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Conserved domains on  [gi|2627930625|ref|WP_320908204|]
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MULTISPECIES: von Willebrand factor type A domain-containing protein [Bacteroides]

Protein Classification

vWA domain-containing protein( domain architecture ID 13939702)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 152-470 2.02e-107

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


:

Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 325.13  E-value: 2.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 152 EENGFKKVNENPLSTFSIDVDAASYSNMRRYLNRGELPPADAIRTEELINYFSYNYPQPTGkdpvkittEIGSCPWNKNH 231
Cdd:COG2304     1 AEAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTG--------RLAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 232 RLVRIGLKAKEIPTEKLPVSNLVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQ 311
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 312 KIREAIDELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLIEQERKSGVYLTVLGYGMg 391
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2627930625 392 NYKDSKMQILAEKGNGNHAYIDNLQEANRVLVNEFGAtmhtvakdvklqiefnpsqvqayrlIGYESRLLKDEDFNNDA 470
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSR-------------------------IGYENRALATEDFPLPY 284
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 428-613 2.85e-103

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


:

Pssm-ID: 432277  Cd Length: 182  Bit Score: 310.24  E-value: 2.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 428 ATMHTVAKDVKLQIEFNPSQVQAYRLIGYESRLLKDEDFNNDAKDAGEMGAGHTVTAFYEVVPAGVESNFvnkVDDLKYQ 507
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDL---VDPLKYQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 508 KKVKPalqPTTGSKELLTVKLRYKAPDEDISKKLELPLVD--NKGNNVSSDFRFAAAVAMFGQLLRDSDFKGDATYTQVI 585
Cdd:pfam12034  78 DAEAA---AAANSDELATVKLRYKLPDGDKSRLIEYPVADaaTAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVI 154

                         170       180
                  ....*....|....*....|....*...
gi 2627930625 586 AMVKTALDNDERGYRREFLRLVETADGL 613
Cdd:pfam12034 155 ELARGAKGEDPDGYRAEFIRLVEKAKSL 182
OMP_RagA_SusC super family cl37378
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
 29-128 8.83e-34

TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]


The actual alignment was detected with superfamily member TIGR04056:

Pssm-ID: 274948 [Multi-domain]  Cd Length: 981  Bit Score: 137.72  E-value: 8.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  29 TVKGKVTDAaDGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGEKLIFSYIGYETQTVKVTS-ERLNITMQANSQILEE 107
Cdd:TIGR04056   2 TVTGVVVDE-TGEPLIGASVVVKGTTNGTITDIDGNFSLKVPPGAVLVFSYIGYKTQEVKVKGqKNLNITLKEDTQELDE 80

                          90       100
                  ....*....|....*....|.
gi 2627930625 108 CVVVGYGMQKQVSMCGAVSNI 128
Cdd:TIGR04056  81 VVVVGYGTQKKKSLTGAVSTV 101
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 152-470 2.02e-107

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 325.13  E-value: 2.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 152 EENGFKKVNENPLSTFSIDVDAASYSNMRRYLNRGELPPADAIRTEELINYFSYNYPQPTGkdpvkittEIGSCPWNKNH 231
Cdd:COG2304     1 AEAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTG--------RLAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 232 RLVRIGLKAKEIPTEKLPVSNLVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQ 311
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 312 KIREAIDELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLIEQERKSGVYLTVLGYGMg 391
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2627930625 392 NYKDSKMQILAEKGNGNHAYIDNLQEANRVLVNEFGAtmhtvakdvklqiefnpsqvqayrlIGYESRLLKDEDFNNDA 470
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSR-------------------------IGYENRALATEDFPLPY 284
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 428-613 2.85e-103

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 310.24  E-value: 2.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 428 ATMHTVAKDVKLQIEFNPSQVQAYRLIGYESRLLKDEDFNNDAKDAGEMGAGHTVTAFYEVVPAGVESNFvnkVDDLKYQ 507
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDL---VDPLKYQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 508 KKVKPalqPTTGSKELLTVKLRYKAPDEDISKKLELPLVD--NKGNNVSSDFRFAAAVAMFGQLLRDSDFKGDATYTQVI 585
Cdd:pfam12034  78 DAEAA---AAANSDELATVKLRYKLPDGDKSRLIEYPVADaaTAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVI 154

                         170       180
                  ....*....|....*....|....*...
gi 2627930625 586 AMVKTALDNDERGYRREFLRLVETADGL 613
Cdd:pfam12034 155 ELARGAKGEDPDGYRAEFIRLVEKAKSL 182
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 251-422 1.30e-79

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: 248.73  E-value: 1.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 251 SNLVFLIDVSGSMYGPqRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDELTAGGSTAGGE 330
Cdd:cd01465     1 LNLVFVIDRSGSMDGP-KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 331 GIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLIEQERKSGVYLTVLGYGmGNYKDSKMQILAEKGNGNHA 410
Cdd:cd01465    80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158

                         170
                  ....*....|..
gi 2627930625 411 YIDNLQEANRVL 422
Cdd:cd01465   159 YIDNLAEARKVF 170
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 142-235 5.80e-61

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 197.37  E-value: 5.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 142 DMNTEEYKNIEENGFKKVNENPLSTFSIDVDAASYSNMRRYLNRGELPPADAIRTEELINYFSYNYPQPTGKDPVKITTE 221
Cdd:pfam12450   1 PFNTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFINQGQLPPADAVRIEEMINYFDYDYPQPTGDDPFSVTTE 80

                          90
                  ....*....|....
gi 2627930625 222 IGSCPWNKNHRLVR 235
Cdd:pfam12450  81 VAPCPWNPDHKLLR 94
OMP_RagA_SusC TIGR04056
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
 29-128 8.83e-34

TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 274948 [Multi-domain]  Cd Length: 981  Bit Score: 137.72  E-value: 8.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  29 TVKGKVTDAaDGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGEKLIFSYIGYETQTVKVTS-ERLNITMQANSQILEE 107
Cdd:TIGR04056   2 TVTGVVVDE-TGEPLIGASVVVKGTTNGTITDIDGNFSLKVPPGAVLVFSYIGYKTQEVKVKGqKNLNITLKEDTQELDE 80

                          90       100
                  ....*....|....*....|.
gi 2627930625 108 CVVVGYGMQKQVSMCGAVSNI 128
Cdd:TIGR04056  81 VVVVGYGTQKKKSLTGAVSTV 101
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 252-418 5.66e-21

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: 90.59  E-value: 5.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLR---DADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDEL--TAGGST 326
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsyKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  327 AGGEGIKLAYKI---AKKNFVKGGNNRIILCTDGDFNVGvssNEGLENLIEQERKSGVYLTVLGYGmGNYKDSKMQILAE 403
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVG-NDVDEEELKKLAS 155

                          170
                   ....*....|....*
gi 2627930625  404 KGNGNHAYIDNLQEA 418
Cdd:smart00327 156 APGGVYVFLPELLDL 170
CarbopepD_reg_2 pfam13715
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 30-110 6.48e-18

CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.


Pssm-ID: 433425 [Multi-domain]  Cd Length: 88  Bit Score: 78.79  E-value: 6.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  30 VKGKVTDAADGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGEK--LIFSYIGYETQTVKVTSER-----LNITMQANS 102
Cdd:pfam13715   1 ISGTVVDENTGEPLPGATVYVKGTTKGTVTDADGNFELKNLPAGTytLVVSFVGYKTQEKKVTVSNdntldVNFLLKEDA 80


                  ....*...
gi 2627930625 103 QILEECVV 110
Cdd:pfam13715  81 LLLDEVVV 88
PRK13685 PRK13685
hypothetical protein; Provisional
 254-361 3.14e-06

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 49.31  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 254 VFLIDVSGSMYG----PQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSgsDKQKIREAIDELTAGGSTAGG 329
Cdd:PRK13685   92 MLVIDVSQSMRAtdvePNRLAAAQEAAKQFADELTPGINLGLIAFAGTATVLVSPTT--NREATKNAIDKLQLADRTATG 169

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2627930625 330 EGIKLAYK-IAKKNFVKGGNN-----RIILCTDGDFNV 361
Cdd:PRK13685  170 EAIFTALQaIATVGAVIGGGDtpppaRIVLMSDGKETV 207
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 30-98 1.73e-05

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 43.28  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2627930625  30 VKGKVTDAaDGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGE-KLIFSYIGYETQTVKVTSE------RLNITM 98
Cdd:cd11308     2 IKGFVTDA-TGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTyNVTASAPGYQPVTKTVTVPnnfsatVVNFTL 76
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 256-428 1.77e-05

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 47.96  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 256 LIDVSGSMYGPQRLGLVQSSLKL-LVNNLRDADRVAIVVYSGSA---GERLPSTSGSDKQKIREAIDELTAGGsTAGGEG 331
Cdd:TIGR00868 310 VLDKSGSMTVEDRLKRMNQAAKLfLLQTVEKGSWVGMVTFDSAAyikNELIQITSSAERDALTANLPTAASGG-TSICSG 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 332 IKLAYKIAKKNFVKGGNNRIILCTDGDFNvgvssneGLENLIEQERKSGVYLTVLgyGMGNYKDSKMQILAEKGNGNHAY 411
Cdd:TIGR00868 389 LKAAFQVIKKSYQSTDGSEIVLLTDGEDN-------TISSCFEEVKQSGAIIHTI--ALGPSAAKELEELSDMTGGLRFY 459

                         170
                  ....*....|....*..
gi 2627930625 412 IdNLQEANRVLVNEFGA 428
Cdd:TIGR00868 460 A-SDQADNNGLIDAFGA 475
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 152-470 2.02e-107

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 325.13  E-value: 2.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 152 EENGFKKVNENPLSTFSIDVDAASYSNMRRYLNRGELPPADAIRTEELINYFSYNYPQPTGkdpvkittEIGSCPWNKNH 231
Cdd:COG2304     1 AEAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTG--------RLAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 232 RLVRIGLKAKEIPTEKLPVSNLVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQ 311
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 312 KIREAIDELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLIEQERKSGVYLTVLGYGMg 391
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2627930625 392 NYKDSKMQILAEKGNGNHAYIDNLQEANRVLVNEFGAtmhtvakdvklqiefnpsqvqayrlIGYESRLLKDEDFNNDA 470
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSR-------------------------IGYENRALATEDFPLPY 284
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 428-613 2.85e-103

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 310.24  E-value: 2.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 428 ATMHTVAKDVKLQIEFNPSQVQAYRLIGYESRLLKDEDFNNDAKDAGEMGAGHTVTAFYEVVPAGVESNFvnkVDDLKYQ 507
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVGSKSDL---VDPLKYQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 508 KKVKPalqPTTGSKELLTVKLRYKAPDEDISKKLELPLVD--NKGNNVSSDFRFAAAVAMFGQLLRDSDFKGDATYTQVI 585
Cdd:pfam12034  78 DAEAA---AAANSDELATVKLRYKLPDGDKSRLIEYPVADaaTAFAQASDDFRFAAAVAGFGMLLRGSEYKGDASYDDVI 154

                         170       180
                  ....*....|....*....|....*...
gi 2627930625 586 AMVKTALDNDERGYRREFLRLVETADGL 613
Cdd:pfam12034 155 ELARGAKGEDPDGYRAEFIRLVEKAKSL 182
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 251-422 1.30e-79

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: 248.73  E-value: 1.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 251 SNLVFLIDVSGSMYGPqRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDELTAGGSTAGGE 330
Cdd:cd01465     1 LNLVFVIDRSGSMDGP-KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 331 GIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLIEQERKSGVYLTVLGYGmGNYKDSKMQILAEKGNGNHA 410
Cdd:cd01465    80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158

                         170
                  ....*....|..
gi 2627930625 411 YIDNLQEANRVL 422
Cdd:cd01465   159 YIDNLAEARKVF 170
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 142-235 5.80e-61

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 197.37  E-value: 5.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 142 DMNTEEYKNIEENGFKKVNENPLSTFSIDVDAASYSNMRRYLNRGELPPADAIRTEELINYFSYNYPQPTGKDPVKITTE 221
Cdd:pfam12450   1 PFNTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFINQGQLPPADAVRIEEMINYFDYDYPQPTGDDPFSVTTE 80

                          90
                  ....*....|....
gi 2627930625 222 IGSCPWNKNHRLVR 235
Cdd:pfam12450  81 VAPCPWNPDHKLLR 94
OMP_RagA_SusC TIGR04056
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
 29-128 8.83e-34

TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 274948 [Multi-domain]  Cd Length: 981  Bit Score: 137.72  E-value: 8.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  29 TVKGKVTDAaDGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGEKLIFSYIGYETQTVKVTS-ERLNITMQANSQILEE 107
Cdd:TIGR04056   2 TVTGVVVDE-TGEPLIGASVVVKGTTNGTITDIDGNFSLKVPPGAVLVFSYIGYKTQEVKVKGqKNLNITLKEDTQELDE 80

                          90       100
                  ....*....|....*....|.
gi 2627930625 108 CVVVGYGMQKQVSMCGAVSNI 128
Cdd:TIGR04056  81 VVVVGYGTQKKKSLTGAVSTV 101
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 252-417 2.26e-33

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: 128.52  E-value: 2.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMYGPQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTsgSDKQKIREAIDELTAGGSTAGGEG 331
Cdd:COG1240    94 DVVLVVDASGSMAAENRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGGTPLGDA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 332 IKLAYKIAkKNFVKGGNNRIILCTDGDFNVGvssNEGLENLIEQERKSGVYLTVLGYGMGNYKDSKMQILAEKGNGNHAY 411
Cdd:COG1240   172 LALALELL-KRADPARRKVIVLLTDGRDNAG---RIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREIAEATGGRYFR 247


                  ....*.
gi 2627930625 412 IDNLQE 417
Cdd:COG1240   248 ADDLSE 253
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 252-411 8.56e-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: 106.50  E-value: 8.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLRDA---DRVAIVVYSGSAGERLPSTSGSDKQKIREAIDEL--TAGGST 326
Cdd:cd00198     2 DIVFLLDVSGSM-GGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALkkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 327 AGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNvgvSSNEGLENLIEQERKSGVYLTVLGYGMGNYKDsKMQILAEKGN 406
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPN---DGPELLAEAARELRKLGITVYTIGIGDDANED-ELKEIADKTT 156


                  ....*
gi 2627930625 407 GNHAY 411
Cdd:cd00198   157 GGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 252-418 5.66e-21

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: 90.59  E-value: 5.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLR---DADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDEL--TAGGST 326
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsyKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  327 AGGEGIKLAYKI---AKKNFVKGGNNRIILCTDGDFNVGvssNEGLENLIEQERKSGVYLTVLGYGmGNYKDSKMQILAE 403
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVG-NDVDEEELKKLAS 155

                          170
                   ....*....|....*
gi 2627930625  404 KGNGNHAYIDNLQEA 418
Cdd:smart00327 156 APGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
252-413 1.96e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 86.17  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNL---RDADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDELT--AGGST 326
Cdd:pfam00092   1 DIVFLLDGSGSI-GGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRylGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 327 AGGEGIKLAYKIAKK---NFVKGGNNRIILCTDGDFNVGvssneGLENLIEQERKSGVYLTVLGYgmGNYKDSKMQILAE 403
Cdd:pfam00092  80 NTGKALKYALENLFSsaaGARPGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGV--GNADDEELRKIAS 152

                         170
                  ....*....|
gi 2627930625 404 KGNGNHAYID 413
Cdd:pfam00092 153 EPGEGHVFTV 162
CarbopepD_reg_2 pfam13715
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 30-110 6.48e-18

CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.


Pssm-ID: 433425 [Multi-domain]  Cd Length: 88  Bit Score: 78.79  E-value: 6.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  30 VKGKVTDAADGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGEK--LIFSYIGYETQTVKVTSER-----LNITMQANS 102
Cdd:pfam13715   1 ISGTVVDENTGEPLPGATVYVKGTTKGTVTDADGNFELKNLPAGTytLVVSFVGYKTQEKKVTVSNdntldVNFLLKEDA 80


                  ....*...
gi 2627930625 103 QILEECVV 110
Cdd:pfam13715  81 LLLDEVVV 88
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 232-403 1.95e-15

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 76.64  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 232 RLVRIGLKAKEIPTEKLPVSNLVFLIDVSGSMYGPqRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQ 311
Cdd:COG2425   100 LAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGS-KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 312 KIREAIDELTAGGSTAGGEGIKLAYKIAKKnfVKGGNNRIILCTDGDfnVGVSSNEGLENLieQERKSGVYLTVLgyGMG 391
Cdd:COG2425   179 DAIEFLSGLFAGGGTDIAPALRAALELLEE--PDYRNADIVLITDGE--AGVSPEELLREV--RAKESGVRLFTV--AIG 250

                         170
                  ....*....|...
gi 2627930625 392 NYKDSK-MQILAE 403
Cdd:COG2425   251 DAGNPGlLEALAD 263
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 253-412 3.57e-15

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 73.19  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 253 LVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLP--STSGSDKQKIREAIDELTAGGSTAGGE 330
Cdd:cd01466     3 LVAVLDVSGSMAG-DKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPlrRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 331 GIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSsneglenlieQERKSGVYLTVLGYGMGNYKDS-KMQILAEKGNGNH 409
Cdd:cd01466    82 GLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAV----------VLRADNAPIPIHTFGLGASHDPaLLAFIAEITGGTF 151


                  ...
gi 2627930625 410 AYI 412
Cdd:cd01466   152 SYV 154
VWA_2 pfam13519
von Willebrand factor type A domain;
253-353 4.09e-15

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 71.17  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 253 LVFLIDVSGSM----YGPQRLGLVQSSLKLLVNNLRDaDRVAIVVYSGSAGERLPSTsgSDKQKIREAIDELTA-GGSTA 327
Cdd:pfam13519   1 LVFVLDTSGSMrngdYGPTRLEAAKDAVLALLKSLPG-DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPkGGGTN 77

                          90       100
                  ....*....|....*....|....*.
gi 2627930625 328 GGEGIKLAYKIAKKNfVKGGNNRIIL 353
Cdd:pfam13519  78 LAAALQLARAALKHR-RKNQPRRIVL 102
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 252-411 1.11e-11

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: 63.46  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLR---DADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDELT--AGGST 326
Cdd:cd01450     2 DIVFLLDGSESV-GPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKylGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 327 AggegIKLAYKIAKKNFVKGGNNR------IILCTDGDFNVGvssnEGLENLIEQERKSGVYLTVLGYGMGNykDSKMQI 400
Cdd:cd01450    81 N----TGKALQYALEQLFSESNARenvpkvIIVLTDGRSDDG----GDPKEAAAKLKDEGIKVFVVGVGPAD--EEELRE 150

                         170
                  ....*....|.
gi 2627930625 401 LAEKGNGNHAY 411
Cdd:cd01450   151 IASCPSERHVF 161
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 252-363 4.49e-11

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 61.96  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSM-----YGPQRLGLVQSSLKLLVNNlRDADRVAIVVYSGSAGERLPSTSG--SDKQKIREaIDELTAGG 324
Cdd:cd01467     4 DIMIALDVSGSMlaqdfVKPSRLEAAKEVLSDFIDR-RENDRIGLVVFAGAAFTQAPLTLDreSLKELLED-IKIGLAGQ 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2627930625 325 STAGGEGIKLAYKIAKKNfvKGGNNRIILCTDGDFNVGV 363
Cdd:cd01467    82 GTAIGDAIGLAIKRLKNS--EAKERVIVLLTDGENNAGE 118
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 252-419 2.15e-10

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 59.92  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMYGPqRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSGSDKQKIREAID---ELTAGGSTAG 328
Cdd:cd01461     4 EVVFVIDTSGSMSGT-KIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEyvnRLQALGGTNM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 329 GEGIKLAYKiaKKNFVKGGNNRIILCTDGDfnvgVSSNEGLENLIEQERKSGVYLTVLgyGMGNYKDSK-MQILAEKGNG 407
Cdd:cd01461    83 NDALEAALE--LLNSSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTF--GIGSDVNTYlLERLAREGRG 154

                         170
                  ....*....|..
gi 2627930625 408 NHAYIDNLQEAN 419
Cdd:cd01461   155 IARRIYETDDIE 166
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
244-403 1.28e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.01  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 244 PTEKLPVsnlVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDAD------RVAIVVYSGSAGERLPSTSGSDKQkireaI 317
Cdd:COG4245     2 PMRRLPV---YLLLDTSGSMSG-EPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAKVLLPLTDLEDFQ-----P 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 318 DELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNR-------IILCTDG---DFNVgvssNEGLENLIEQERKSGVYLTVLG 387
Cdd:COG4245    73 PDLSASGGTPLGAALELLLDLIERRVQKYTAEGkgdwrpvVFLITDGeptDSDW----EAALQRLKDGEAAKKANIFAIG 148

                         170
                  ....*....|....*.
gi 2627930625 388 YGmgnyKDSKMQILAE 403
Cdd:COG4245   149 VG----PDADTEVLKQ 160
VWA_3 pfam13768
von Willebrand factor type A domain;
251-408 1.71e-09

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 56.64  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 251 SNLVFLIDVSGSMYGPQRlgLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLP---STSGSDKQKIREAIDELTAggsTA 327
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPK--LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPgwrVVSPRSLQEAFQFIKTLQP---PL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 328 GGEGIKLAYKIAKKNFVKGGNNR-IILCTDGdfnvgvSSNEGLENLIEQERKSGVYLTVLGYGMGNYKDS-KMQILAEKG 405
Cdd:pfam13768  76 GGSDLLGALKEAVRAPASPGYIRhVLLLTDG------SPMQGETRVSDLISRAPGKIRFFAYGLGASISApMLQLLAEAS 149


                  ...
gi 2627930625 406 NGN 408
Cdd:pfam13768 150 NGT 152
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 240-411 4.63e-09

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


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 56.67  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 240 AKEIPTEKLPVSNLVFLIDVSGSMY-----GPQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSA------------GERL 302
Cdd:cd01456    10 LEPVETEPQLPPNVAIVLDNSGSMRevdggGETRLDNAKAALDETANALPDGTRLGLWTFSGDGdnpldvrvlvpkGCLT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 303 PSTSGSDKQKIREAIDELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNVGVSSNEGLENLI-EQERKSGV 381
Cdd:cd01456    90 APVNGFPSAQRSALDAALNSLQTPTGWTPLAAALAEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAkRRTPAPPI 169

                         170       180       190
                  ....*....|....*....|....*....|
gi 2627930625 382 YLTVLGYGMGNYKDSKMQIlAEKGNGNHAY 411
Cdd:cd01456   170 KVNVIDFGGDADRAELEAI-AEATGGTYAY 198
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
29-98 2.79e-08

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 51.13  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625  29 TVKGKVTDAaDGFGIIGCTVLVK----GTTRSTITNVDGEYTIRA-NKGE-KLIFSYIGYETQTVKV------TSERLNI 96
Cdd:pfam13620   1 TISGTVTDP-SGAPVPGATVTVTntdtGTVRTTTTDADGRYRFPGlPPGTyTVTVSAPGFKTATRTGvtvtagQTTTLDV 79


                  ..
gi 2627930625  97 TM 98
Cdd:pfam13620  80 TL 81
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 251-413 5.96e-08

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: 52.40  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 251 SNLVFLIDVSGSMygpqrLGLVQSSLKLLVNNLR------DADRVAIVVYSGSAGERLPSTSGS--DKQKIREAIDELTA 322
Cdd:cd01476     1 LDLLFVLDSSGSV-----RGKFEKYKKYIERIVEgleigpTATRVALITYSGRGRQRVRFNLPKhnDGEELLEKVDNLRF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 323 -GGSTAGGEGIKLAYKI------AKKNFVKggnnRIILCTDGdfnvgvSSNEGLENLIEQERkSGVYLTVLGYGMGNYKD 395
Cdd:cd01476    76 iGGTTATGAAIEVALQQldpsegRREGIPK----VVVVLTDG------RSHDDPEKQARILR-AVPNIETFAVGTGDPGT 144

                         170
                  ....*....|....*....
gi 2627930625 396 SKMQILAE-KGNGNHAYID 413
Cdd:cd01476   145 VDTEELHSiTGNEDHIFTD 163
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 252-391 1.03e-07

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: 52.39  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMYGPQRLGLVQSSLKLLVNNL---RDADRVAIVVYSGSAGE--RLPSTSGSDKQKIREAIDELTAGGST 326
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLnisPDEINLYLVTFSTNAKEliRLSSPNSTNKDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2627930625 327 AGGEGIKLAYKIAKKNFVKGGNNR------IILCTDGDFNvgvsSNEGLENLIEQERKSGVYLTVLGYGMG 391
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRenapqlVIIMTDGIPD----SKFRTLKEARKLRERGVIIAVLGVGQG 148
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 252-362 2.02e-07

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 51.51  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLV-FLIDVSGSMYGPQRLGLVQSSLKLLvnnLRDA----DRVAIVVYSGSAGE-RLPSTSGSDKQKIReaIDELTAGGS 325
Cdd:cd01451     1 NLViFVVDASGSMAARHRMAAAKGAVLSL---LRDAyqrrDKVALIAFRGTEAEvLLPPTRSVELAKRR--LARLPTGGG 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2627930625 326 TAGGEGIKLAYKIAKKNFVKGGNNR-IILCTDGDFNVG 362
Cdd:cd01451    76 TPLAAGLLAAYELAAEQARDPGQRPlIVVITDGRANVG 113
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 252-415 1.28e-06

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 49.31  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLRDADRVAIVVYS-------GSAGERLPSTSGSDKQKIREAIDELTAGG 324
Cdd:cd01463    15 DIVILLDVSGSMTG-QRLHLAKQTVSSILDTLSDNDFFNIITFSnevnpvvPCFNDTLVQATTSNKKVLKEALDMLEAKG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 325 STAGGEGIKLAYKIAKKNFVKGGNNR-------IILCTDGdfnvGVSSNEGLENLIEQERKSGVYLTVLGYGMG--NYKD 395
Cdd:cd01463    94 IANYTKALEFAFSLLLKNLQSNHSGSrsqcnqaIMLITDG----VPENYKEIFDKYNWDKNSEIPVRVFTYLIGreVTDR 169

                         170       180
                  ....*....|....*....|
gi 2627930625 396 SKMQILAEKGNGNHAYIDNL 415
Cdd:cd01463   170 REIQWMACENKGYYSHIQSL 189
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 252-411 1.57e-06

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: 48.38  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLRDAD---RVAIVVYSGSAGERLPSTSGSDKQKIREAIDELT-AGGSTA 327
Cdd:cd01472     2 DIVFLVDGSESI-GLSNFNLVKDFVKRVVERLDIGPdgvRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRyIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 328 GGEGIKlayKIAKKNFVK------GGNNRIILCTDGDfnvgvSSNEGLENLIeQERKSGVylTVLGYGMGNYKDSKMQIL 401
Cdd:cd01472    81 TGKALK---YVRENLFTEasgsreGVPKVLVVITDGK-----SQDDVEEPAV-ELKQAGI--EVFAVGVKNADEEELKQI 149

                         170
                  ....*....|
gi 2627930625 402 AEKGNGNHAY 411
Cdd:cd01472   150 ASDPKELYVF 159
PRK13685 PRK13685
hypothetical protein; Provisional
 254-361 3.14e-06

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 49.31  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 254 VFLIDVSGSMYG----PQRLGLVQSSLKLLVNNLRDADRVAIVVYSGSAGERLPSTSgsDKQKIREAIDELTAGGSTAGG 329
Cdd:PRK13685   92 MLVIDVSQSMRAtdvePNRLAAAQEAAKQFADELTPGINLGLIAFAGTATVLVSPTT--NREATKNAIDKLQLADRTATG 169

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2627930625 330 EGIKLAYK-IAKKNFVKGGNN-----RIILCTDGDFNV 361
Cdd:PRK13685  170 EAIFTALQaIATVGAVIGGGDtpppaRIVLMSDGKETV 207
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 245-357 4.85e-06

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 47.33  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 245 TEKLPVsnlVFLIDVSGSMYGpQRLGLVQSSLKLLVNNLR------DADRVAIVVYSGSAGERLPSTSGSDKQkireaID 318
Cdd:cd01464     1 MRRLPI---YLLLDTSGSMAG-EPIEALNQGLQMLQSELRqdpyalESVEISVITFDSAARVIVPLTPLESFQ-----PP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2627930625 319 ELTAGGSTAGGEGIKLAYKIAKKNFVKGGNNR-------IILCTDG 357
Cdd:cd01464    72 RLTASGGTSMGAALELALDCIDRRVQRYRADQkgdwrpwVFLLTDG 117
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 30-98 1.73e-05

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 43.28  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2627930625  30 VKGKVTDAaDGFGIIGCTVLVKGTTRSTITNVDGEYTIRANKGE-KLIFSYIGYETQTVKVTSE------RLNITM 98
Cdd:cd11308     2 IKGFVTDA-TGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTyNVTASAPGYQPVTKTVTVPnnfsatVVNFTL 76
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 256-428 1.77e-05

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 47.96  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 256 LIDVSGSMYGPQRLGLVQSSLKL-LVNNLRDADRVAIVVYSGSA---GERLPSTSGSDKQKIREAIDELTAGGsTAGGEG 331
Cdd:TIGR00868 310 VLDKSGSMTVEDRLKRMNQAAKLfLLQTVEKGSWVGMVTFDSAAyikNELIQITSSAERDALTANLPTAASGG-TSICSG 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 332 IKLAYKIAKKNFVKGGNNRIILCTDGDFNvgvssneGLENLIEQERKSGVYLTVLgyGMGNYKDSKMQILAEKGNGNHAY 411
Cdd:TIGR00868 389 LKAAFQVIKKSYQSTDGSEIVLLTDGEDN-------TISSCFEEVKQSGAIIHTI--ALGPSAAKELEELSDMTGGLRFY 459

                         170
                  ....*....|....*..
gi 2627930625 412 IdNLQEANRVLVNEFGA 428
Cdd:TIGR00868 460 A-SDQADNNGLIDAFGA 475
bchD PRK13406
magnesium chelatase subunit D; Provisional
 253-362 5.44e-04

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 43.09  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 253 LVFLIDVSGS--MygpQRLGLVQSSLKLLvnnLRDA----DRVAIVVYSGSAGER-LPSTSGSDKQKIREAidELTAGGS 325
Cdd:PRK13406  404 TIFVVDASGSaaL---HRLAEAKGAVELL---LAEAyvrrDQVALVAFRGRGAELlLPPTRSLVRAKRSLA--GLPGGGG 475

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2627930625 326 TAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGDFNVG 362
Cdd:PRK13406  476 TPLAAGLDAAAALALQVRRKGMTPTVVLLTDGRANIA 512
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 248-381 5.93e-04

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: 41.22  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 248 LPVsNLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLRDAD---------RVAIVVYSGSAG-ERLPSTSGSDKQKIREAI 317
Cdd:cd01480     1 GPV-DITFVLDSSESV-GLQNFDITKNFVKRVAERFLKDYyrkdpagswRVGVVQYSDQQEvEAGFLRDIRNYTSLKEAV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2627930625 318 DELT-AGGSTAGGEGIKLAYKIAKKNFVKGGNNRIILCTDGdfNVGVSSNEGLENLIEQERKSGV 381
Cdd:cd01480    79 DNLEyIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDG--HSDGSPDGGIEKAVNEADHLGI 141
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 252-357 4.82e-03

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: 38.65  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMYG--PQRLGLVQSSLKLLVN-NLRdadrVAIVVYSGSAGERLPSTSgsDKQKIR---EAIDELTAGGS 325
Cdd:cd01474     6 DLYFVLDKSGSVAAnwIEIYDFVEQLVDRFNSpGLR----FSFITFSTRATKILPLTD--DSSAIIkglEVLKKVTPSGQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2627930625 326 TAGGEGIKLA-YKIAKKNfvKGG---NNRIILCTDG 357
Cdd:cd01474    80 TYIHEGLENAnEQIFNRN--GGGretVSVIIALTDG 113
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 253-357 4.85e-03

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 38.04  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 253 LVFLIDVSGSMyGPQRLGLVQSSLKLLVNNL---RDADRVAIVVYSGSAGERLPSTSGSDKQKIREAIDELT-AGGSTAG 328
Cdd:cd01482     3 IVFLVDGSWSI-GRSNFNLVRSFLSSVVEAFeigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPyKGGNTRT 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2627930625 329 GEGIKLaykIAKKNFVKGGNNR------IILCTDG 357
Cdd:cd01482    82 GKALTH---VREKNFTPDAGARpgvpkvVILITDG 113
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 252-417 4.99e-03

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: 38.81  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMyGPQRLGLVQSSLKLLVNNLRDAD---RVAIVVYSGSAGERLpSTSGSDKQKIREAIDELTA------ 322
Cdd:cd01470     2 NIYIALDASDSI-GEEDFDEAKNAIKTLIEKISSYEvspRYEIISYASDPKEIV-SIRDFNSNDADDVIKRLEDfnyddh 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 323 GGSTagGEGIKLAYK-------IAKKNFVKGGN---NRIILCTDGDFNVGVSSNEGLE---NLIEQERKSGV----YLTV 385
Cdd:cd01470    80 GDKT--GTNTAAALKkvyermaLEKVRNKEAFNetrHVIILFTDGKSNMGGSPLPTVDkikNLVYKNNKSDNpredYLDV 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2627930625 386 LGYGMG-NYKDSKMQILA-EKGNGNHAYI----DNLQE 417
Cdd:cd01470   158 YVFGVGdDVNKEELNDLAsKKDNERHFFKlkdyEDLQE 195
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
252-356 9.04e-03

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 38.65  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627930625 252 NLVFLIDVSGSMY----GPQRLGLVQSSLKLLVNN-LRDADRVAIVVYSGSAGERLPSTSGSDK-QKIREAIDELTAGGS 325
Cdd:COG1721   149 TVVLLLDTSASMRfgsgGPSKLDLAVEAAASLAYLaLRQGDRVGLLTFGDRVRRYLPPRRGRRHlLRLLEALARLEPAGE 228

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2627930625 326 TAGGEGIKLAYKIAKKnfvkggNNRIILCTD 356
Cdd:COG1721   229 TDLAAALRRLARRLPR------RSLVVLISD 253
 
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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