9.72e-04

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 41.59  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 125 LFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSiiphdfrrM--------KEFVSTVMEQLKKSKTlFSLMQYSEEF 196
Cdd:COG2425   95 LALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGS--------MagskeaaaKAAALALLRALRPNRR-FGVILFDTEV 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 197 RIHFTFKefqNNPNPRSLVKPI--TQLLGRTHTATGIRKVVRELfnitnGARKNAFKILVVITDGEkfgDPLGYEDVIPE 274
Cdd:COG2425  166 VEDLPLT---ADDGLEDAIEFLsgLFAGGGTDIAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLRE 234

                        170
                 ....*....|....*...
gi 767988556 275 AD-REGVIR-YVIGVGDA 290
Cdd:COG2425  235 VRaKESGVRlFTVAIGDA 252
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 151-296 1.07e-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: 40.39  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 151 IAFLIDGSGSIipHDFRRMKEFVSTVM---EQLKKSKTLFSLMQYS------EEFRIhFTFKEFQNNPNPRSLvKPITQL 221
Cdd:cd01454    3 VTLLLDLSGSM--RSDRRIDVAKKAAVllaEALEACGVPHAILGFTtdaggrERVRW-IKIKDFDESLHERAR-KRLAAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988556 222 LGRTHTATG--IRKVVRELfnitnGARKNAFKILVVITDGEKF------GDPLGYED---VIPEADREGVIRYVIGVG-D 289
Cdd:cd01454   79 SPGGNTRDGaaIRHAAERL-----LARPEKRKILLVISDGEPNdldyyeGNVFATEDalrAVIEARKLGIEVFGITIDrD 153


                 ....*..
gi 767988556 290 AFRSEKS 296
Cdd:cd01454  154 ATTVDKE 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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