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Conserved domains on  [gi|261878614|ref|NP_001159906|]
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inter-alpha-trypsin inhibitor heavy chain H1 isoform b [Homo sapiens]

Protein Classification

vWA_interalpha_trypsin_inhibitor and ITI_HC_C domain-containing protein( domain architecture ID 10106957)

protein containing domains VIT_2, vWA_interalpha_trypsin_inhibitor, and ITI_HC_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 563-750 4.79e-93

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


:

Pssm-ID: 461981  Cd Length: 189  Bit Score: 288.33  E-value: 4.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  563 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  641 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 720
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878614  721 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 750
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 3.67e-67

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: 219.39  E-value: 3.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 147 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 227 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878614 307 MENNGRAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT_2 super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-24 4.97e-07

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


The actual alignment was detected with superfamily member smart00609:

Pssm-ID: 470654 [Multi-domain]  Cd Length: 130  Bit Score: 49.28  E-value: 4.97e-07
                           10        20
                   ....*....|....*....|....
gi 261878614     1 MEQFTIHLTVNPQSKVTFQLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 563-750 4.79e-93

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 288.33  E-value: 4.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  563 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  641 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 720
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878614  721 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 750
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 3.67e-67

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: 219.39  E-value: 3.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 147 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 227 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878614 307 MENNGRAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 140-349 1.01e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 134.07  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 140 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFV 217
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 218 RGFSLDEATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNV 297
Cdd:COG2304  158 DRLQAGGGTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDY 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 261878614 298 DFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 349
Cdd:COG2304  233 NEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-327 1.43e-24

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: 100.99  E-value: 1.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614   150 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 224
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614   225 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 304
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 261878614   305 MSMENNGRAQRIYEDHDATQQLQ 327
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
150-332 2.41e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.95  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  150 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 225
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  226 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 305
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 261878614  306 SMENNgrAQRIYEDHDATqQLQGFYSQ 332
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 174
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-24 4.97e-07

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 49.28  E-value: 4.97e-07
                           10        20
                   ....*....|....*....|....
gi 261878614     1 MEQFTIHLTVNPQSKVTFQLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 141-293 2.12e-03

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 40.75  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  141 PQNLTNMNKN------VVFVIDISGSMRgQKVKQTKEALLKIL-GDMQPGDYFDLVLFGTR---VQSWKGSLVQaseanL 210
Cdd:TIGR03436  40 PQTIASFRREtdlpltVGLVIDTSGSMR-NDLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrlLQDFTSDPRL-----L 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  211 QAAQDFVR--GFSLDEATNLNGGLLRGIEILNQVQ-ESLPELSNHAS------ILIMLTDGDPTEGVTDRSQIlknVRNA 281
Cdd:TIGR03436 114 EAALNRLKppLRTDYNSSGAFVRDGGGTALYDAITlAALEQLANALAgipgrkALIVISDGGDNRSRDTLERA---IDAA 190

                         170
                  ....*....|..
gi 261878614  282 IRGRFPLYNLGF 293
Cdd:TIGR03436 191 QRADVAIYSIDA 202
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 563-750 4.79e-93

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 288.33  E-value: 4.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  563 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  641 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 720
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878614  721 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 750
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 3.67e-67

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: 219.39  E-value: 3.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 147 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 227 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878614 307 MENNGRAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 140-349 1.01e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 134.07  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 140 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFV 217
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 218 RGFSLDEATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNV 297
Cdd:COG2304  158 DRLQAGGGTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDY 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 261878614 298 DFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 349
Cdd:COG2304  233 NEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-327 1.43e-24

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: 100.99  E-value: 1.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614   150 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 224
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614   225 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 304
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 261878614   305 MSMENNGRAQRIYEDHDATQQLQ 327
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 140-306 2.59e-22

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 97.44  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 140 APQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSwkgSLVQASEANLQAAQDFVRG 219
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 220 FSLDEATNLNGGLLRGIEILNQVQeslpelsNHASILIMLTDGDPTEgvtDRSQILKNVRNAiRGRFPLYNLGFGHNVDF 299
Cdd:COG2425  187 LFAGGGTDIAPALRAALELLEEPD-------YRNADIVLITDGEAGV---SPEELLREVRAK-ESGVRLFTVAIGDAGNP 255


                 ....*..
gi 261878614 300 NFLEVMS 306
Cdd:COG2425  256 GLLEALA 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 150-334 3.51e-22

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: 96.93  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 150 NVVFVIDISGSMRGQ-KVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASEANLQAAQDFVRGFSLDEATNL 228
Cdd:COG1240   94 DVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-----VLLPLTRDREALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 229 NGGLLRGIEILNQVQESLPelsnhaSILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHN-VDFNFLEVMSM 307
Cdd:COG1240  169 GDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLREIAE 239

                        170       180
                 ....*....|....*....|....*..
gi 261878614 308 ENNGRAQRIyedhDATQQLQGFYSQVA 334
Cdd:COG1240  240 ATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
150-332 2.41e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.95  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  150 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 225
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  226 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 305
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 261878614  306 SMENNgrAQRIYEDHDATqQLQGFYSQ 332
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-311 9.14e-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: 89.93  E-value: 9.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 150 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRgFSLDEAT 226
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-KGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 227 NLNGGLLRGIEILNQvqeslPELSNHASILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHNVDFNFLEVMS 306
Cdd:cd00198   81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 261878614 307 MENNG 311
Cdd:cd00198  153 DKTTG 157
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 150-316 1.20e-16

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: 78.08  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 150 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVqswkGSLVQASEANLQAA-QDFVRGFSLDEATNL 228
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 229 NGGLLRGIEILnqVQESLPELSNHasiLIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMSME 308
Cdd:cd01465   78 GAGIQLGYQEA--QKHFVPGGVNR---ILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ....*...
gi 261878614 309 NNGRAQRI 316
Cdd:cd01465  153 GNGNTAYI 160
VWA_3 pfam13768
von Willebrand factor type A domain;
149-314 1.56e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.96  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  149 KNVVFVIDISGSMRGQKVKQtKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDE-ATN 227
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLgGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  228 LNGGLLRGIEilnqvQESLPELSNHasiLIMLTDGDPTEGVTDrsqILKNVRNAiRGRFPLYNLGFGHNVDFNFLEVMSM 307
Cdd:pfam13768  80 LLGALKEAVR-----APASPGYIRH---VLLLTDGSPMQGETR---VSDLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 261878614  308 ENNGRAQ 314
Cdd:pfam13768 148 ASNGTYE 154
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
150-303 2.96e-11

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 63.41  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 150 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQP------GDYFDLVLFGTRVQsWKGSLVQASEanLQAAQDFVRGfsld 223
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQdpyaleTVEVSVITFDGEAK-VLLPLTDLED--FQPPDLSASG---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 224 eATNLNGGLLRGIEIL-NQVQESLPE-LSNHASILIMLTDGDPTEgvTDRSQILKNVRNAIRGRFP-LYNLGFGHNVDFN 300
Cdd:COG4245   80 -GTPLGAALELLLDLIeRRVQKYTAEgKGDWRPVVFLITDGEPTD--SDWEAALQRLKDGEAAKKAnIFAIGVGPDADTE 156


                 ...
gi 261878614 301 FLE 303
Cdd:COG4245  157 VLK 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 151-311 4.78e-09

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: 55.86  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 151 VVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTrvQSWKGS-LVQASEANLQAAQDFVRGFSLDEATNLN 229
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFST--SAKRLSpLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 230 GGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTdrsqilknVRNAIRGRFPLYNLGFGHNVDFNFLEVMSMEN 309
Cdd:cd01466   81 GGLKKALKVLGDRRQ-----KNPVASIMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIAEIT 147


                 ..
gi 261878614 310 NG 311
Cdd:cd01466  148 GG 149
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 149-334 5.57e-08

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: 53.55  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 149 KNVVFVIDISGSMRGQK---VKQTKEALLKILGDmqpGDYFDLVLFGTRVQS----WKGSLVQASEANLQAAQDFVRGFS 221
Cdd:cd01463   14 KDIVILLDVSGSMTGQRlhlAKQTVSSILDTLSD---NDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 222 LDEATNLNGGLLRGIEILNQVQESLpeLSNHASI---LIMLTdgdpTEGVTDR-SQILK--NVRNAIRGRFPLYNLGFG- 294
Cdd:cd01463   91 AKGIANYTKALEFAFSLLLKNLQSN--HSGSRSQcnqAIMLI----TDGVPENyKEIFDkyNWDKNSEIPVRVFTYLIGr 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 261878614 295 HNVDFNFLEVMSMENngraqriyedhdatqqlQGFYSQVA 334
Cdd:cd01463  165 EVTDRREIQWMACEN-----------------KGYYSHIQ 187
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-24 4.97e-07

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 49.28  E-value: 4.97e-07
                           10        20
                   ....*....|....*....|....
gi 261878614     1 MEQFTIHLTVNPQSKVTFQLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
VWA_2 pfam13519
von Willebrand factor type A domain;
151-259 7.29e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 45.36  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  151 VVFVIDISGSMRGQKVKQT-----KEALLKILGDMqPGDYFDLVLFGTRVQ---SWKGSLVQASEAnLQAAQDFVRGfsl 222
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSL-PGDRVGLVTFGDGPEvliPLTKDRAKILRA-LRRLEPKGGG--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 261878614  223 deaTNLNGGLLRGIEILNQVQeslpelSNHASILIML 259
Cdd:pfam13519  76 ---TNLAAALQLARAALKHRR------KNQPRRIVLI 103
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-277 1.75e-04

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: 42.66  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 150 NVVFVIDISGSMRGQKVKQTKEALLKILgdmqpgDYFDLVLFGTRVqswkgSLVQAS-----EANLQAAQDF------VR 218
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLV------EKLDIGPDKTRV-----GLVQYSddvrvEFSLNDYKSKddllkaVK 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261878614 219 GFSLD--EATNLNGGLLRGIEILNQVQESlpeLSNHASILIMLTDGDPTEG--VTDRSQILKN 277
Cdd:cd01450   71 NLKYLggGGTNTGKALQYALEQLFSESNA---RENVPKVIIVLTDGRSDDGgdPKEAAAKLKD 130
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 151-269 1.34e-03

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: 40.34  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 151 VVFVIDISGSMRG-QKVKQTKEALLKILGD---------MQP--GDYFDLVLFGTRvqswkgSLVQASeanlQAAQDFVR 218
Cdd:cd01451    3 VIFVVDASGSMAArHRMAAAKGAVLSLLRDayqrrdkvaLIAfrGTEAEVLLPPTR------SVELAK----RRLARLPT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 261878614 219 GfsldEATNLNGGLLRGIEILNQVQESLPElsnhASILIMLTDG------DPTEGVT 269
Cdd:cd01451   73 G----GGTPLAAGLLAAYELAAEQARDPGQ----RPLIVVITDGranvgpDPTADRA 121
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 141-293 2.12e-03

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 40.75  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  141 PQNLTNMNKN------VVFVIDISGSMRgQKVKQTKEALLKIL-GDMQPGDYFDLVLFGTR---VQSWKGSLVQaseanL 210
Cdd:TIGR03436  40 PQTIASFRREtdlpltVGLVIDTSGSMR-NDLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrlLQDFTSDPRL-----L 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614  211 QAAQDFVR--GFSLDEATNLNGGLLRGIEILNQVQ-ESLPELSNHAS------ILIMLTDGDPTEGVTDRSQIlknVRNA 281
Cdd:TIGR03436 114 EAALNRLKppLRTDYNSSGAFVRDGGGTALYDAITlAALEQLANALAgipgrkALIVISDGGDNRSRDTLERA---IDAA 190

                         170
                  ....*....|..
gi 261878614  282 IRGRFPLYNLGF 293
Cdd:TIGR03436 191 QRADVAIYSIDA 202
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 149-280 9.30e-03

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: 37.76  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878614 149 KNVVFVIDISGSMRGQKVKQTK--EALLKILGDMQPGDYFDLVLFGTRVQswkgslvQASEANLQAAQD---FVRGFSLD 223
Cdd:cd01476    1 LDLLFVLDSSGSVRGKFEKYKKyiERIVEGLEIGPTATRVALITYSGRGR-------QRVRFNLPKHNDgeeLLEKVDNL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261878614 224 EA----TNLNGGLLRGieiLNQVQESLPELSNHASILIMLTDGDPTEGVTDRSQILKNVRN 280
Cdd:cd01476   74 RFiggtTATGAAIEVA---LQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPN 131
 
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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