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Conserved domains on  [gi|2273809782|ref|NP_001396393|]
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cochlin isoform 7 precursor [Mus musculus]

Protein Classification

LCCL and vWA_collagen domain-containing protein( domain architecture ID 10652018)

protein containing domains LCCL, vWFA, and vWA_collagen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 166-322 4.57e-76

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.


The actual alignment was detected with superfamily member cd01482:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 237.18  E-value: 4.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 245
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVAFVDK 322
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 344-505 1.02e-56

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: 186.66  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA 423
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVFGPIRDSP--NKNFLVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAFF 501
Cdd:cd01472    81 TGKALKYVRENLFTEASGSRegVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 2273809782 502 TREF 505
Cdd:cd01472   161 VADF 164
LCCL smart00603
LCCL domain;
32-114 1.08e-41

LCCL domain;


:

Pssm-ID: 128866  Cd Length: 85  Bit Score: 144.07  E-value: 1.08e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782   32 IPVTCFTRGLDIRKEKAD--VLCPGGCSLEEFSVFGNIVYASVSSICGAAVHRGVIGTSGGPVRVYSLPGRENYSSVDAN 109
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 2273809782  110 GIQSQ 114
Cdd:smart00603  81 GIQSE 85
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 166-322 4.57e-76

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: 237.18  E-value: 4.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 245
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVAFVDK 322
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 344-505 1.02e-56

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: 186.66  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA 423
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVFGPIRDSP--NKNFLVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAFF 501
Cdd:cd01472    81 TGKALKYVRENLFTEASGSRegVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 2273809782 502 TREF 505
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
345-514 1.33e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.21  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 345 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA- 423
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVF-GPIRDSPN-KNFLVIVTDGQSYD-DVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAF 500
Cdd:pfam00092  81 TGKALKYALENLFsSAAGARPGaPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 2273809782 501 FTREFTGLEPIVSD 514
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
167-311 7.27e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.81  E-value: 7.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 167 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 245
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
LCCL smart00603
LCCL domain;
32-114 1.08e-41

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 144.07  E-value: 1.08e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782   32 IPVTCFTRGLDIRKEKAD--VLCPGGCSLEEFSVFGNIVYASVSSICGAAVHRGVIGTSGGPVRVYSLPGRENYSSVDAN 109
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 2273809782  110 GIQSQ 114
Cdd:smart00603  81 GIQSE 85
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 345-505 5.66e-37

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: 134.50  E-value: 5.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  345 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRY-MSGGTA 423
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  424 TGDAIAFTVRNVFGPIRDS--PNKNFLVIVTDGQSYD---DVRGPAAAAHDAGITIFSVGV-AWAPLDDLRDMASKPKES 497
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGV 160


                   ....*...
gi 2273809782  498 HAFFTREF 505
Cdd:smart00327 161 YVFLPELL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-310 8.94e-34

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: 126.03  E-value: 8.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  167 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 245
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273809782  246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 310
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
34-123 4.34e-33

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 121.23  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  34 VTCFTRGLDIRK------EKADVLCPGGCSLEEFSVFGNIVYASVSSICGAAVHRGVIGTSGGPVRVYSLPGRENYSSVD 107
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 2273809782 108 ANGIQSQMLSRWSASF 123
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 343-491 7.28e-10

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.95  E-value: 7.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 343 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdyNTKENVLAVLANIRyMSG 420
Cdd:COG1240    92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273809782 421 GTATGDAIAfTVRNVFGPIRDSPNKnFLVIVTDGQSYDDVRGP---AAAAHDAGITIFSVGVAWAPLDD--LRDMA 491
Cdd:COG1240   165 GTPLGDALA-LALELLKRADPARRK-VIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA 238
PRK09193 PRK09193
indolepyruvate ferredoxin oxidoreductase; Validated
 441-527 2.35e-04

indolepyruvate ferredoxin oxidoreductase; Validated


Pssm-ID: 236404 [Multi-domain]  Cd Length: 1165  Bit Score: 44.05  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  441 DSPNKNFLvIVTDGQSYDDVRGP-------AAAAHDAGITIFSVGVAWaPLDdlrdmaskPKEshaffTREF-TGLEPIV 512
Cdd:PRK09193   279 DSPNARLG-IVAAGKAYLDVRQAlrdlgldEETAARLGIRLYKVGMVW-PLE--------PQG-----VRAFaEGLDEIL 343

                           90
                   ....*....|....*..
gi 2273809782  513 sdVI--RgicRDFLESQ 527
Cdd:PRK09193   344 --VVeeK---RQIIEYQ 355
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 166-322 4.57e-76

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: 237.18  E-value: 4.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 245
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVAFVDK 322
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 166-321 1.20e-60

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: 197.07  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 245
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVAFVD 321
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL 156
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 344-505 1.02e-56

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: 186.66  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA 423
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVFGPIRDSP--NKNFLVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAFF 501
Cdd:cd01472    81 TGKALKYVRENLFTEASGSRegVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 2273809782 502 TREF 505
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
345-514 1.33e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.21  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 345 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA- 423
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVF-GPIRDSPN-KNFLVIVTDGQSYD-DVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAF 500
Cdd:pfam00092  81 TGKALKYALENLFsSAAGARPGaPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 2273809782 501 FTREFTGLEPIVSD 514
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 344-500 1.10e-43

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: 152.06  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSG-GT 422
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 423 ATGDAIAFTVRNVFGPIRDSPN-KNFLVIVTDGQSYD--DVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHA 499
Cdd:cd01450    81 NTGKALQYALEQLFSESNARENvPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERHV 160


                  .
gi 2273809782 500 F 500
Cdd:cd01450   161 F 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 346-505 2.24e-43

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: 151.67  E-value: 2.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 346 IAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTATG 425
Cdd:cd01482     3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 426 DAIAFTVRNVFGPIRDSpNKNF---LVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESHAFFT 502
Cdd:cd01482    83 KALTHVREKNFTPDAGA-RPGVpkvVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                  ...
gi 2273809782 503 REF 505
Cdd:cd01482   162 ADF 164
VWA pfam00092
von Willebrand factor type A domain;
167-311 7.27e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.81  E-value: 7.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 167 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 245
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
LCCL smart00603
LCCL domain;
32-114 1.08e-41

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 144.07  E-value: 1.08e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782   32 IPVTCFTRGLDIRKEKAD--VLCPGGCSLEEFSVFGNIVYASVSSICGAAVHRGVIGTSGGPVRVYSLPGRENYSSVDAN 109
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 2273809782  110 GIQSQ 114
Cdd:smart00603  81 GIQSE 85
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 166-311 1.77e-39

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: 140.89  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-S 244
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273809782 245 NTGKALKHTAQKFFTaDTGVRKGIPKVVVVFIDGWPSD--DIEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:cd01450    81 NTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEEL 148
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 344-522 1.52e-38

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: 140.60  E-value: 1.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA 423
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVFGPI-----RDSPNKNFLVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPKESH 498
Cdd:cd01475    83 TGLAIQYAMNNAFSEAegarpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|....
gi 2273809782 499 AFFTREFTGLEPIVSDVIRGICRD 522
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVV 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 345-505 5.66e-37

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: 134.50  E-value: 5.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  345 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRY-MSGGTA 423
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  424 TGDAIAFTVRNVFGPIRDS--PNKNFLVIVTDGQSYD---DVRGPAAAAHDAGITIFSVGV-AWAPLDDLRDMASKPKES 497
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGV 160


                   ....*...
gi 2273809782  498 HAFFTREF 505
Cdd:smart00327 161 YVFLPELL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-310 8.94e-34

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: 126.03  E-value: 8.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  167 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 245
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273809782  246 TGKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 310
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
34-123 4.34e-33

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 121.23  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  34 VTCFTRGLDIRK------EKADVLCPGGCSLEEFSVFGNIVYASVSSICGAAVHRGVIGTSGGPVRVYSLPGRENYSSVD 107
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 2273809782 108 ANGIQSQMLSRWSASF 123
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 344-511 3.34e-32

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: 121.69  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMSGGTA 423
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNVFGPIRDS-PN-KNFLVIVTDGQSYDDVRGPAA--AAHDAGITIFSVGVAWA-----PLDDLRDMASKP 494
Cdd:cd01469    81 TATAIQYVVTELFSESNGArKDaTKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIASKP 160

                         170
                  ....*....|....*..
gi 2273809782 495 KESHAFFTREFTGLEPI 511
Cdd:cd01469   161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 166-319 1.37e-28

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: 111.26  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNS- 244
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273809782 245 NTGKALKHTAQKFFTADTGVR--KGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELgmvQDVAF 319
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAEL---QQIAF 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 344-500 1.67e-28

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: 111.12  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRY-MSGGT 422
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 423 ATGDAIAfTVRNVFGPIRDSPNKNFLVIVTDGQSYDDVRGPAAAAHDA---GITIFSVGV-AWAPLDDLRDMASKPKESH 498
Cdd:cd00198    81 NIGAALR-LALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELrklGITVYTIGIgDDANEDELKEIADKTTGGA 159


                  ..
gi 2273809782 499 AF 500
Cdd:cd00198   160 VF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 166-311 4.43e-27

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: 109.01  E-value: 4.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 245
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273809782 246 TGKALKHTAQKFFTADTGVRKG---IPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEEL 151
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 345-505 1.33e-24

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: 100.09  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 345 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRYMsGGTA- 423
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLR-GGSQl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 -TGDAIAFTVRNVF-----GPIRDSPNKnFLVIVTDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLRDMASKPkeS 497
Cdd:cd01481    81 nTGSALDYVVKNLFtksagSRIEEGVPQ-FLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--S 157


                  ....*...
gi 2273809782 498 HAFFTREF 505
Cdd:cd01481   158 FVFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 166-314 1.26e-22

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: 94.39  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRrFNLQKNFVGKVALMLGIGTEGPHVGLVQAS--EHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN 243
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273809782 244 SNTGKALKHTAQkFFTADTGVRKGIPKVVVVFIDGWPSDDIEEAGIVARE-FGVNVFIVSVAKPIP---EELGMV 314
Cdd:cd01476    80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDPGTvdtEELHSI 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 166-311 2.59e-21

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 90.70  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 166 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFR-GGNS 244
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 245 NTGKALKHTAQKFFTADtgvRKGIPKVVVVFIDGWPSDD---IEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:cd00198    81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDE 147
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 167-283 3.01e-21

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: 90.88  E-value: 3.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 167 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNT 246
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2273809782 247 GKALKHTAQKFFTADTGVRKGIPKVVVVFIDGWPSDD 283
Cdd:cd01469    82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDD 118
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 344-498 6.83e-21

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: 90.14  E-value: 6.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTF------EISDIGAKIAAVQFTYDQRTEFSFTDYNTKENVLAV-LANIR 416
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 417 YMSGGTATGDAIAFTVRNVfgpIRDSP--NKNFLVIVTDGQSY-DDVRGPAAAAHDA---GITIFSVGVAWAPLDDLRDM 490
Cdd:cd01480    83 YIGGGTFTDCALKYATEQL---LEGSHqkENKFLLVITDGHSDgSPDGGIEKAVNEAdhlGIKIFFVAVGSQNEEPLSRI 159


                  ....*...
gi 2273809782 491 ASKPKESH 498
Cdd:cd01480   160 ACDGKSAL 167
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 345-501 1.63e-16

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: 77.05  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 345 NIAFLIDGSSSVGDSnFRLMLEFVSNIAKTFEISDIGAKIAAVQFT--YDQRTEFSFTDYNTKENVLAVLANIRYMSGGT 422
Cdd:cd01476     2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 423 ATGDAI--AFTVRNVFGPIRDSPNKNfLVIVTDGQSYDDVRGPAAAAH-DAGITIFSVGVAWAPLDD---LRDMASKPKe 496
Cdd:cd01476    81 ATGAAIevALQQLDPSEGRREGIPKV-VVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDPGTVDteeLHSITGNED- 158


                  ....*
gi 2273809782 497 sHAFF 501
Cdd:cd01476   159 -HIFT 162
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 164-331 1.97e-13

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: 68.95  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 164 CKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGP------HVGLVQASEHPKIEF----YLKNFTSAKDvlfA 233
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAgflrDIRNYTSLKE---A 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 234 IKEVGFRGGNSNTGKALKHTAQKFFtadTGVRKGIPKVVVVFIDGWP--SDD--IEEAGIVAREFGVNVFIVSVAKpipe 309
Cdd:cd01480    78 VDNLEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSdgSPDggIEKAVNEADHLGIKIFFVAVGS---- 150

                         170       180
                  ....*....|....*....|..
gi 2273809782 310 elgmvqdvaFVDKPLVQKLCTH 331
Cdd:cd01480   151 ---------QNEEPLSRIACDG 163
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 344-478 2.66e-10

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: 59.71  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSN-FRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYNTKE-----NVLAVLANIRY 417
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNkdlalNAIRALLSLYY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273809782 418 MSGGTATGDAIAFTVRNVFGPIRDSPNKNFLVIV-TDGQSYDDVRGPAAAA--HDAG--ITIFSVG 478
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIImTDGIPDSKFRTLKEARklRERGviIAVLGVG 146
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 167-303 3.97e-10

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: 59.32  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 167 DIAFLIDGSFNIG-QRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLK--NFTSAKDVLFAI---KEVGFR 240
Cdd:cd01471     2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspNSTNKDLALNAIralLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273809782 241 GGNSNTGKALKHTAQKFFTAdTGVRKGIPKVVVVFIDGWPSDD---IEEAGiVAREFGVNVFIVSV 303
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrtLKEAR-KLRERGVIIAVLGV 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 343-491 7.28e-10

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.95  E-value: 7.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 343 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdyNTKENVLAVLANIRyMSG 420
Cdd:COG1240    92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273809782 421 GTATGDAIAfTVRNVFGPIRDSPNKnFLVIVTDGQSYDDVRGP---AAAAHDAGITIFSVGVAWAPLDD--LRDMA 491
Cdd:COG1240   165 GTPLGDALA-LALELLKRADPARRK-VIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA 238
VWA_2 pfam13519
von Willebrand factor type A domain;
168-275 1.64e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.99  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 168 IAFLIDGSF-----NIGQRRFNLQKNFVgkVALMLGIGTEgpHVGLVQASEHPKIEFYLKnfTSAKDVLFAIKEVGFRGG 242
Cdd:pfam13519   1 LVFVLDTSGsmrngDYGPTRLEAAKDAV--LALLKSLPGD--RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2273809782 243 NSNTGKALKHTAQKFFTAdtgvRKGIPKVVVVF 275
Cdd:pfam13519  75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 340-520 1.02e-05

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: 46.35  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 340 CYNSVNIAFLIDGSSSVGDSNFRLMlEFVSNIAKTFeiSDIGAKIAAVQFTYDQRTEFSFTDYNTKENV-LAVLANIrYM 418
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKV-TP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 419 SGGTATGDAIAFTVRNVFGPIRDSPNKNFLVI-VTDGQSYDDvrGPAAAAHDA------GITIFSVGVAWAPLDDLRDMA 491
Cdd:cd01474    77 SGQTYIHEGLENANEQIFNRNGGGRETVSVIIaLTDGQLLLN--GHKYPEHEAklsrklGAIVYCVGVTDFLKSQLINIA 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2273809782 492 SKPKesHAFFTRE-FTGLEPIVSDVIRGIC 520
Cdd:cd01474   155 DSKE--YVFPVTSgFQALSGIIESVVKKAC 182
VWA_2 pfam13519
von Willebrand factor type A domain;
346-430 3.82e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.66  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 346 IAFLIDGSSSVGD-----SNFRLMLEFVSNIAKTFEISdigaKIAAVQFTYDQRTEFSFTDynTKENVLAVLANIRYMSG 420
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90
                  ....*....|
gi 2273809782 421 GTATGDAIAF 430
Cdd:pfam13519  75 GTNLAAALQL 84
PRK09193 PRK09193
indolepyruvate ferredoxin oxidoreductase; Validated
 441-527 2.35e-04

indolepyruvate ferredoxin oxidoreductase; Validated


Pssm-ID: 236404 [Multi-domain]  Cd Length: 1165  Bit Score: 44.05  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782  441 DSPNKNFLvIVTDGQSYDDVRGP-------AAAAHDAGITIFSVGVAWaPLDdlrdmaskPKEshaffTREF-TGLEPIV 512
Cdd:PRK09193   279 DSPNARLG-IVAAGKAYLDVRQAlrdlgldEETAARLGIRLYKVGMVW-PLE--------PQG-----VRAFaEGLDEIL 343

                           90
                   ....*....|....*..
gi 2273809782  513 sdVI--RgicRDFLESQ 527
Cdd:PRK09193   344 --VVeeK---RQIIEYQ 355
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 344-500 4.09e-04

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: 41.10  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIgakIAAVQFTYDQRTEFSFTDYNTKENVLAVLANIRyMSGGTA 423
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDR---LAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 424 TGDAIAFTVRNV---FGPIRdspnKNFLVIVTDGQSY------DDVRGPAAAAHDAGITIFSVGVAWAPLDDL-RDMASK 493
Cdd:cd01465    77 GGAGIQLGYQEAqkhFVPGG----VNRILLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFGDNYNEDLmEAIADA 152


                  ....*..
gi 2273809782 494 PKESHAF 500
Cdd:cd01465   153 GNGNTAY 159
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 167-311 9.26e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 40.38  E-value: 9.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 167 DIAFLIDGSFNIGQRRFNLQ-KNFVGKVALMLGIGTEGPHVGLVQASEHPK--IEFYLKNFTSAKDVLFAIKEVG---FR 240
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKnsyRS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273809782 241 GGNSNTGKALKHtAQKFFTADTGVRKGIPKVVVVFIDG---WPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 311
Cdd:cd01473    82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTDGndtSASKkELQDISLLYKEENVKLLVVGVGAASENKL 155
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 344-479 1.29e-03

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: 40.01  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273809782 344 VNIAFLIDGSSSVGDSNFRLM--LEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFT-DYntkENVLAVLANIR-YMS 419
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTlDR---ESLKELLEDIKiGLA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273809782 420 G-GTATGDAIAFTVRNvfgpIRDSPNKN-FLVIVTDGQSYDDVRGPAAAAHDA---GITIFSVGV 479
Cdd:cd01467    80 GqGTAIGDAIGLAIKR----LKNSEAKErVIVLLTDGENNAGEIDPATAAELAknkGVRIYTIGV 140
PRK13029 PRK13029
indolepyruvate ferredoxin oxidoreductase family protein;
433-496 3.13e-03

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237278 [Multi-domain]  Cd Length: 1186  Bit Score: 40.54  E-value: 3.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273809782  433 RNVFgpirDSPNKNFLvIVTDGQSYDDVR--------GPAAAAHdAGITIFSVGVAWaPLD--DLRDMASKPKE 496
Cdd:PRK13029   278 RLVI----DGPNPRLG-IIAAGKAYLDVRqalrdlglDDATCAA-LGIRLLKVGCVW-PLDpqSVREFAQGLEE 344
 
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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