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Conserved domains on  [gi|2208424302|ref|NP_001276804|]
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inter-alpha-trypsin inhibitor heavy chain H6 precursor [Mus musculus]

Protein Classification

vWA_interalpha_trypsin_inhibitor and ITI_HC_C domain-containing protein( domain architecture ID 13065794)

protein containing domains VIT, marine_srt_targ, vWA_interalpha_trypsin_inhibitor, and ITI_HC_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
280-464 5.44e-64

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: 214.39  E-value: 5.44e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  280 LEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNIWKAeGSIQATVQNIHSAKNYVSRMEADGW 359
Cdd:cd01461      1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSP-SSVSATAENVAAAIEYVNRLQALGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  360 TDINAALLAAASVLNHSNqepgkgrgvGQIPLIMFLTDGEptagETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLR 439
Cdd:cd01461     80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146
                          170       180
                   ....*....|....*....|....*
gi 2208424302  440 RLSLENQGEARRIYEDADAALQLEG 464
Cdd:cd01461    147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
1087-1268 3.28e-54

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: 429061  Cd Length: 189  Bit Score: 187.41  E-value: 3.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1087 KAGLHVSGQLLGAPSRPSHKDQTRTYFHIITITSdKPRAYNITISRSSISV-QGESTLSLSWNQRALVKKPHLELHVASA 1165
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVV-KPLGVKIEVTPEKITLkDGEKRLVLSWSDTASVKQPGLTVSVVKN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1166 ALLTVRLGPHLNFFILRHQYRHPSTLQLPHLGFYVANGSGLSPSARGLMGQFQY-TDIRLVTGPSGS------YLQKHHG 1238
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKPHPYQVDHLGFYIVNSKGLSPSVHGLLGQFLHePEVEVTDVRPGSdpekpdATMKVKG 159
                          170       180       190
                   ....*....|....*....|....*....|
gi 2208424302 1239 LDVPVVLGKRLLKESPRLLPRWTSCWIVKR 1268
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
40-150 3.02e-46

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) stabilisation and tumor 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: 445889 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 3.02e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302    40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:smart00609   20 LKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAGL 99
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2208424302   120 VGIRDRESENFRISTMLAAGTKATFALAYEE 150
Cdd:smart00609  100 VRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
marine_srt_targ super family cl37326
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
51-630 2.74e-38

marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).


The actual alignment was detected with superfamily member TIGR03788:

Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 152.54  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   51 ANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAHVgirDRESENF 130
Cdd:TIGR03788   14 ARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV---EQQRPNL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  131 RISTM--LAAGTKATFALAYEELLQRHQG----RYQLVVGLR--PGQLVrklNVEITVSERT-GIAYVHIP-PLRTSQVC 200
Cdd:TIGR03788   91 FTNKVanIGPGETVVVTIEYQQPVSYSSGtfslRLPLTVTPRyiPGSTV---NTVTDVNNSGwAIPTTQVPdADKISAPR 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  201 TnnqTSEGDLPPSTR------IQRGETCVHITfSPT------LRDQSAFSSS----GIMADFTihYDVSMEDIIGDV--- 261
Cdd:TIGR03788  168 V---LDPDDDAPSSQasinvdLNAGLPLDSIT-SPShpiqieQQGQSGYTISlaqgQVIADRD--FVLTWRPAQGEApsa 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  262 ----QVYGGYfiHY--------FAPRGLQPLEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN 329
Cdd:TIGR03788  242 alfrEQIGGE--RYglamvmppTEAAVAQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  330 -IWKaeGSIQATVQNIHSAKNYVSRMEADGWTDInaALLAAASVLNHSNQEPGKGRGVgqipliMFLTDGEpTAGEttpS 408
Cdd:TIGR03788  320 lLFP--VPVPATAHNLARARQFVAGLQADGGTEM--AGALSAALRDDGPESSGALRQV------VFLTDGA-VGNE---D 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  409 VILSNIRQALAHRvSLFSLAFGDDADFSLLRRLSLENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDYLGGWVGA 488
Cdd:TIGR03788  386 ALFQLIRTKLGDS-RLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAAD 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  489 SSRAHFPNYFHGSELVVAGKVQPGEQELGIhlAARGPNGHLLVAHHSEEASNSSQkafgcpgkpalnvthfIHRLWAYVT 568
Cdd:TIGR03788  465 VYPSPIPDLYRGEPLQIAIKLQQAAGELQL--TGRTGSQPWSQQLDLDSAAPGKG----------------IDKLWARRK 526
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2208424302  569 IGELLKARFQAKDTTtrrllAAKA--LNLSLEYNFVTPLTSLVVVHLEKTNEEAMTQPSTTAKT 630
Cdd:TIGR03788  527 IDSLEDSLRYGANEE-----KVKDqvTALALNHHLVSPFTSFVAVEETPIRPAAESLNSEASPN 585
PHA03247 super family cl33720
large tegument protein UL36; Provisional
655-996 1.80e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  655 KVFSKSRPTKPTSTIIAPTMKvtsskelgALGWWSNSLTTSVQPKPQ------IPGQDSSTLALPTLKMKPLAHVPSNSN 728
Cdd:PHA03247  2666 RARRLGRAAQASSPPQRPRRR--------AARPTVGSLTSLADPPPPpptpepAPHALVSATPLPPGPAAARQASPALPA 2737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  729 DPLPRKPSTSTHQNPGITSLVNSGTYILPLNPVSPSQPKGGTMKHFNSFSPFKLPASSDAHPTPDTPS-----YLQPVSQ 803
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAA 2817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  804 EPISQS-SQSVPQPkyisTFQIPKHPlhlsskdlaPKTSPNLPHSKP--GNVLPKSP---KIPSSHEPSVSSHQTSP--S 875
Cdd:PHA03247  2818 LPPAASpAGPLPPP----TSAQPTAP---------PPPPGPPPPSLPlgGSVAPGGDvrrRPPSRSPAAKPAAPARPpvR 2884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  876 LLLSKSRTPTTYSTQIPLPARPRPLVPQSlntfsntlssstspsstvatsiPGEPLPSPFTPTLTSLLPTARRWHQQDPL 955
Cdd:PHA03247  2885 RLARPAVSRSTESFALPPDQPERPPQPQA----------------------PPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2208424302  956 LGPKS-TSTLPEAITLHLLPEKLHLLSESVEESKFVESLNPP 996
Cdd:PHA03247  2943 LAPTTdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
280-464 5.44e-64

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: 214.39  E-value: 5.44e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  280 LEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNIWKAeGSIQATVQNIHSAKNYVSRMEADGW 359
Cdd:cd01461      1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSP-SSVSATAENVAAAIEYVNRLQALGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  360 TDINAALLAAASVLNHSNqepgkgrgvGQIPLIMFLTDGEptagETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLR 439
Cdd:cd01461     80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146
                          170       180
                   ....*....|....*....|....*
gi 2208424302  440 RLSLENQGEARRIYEDADAALQLEG 464
Cdd:cd01461    147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
1087-1268 3.28e-54

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: 429061  Cd Length: 189  Bit Score: 187.41  E-value: 3.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1087 KAGLHVSGQLLGAPSRPSHKDQTRTYFHIITITSdKPRAYNITISRSSISV-QGESTLSLSWNQRALVKKPHLELHVASA 1165
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVV-KPLGVKIEVTPEKITLkDGEKRLVLSWSDTASVKQPGLTVSVVKN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1166 ALLTVRLGPHLNFFILRHQYRHPSTLQLPHLGFYVANGSGLSPSARGLMGQFQY-TDIRLVTGPSGS------YLQKHHG 1238
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKPHPYQVDHLGFYIVNSKGLSPSVHGLLGQFLHePEVEVTDVRPGSdpekpdATMKVKG 159
                          170       180       190
                   ....*....|....*....|....*....|
gi 2208424302 1239 LDVPVVLGKRLLKESPRLLPRWTSCWIVKR 1268
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
40-150 3.02e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 3.02e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302    40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:smart00609   20 LKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAGL 99
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2208424302   120 VGIRDRESENFRISTMLAAGTKATFALAYEE 150
Cdd:smart00609  100 VRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
51-630 2.74e-38

marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 152.54  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   51 ANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAHVgirDRESENF 130
Cdd:TIGR03788   14 ARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV---EQQRPNL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  131 RISTM--LAAGTKATFALAYEELLQRHQG----RYQLVVGLR--PGQLVrklNVEITVSERT-GIAYVHIP-PLRTSQVC 200
Cdd:TIGR03788   91 FTNKVanIGPGETVVVTIEYQQPVSYSSGtfslRLPLTVTPRyiPGSTV---NTVTDVNNSGwAIPTTQVPdADKISAPR 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  201 TnnqTSEGDLPPSTR------IQRGETCVHITfSPT------LRDQSAFSSS----GIMADFTihYDVSMEDIIGDV--- 261
Cdd:TIGR03788  168 V---LDPDDDAPSSQasinvdLNAGLPLDSIT-SPShpiqieQQGQSGYTISlaqgQVIADRD--FVLTWRPAQGEApsa 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  262 ----QVYGGYfiHY--------FAPRGLQPLEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN 329
Cdd:TIGR03788  242 alfrEQIGGE--RYglamvmppTEAAVAQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  330 -IWKaeGSIQATVQNIHSAKNYVSRMEADGWTDInaALLAAASVLNHSNQEPGKGRGVgqipliMFLTDGEpTAGEttpS 408
Cdd:TIGR03788  320 lLFP--VPVPATAHNLARARQFVAGLQADGGTEM--AGALSAALRDDGPESSGALRQV------VFLTDGA-VGNE---D 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  409 VILSNIRQALAHRvSLFSLAFGDDADFSLLRRLSLENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDYLGGWVGA 488
Cdd:TIGR03788  386 ALFQLIRTKLGDS-RLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAAD 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  489 SSRAHFPNYFHGSELVVAGKVQPGEQELGIhlAARGPNGHLLVAHHSEEASNSSQkafgcpgkpalnvthfIHRLWAYVT 568
Cdd:TIGR03788  465 VYPSPIPDLYRGEPLQIAIKLQQAAGELQL--TGRTGSQPWSQQLDLDSAAPGKG----------------IDKLWARRK 526
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2208424302  569 IGELLKARFQAKDTTtrrllAAKA--LNLSLEYNFVTPLTSLVVVHLEKTNEEAMTQPSTTAKT 630
Cdd:TIGR03788  527 IDSLEDSLRYGANEE-----KVKDqvTALALNHHLVSPFTSFVAVEETPIRPAAESLNSEASPN 585
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
40-148 2.04e-32

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) stabilisation and tumor 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.


Pssm-ID: 430025 [Multi-domain]  Cd Length: 111  Bit Score: 121.86  E-value: 2.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:pfam08487    4 VSVEATITGRIARTTVTQTFVNPSSEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKTAGL 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 2208424302  120 VgiRDRESENFRIST-MLAAGTKATFALAY 148
Cdd:pfam08487   84 L--EQDDPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
283-458 7.12e-22

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: 94.06  E-value: 7.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWKAEGSIqatvQNIHSAKNYVSRME--AD 357
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSykLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   358 GWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGettPSVILSNIRQALAHRVSLFSLAFGDDADFSL 437
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSA--GSRRGAPKV--VILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
                           170       180
                    ....*....|....*....|.
gi 2208424302   438 LRRLSLENQGEARRIYEDADA 458
Cdd:smart00327  150 LKKLASAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
283-468 6.56e-16

von Willebrand factor type A domain;


Pssm-ID: 425461 [Multi-domain]  Cd Length: 174  Bit Score: 76.93  E-value: 6.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA---SDSFNIITFSDTVNIWkaegsIQ-ATVQNIHSAKNYVSRME--A 356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTE-----FPlNDYSSKEELLSAVDNLRylG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  357 DGWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGEttpsvILSNIRQALAHRVSLFSLAFGdDADFS 436
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAA--GARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDE 145
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2208424302  437 LLRRLSLENqgEARRIYEDADAAlQLEGLYAE 468
Cdd:pfam00092  146 ELRKIASEP--GEGHVFTVSDFE-ALEDLQDQ 174
PHA03247 PHA03247
large tegument protein UL36; Provisional
655-996 1.80e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  655 KVFSKSRPTKPTSTIIAPTMKvtsskelgALGWWSNSLTTSVQPKPQ------IPGQDSSTLALPTLKMKPLAHVPSNSN 728
Cdd:PHA03247  2666 RARRLGRAAQASSPPQRPRRR--------AARPTVGSLTSLADPPPPpptpepAPHALVSATPLPPGPAAARQASPALPA 2737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  729 DPLPRKPSTSTHQNPGITSLVNSGTYILPLNPVSPSQPKGGTMKHFNSFSPFKLPASSDAHPTPDTPS-----YLQPVSQ 803
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAA 2817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  804 EPISQS-SQSVPQPkyisTFQIPKHPlhlsskdlaPKTSPNLPHSKP--GNVLPKSP---KIPSSHEPSVSSHQTSP--S 875
Cdd:PHA03247  2818 LPPAASpAGPLPPP----TSAQPTAP---------PPPPGPPPPSLPlgGSVAPGGDvrrRPPSRSPAAKPAAPARPpvR 2884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  876 LLLSKSRTPTTYSTQIPLPARPRPLVPQSlntfsntlssstspsstvatsiPGEPLPSPFTPTLTSLLPTARRWHQQDPL 955
Cdd:PHA03247  2885 RLARPAVSRSTESFALPPDQPERPPQPQA----------------------PPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2208424302  956 LGPKS-TSTLPEAITLHLLPEKLHLLSESVEESKFVESLNPP 996
Cdd:PHA03247  2943 LAPTTdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
283-481 4.19e-06

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


Pssm-ID: 225187 [Multi-domain]  Cd Length: 399  Bit Score: 50.72  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiWKAEGSIQATVQNIHSAKNYVSRmeADGWTDI 362
Cdd:COG2304     39 NLTLAIDTSGSMTGALLELAKSAAIELVNGLNPGDLLSIVTFAGSAD-VLIPPTGATNKESITAAIDQSLQ--AGGATAV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  363 naALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRLS 442
Cdd:COG2304    116 --EASLSLAVELAA-----KALPRGTLNRILLLTDGENNLGLVDPSRLSALAKLAAGKGIVLDTLGLGDDVNEDELTGIA 188
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2208424302  443 LENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDY 481
Cdd:COG2304    189 AAANGNLAFIYLSSLSEAQFVIALEKSQTVLLVIGVTDA 227
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
690-905 1.78e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 427171 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  690 NSLTTSVQPKPQIPGQDS-STLALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPgiTSLVNSGTYILPLNPVSP-SQPK 767
Cdd:pfam03154  141 NRSTSPSIPSPQDNESDSdSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA--TAGPTPSAPSVPPQGSPAtSQPP 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  768 GGTMKHFNSFSPFKLPASSDAHPTPDTPSYLQPVSQE--PISQSSQSVPQPKYISTFQIPKHPLHLSskdlapktSPNLP 845
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPppPSQVSPQPLPQPSLHGQMPPMPHSLQTG--------PSHMQ 290
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  846 HSKPGNVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSL 905
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
694-906 1.94e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  694 TSVQPKPQIPGQDSST-LALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPGITSlvnsgtyilPLNPVSPSQPKGGTMK 772
Cdd:NF033839   297 PGMQPSPQPEKKEVKPePETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK---------PEVKPQPEKPKPEVKP 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  773 HFNSFSPfklpassDAHPTPDTPSYL---QPVSQEPISQSSQSVPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKP 849
Cdd:NF033839   368 QPEKPKP-------EVKPQPETPKPEvkpQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKP 440
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2208424302  850 G-NVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARP-----RPLVPQSLN 906
Cdd:NF033839   441 EvKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPqaddkKPSTPNNLS 503
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
280-464 5.44e-64

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: 214.39  E-value: 5.44e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  280 LEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNIWKAeGSIQATVQNIHSAKNYVSRMEADGW 359
Cdd:cd01461      1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSP-SSVSATAENVAAAIEYVNRLQALGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  360 TDINAALLAAASVLNHSNqepgkgrgvGQIPLIMFLTDGEptagETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLR 439
Cdd:cd01461     80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146
                          170       180
                   ....*....|....*....|....*
gi 2208424302  440 RLSLENQGEARRIYEDADAALQLEG 464
Cdd:cd01461    147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
1087-1268 3.28e-54

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: 429061  Cd Length: 189  Bit Score: 187.41  E-value: 3.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1087 KAGLHVSGQLLGAPSRPSHKDQTRTYFHIITITSdKPRAYNITISRSSISV-QGESTLSLSWNQRALVKKPHLELHVASA 1165
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVV-KPLGVKIEVTPEKITLkDGEKRLVLSWSDTASVKQPGLTVSVVKN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1166 ALLTVRLGPHLNFFILRHQYRHPSTLQLPHLGFYVANGSGLSPSARGLMGQFQY-TDIRLVTGPSGS------YLQKHHG 1238
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKPHPYQVDHLGFYIVNSKGLSPSVHGLLGQFLHePEVEVTDVRPGSdpekpdATMKVKG 159
                          170       180       190
                   ....*....|....*....|....*....|
gi 2208424302 1239 LDVPVVLGKRLLKESPRLLPRWTSCWIVKR 1268
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
40-150 3.02e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 3.02e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302    40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:smart00609   20 LKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAGL 99
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2208424302   120 VGIRDRESENFRISTMLAAGTKATFALAYEE 150
Cdd:smart00609  100 VRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
51-630 2.74e-38

marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 152.54  E-value: 2.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   51 ANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAHVgirDRESENF 130
Cdd:TIGR03788   14 ARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV---EQQRPNL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  131 RISTM--LAAGTKATFALAYEELLQRHQG----RYQLVVGLR--PGQLVrklNVEITVSERT-GIAYVHIP-PLRTSQVC 200
Cdd:TIGR03788   91 FTNKVanIGPGETVVVTIEYQQPVSYSSGtfslRLPLTVTPRyiPGSTV---NTVTDVNNSGwAIPTTQVPdADKISAPR 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  201 TnnqTSEGDLPPSTR------IQRGETCVHITfSPT------LRDQSAFSSS----GIMADFTihYDVSMEDIIGDV--- 261
Cdd:TIGR03788  168 V---LDPDDDAPSSQasinvdLNAGLPLDSIT-SPShpiqieQQGQSGYTISlaqgQVIADRD--FVLTWRPAQGEApsa 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  262 ----QVYGGYfiHY--------FAPRGLQPLEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN 329
Cdd:TIGR03788  242 alfrEQIGGE--RYglamvmppTEAAVAQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  330 -IWKaeGSIQATVQNIHSAKNYVSRMEADGWTDInaALLAAASVLNHSNQEPGKGRGVgqipliMFLTDGEpTAGEttpS 408
Cdd:TIGR03788  320 lLFP--VPVPATAHNLARARQFVAGLQADGGTEM--AGALSAALRDDGPESSGALRQV------VFLTDGA-VGNE---D 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  409 VILSNIRQALAHRvSLFSLAFGDDADFSLLRRLSLENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDYLGGWVGA 488
Cdd:TIGR03788  386 ALFQLIRTKLGDS-RLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAAD 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  489 SSRAHFPNYFHGSELVVAGKVQPGEQELGIhlAARGPNGHLLVAHHSEEASNSSQkafgcpgkpalnvthfIHRLWAYVT 568
Cdd:TIGR03788  465 VYPSPIPDLYRGEPLQIAIKLQQAAGELQL--TGRTGSQPWSQQLDLDSAAPGKG----------------IDKLWARRK 526
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2208424302  569 IGELLKARFQAKDTTtrrllAAKA--LNLSLEYNFVTPLTSLVVVHLEKTNEEAMTQPSTTAKT 630
Cdd:TIGR03788  527 IDSLEDSLRYGANEE-----KVKDqvTALALNHHLVSPFTSFVAVEETPIRPAAESLNSEASPN 585
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
40-148 2.04e-32

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) stabilisation and tumor 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.


Pssm-ID: 430025 [Multi-domain]  Cd Length: 111  Bit Score: 121.86  E-value: 2.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:pfam08487    4 VSVEATITGRIARTTVTQTFVNPSSEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKTAGL 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 2208424302  120 VgiRDRESENFRIST-MLAAGTKATFALAY 148
Cdd:pfam08487   84 L--EQDDPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
283-458 7.12e-22

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: 94.06  E-value: 7.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWKAEGSIqatvQNIHSAKNYVSRME--AD 357
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSykLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302   358 GWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGettPSVILSNIRQALAHRVSLFSLAFGDDADFSL 437
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSA--GSRRGAPKV--VILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
                           170       180
                    ....*....|....*....|.
gi 2208424302   438 LRRLSLENQGEARRIYEDADA 458
Cdd:smart00327  150 LKKLASAPGGVYVFLPELLDL 170
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
283-459 1.06e-21

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: 93.49  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTvniwkAEGSIQATVQNIHSA-KNYVSRMEADGWTD 361
Cdd:cd01465      2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGA-----AETVLPATPVRDKAAiLAAIDRLTAGGSTA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  362 InaallaaASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRL 441
Cdd:cd01465     77 G-------GAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
                          170
                   ....*....|....*...
gi 2208424302  442 SLENQGEARRIYEDADAA 459
Cdd:cd01465    150 ADAGNGNTAYIDNLAEAR 167
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
283-449 2.59e-20

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: 89.16  E-value: 2.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWkAEGSIQATVQNIHSAKNYVsRMEADGW 359
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVV-LPLTTDTDKADLLEAIDAL-KKGLGGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  360 TDInaallaaASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQAlahRVSLFSLAFGDDADFSLLR 439
Cdd:cd00198     80 TNI-------GAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELK 149
                          170
                   ....*....|
gi 2208424302  440 RLSLENQGEA 449
Cdd:cd00198    150 EIADKTTGGA 159
VWA pfam00092
von Willebrand factor type A domain;
283-468 6.56e-16

von Willebrand factor type A domain;


Pssm-ID: 425461 [Multi-domain]  Cd Length: 174  Bit Score: 76.93  E-value: 6.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA---SDSFNIITFSDTVNIWkaegsIQ-ATVQNIHSAKNYVSRME--A 356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTE-----FPlNDYSSKEELLSAVDNLRylG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  357 DGWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGEttpsvILSNIRQALAHRVSLFSLAFGdDADFS 436
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAA--GARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDE 145
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2208424302  437 LLRRLSLENqgEARRIYEDADAAlQLEGLYAE 468
Cdd:pfam00092  146 ELRKIASEP--GEGHVFTVSDFE-ALEDLQDQ 174
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
282-447 4.61e-14

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: 72.04  E-value: 4.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  282 KNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN--IWKAEGS-IQATVQNIHSAKNYVSRMEADG 358
Cdd:cd01463     14 KDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNpvVPCFNDTlVQATTSNKKVLKEALDMLEAKG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  359 WTDINAALLAAASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPtagETTPSVI-LSNIRQALAHRVSLFSLAFGDDA-DFS 436
Cdd:cd01463     94 IANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVP---ENYKEIFdKYNWDKNSEIPVRVFTYLIGREVtDRR 170
                          170
                   ....*....|.
gi 2208424302  437 LLRRLSLENQG 447
Cdd:cd01463    171 EIQWMACENKG 181
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
284-400 5.57e-11

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: 62.02  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiwKAEGSIQATVQNIHSAKNYVSRMEADGWTDIN 363
Cdd:cd01466      3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAK--RLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2208424302  364 AALLAAASVLnhsnqepGKGRGVGQIPLIMFLTDGEP 400
Cdd:cd01466     81 GGLKKALKVL-------GDRRQKNPVASIMLLSDGQD 110
VWA_3 pfam13768
von Willebrand factor type A domain;
282-450 1.57e-07

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 52.01  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  282 KNVVFVIDVSGSMFGTKLQQtKKAMDTILSDLQASDSFNIITFSDTVNIWKAEGsiqatvQNIHSAknyvSRMEADGWTD 361
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGW------RVVSPR----SLQEAFQFIK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  362 INAALLAAASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTpsvILSNIRQALAHrVSLFSLAFGDDADFSLLRRL 441
Cdd:pfam13768   70 TLQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQGETR---VSDLISRAPGK-IRFFAYGLGASISAPMLQLL 145

                   ....*....
gi 2208424302  442 SLENQGEAR 450
Cdd:pfam13768  146 AEASNGTYE 154
PHA03247 PHA03247
large tegument protein UL36; Provisional
655-996 1.80e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  655 KVFSKSRPTKPTSTIIAPTMKvtsskelgALGWWSNSLTTSVQPKPQ------IPGQDSSTLALPTLKMKPLAHVPSNSN 728
Cdd:PHA03247  2666 RARRLGRAAQASSPPQRPRRR--------AARPTVGSLTSLADPPPPpptpepAPHALVSATPLPPGPAAARQASPALPA 2737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  729 DPLPRKPSTSTHQNPGITSLVNSGTYILPLNPVSPSQPKGGTMKHFNSFSPFKLPASSDAHPTPDTPS-----YLQPVSQ 803
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAA 2817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  804 EPISQS-SQSVPQPkyisTFQIPKHPlhlsskdlaPKTSPNLPHSKP--GNVLPKSP---KIPSSHEPSVSSHQTSP--S 875
Cdd:PHA03247  2818 LPPAASpAGPLPPP----TSAQPTAP---------PPPPGPPPPSLPlgGSVAPGGDvrrRPPSRSPAAKPAAPARPpvR 2884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  876 LLLSKSRTPTTYSTQIPLPARPRPLVPQSlntfsntlssstspsstvatsiPGEPLPSPFTPTLTSLLPTARRWHQQDPL 955
Cdd:PHA03247  2885 RLARPAVSRSTESFALPPDQPERPPQPQA----------------------PPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2208424302  956 LGPKS-TSTLPEAITLHLLPEKLHLLSESVEESKFVESLNPP 996
Cdd:PHA03247  2943 LAPTTdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PHA03247 PHA03247
large tegument protein UL36; Provisional
628-949 4.11e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 4.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  628 AKTSTVTPSSSNRLGLGTGTAQPASvlkvfsksrPTKPTSTIIAPTMKVTSSKELgalgwwSNSLTTSVQPKPQIPGqDS 707
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPA---------PAPPAAPAAGPPRRLTRPAVA------SLSESRESLPSPWDPA-DP 2807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  708 STLALPTLKMKPLAHVPSNsndPLPrKPSTSTHQNPGitslvnsgtyiLPLNPVSPSQPKGGTMKHFNSFSpfKLPASSD 787
Cdd:PHA03247  2808 PAAVLAPAAALPPAASPAG---PLP-PPTSAQPTAPP-----------PPPGPPPPSLPLGGSVAPGGDVR--RRPPSRS 2870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  788 AHPTPDTPSY--LQPVSQEPISQSSQSVPQPkyistfqiPKHPLHLSSKDLAPKTSPNLPHSKPGNVLPKSPKIPSSHEP 865
Cdd:PHA03247  2871 PAAKPAAPARppVRRLARPAVSRSTESFALP--------PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  866 SVSSHQTSPSLLLSKSRTPTTYSTQIP-LPARPRPLVPQSLntfsntlssstspsstvatsiPGEPLPSPFTPTLTSL-L 943
Cdd:PHA03247  2943 LAPTTDPAGAGEPSGAVPQPWLGALVPgRVAVPRFRVPQPA---------------------PSREAPASSTPPLTGHsL 3001

                   ....*.
gi 2208424302  944 PTARRW 949
Cdd:PHA03247  3002 SRVSSW 3007
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
284-442 6.71e-07

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


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 50.80  E-value: 6.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQ----ASDS--FNIITFsdtvniwkaeGSIQATVQNIHSAKN-YVSRMEA 356
Cdd:cd01464      6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRqdpyALESveISVITF----------DSAARVIVPLTPLESfQPPRLTA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  357 DGWTDINAALLAAASVLNHSNQEPgKGRGVGQI-PLIMFLTDGEPTaGETTPSVilSNIRQALAHRVSLFSLAFGDDADF 435
Cdd:cd01464     76 SGGTSMGAALELALDCIDRRVQRY-RADQKGDWrPWVFLLTDGEPT-DDLTAAI--ERIKEARDSKGRIVACAVGPKADL 151

                   ....*..
gi 2208424302  436 SLLRRLS 442
Cdd:cd01464    152 DTLKQIT 158
VWA_2 pfam13519
von Willebrand factor type A domain;
284-330 1.08e-06

von Willebrand factor type A domain;


Pssm-ID: 433277 [Multi-domain]  Cd Length: 103  Bit Score: 48.44  E-value: 1.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2208424302  284 VVFVIDVSGSM-----FGTKLQQTKKAMDTILSDLqASDSFNIITFSDTVNI 330
Cdd:pfam13519    1 LVFVLDTSGSMrngdyLPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEV 51
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
280-434 2.22e-06

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


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 49.74  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  280 LEKNVVFVIDVSGSM------FGTKLQQTKKAMDTILSDLQASDSFNIITFS---DTVNIWKAEGSIQATVQNIH----- 345
Cdd:cd01456     19 LPPNVAIVLDNSGSMrevdggGETRLDNAKAALDETANALPDGTRLGLWTFSgdgDNPLDVRVLVPKGCLTAPVNgfpsa 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  346 ---SAKNYVSRM-EADGWTDINAALlaaasvlnhsnQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNI-RQALAH 420
Cdd:cd01456     99 qrsALDAALNSLqTPTGWTPLAAAL-----------AEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAkRRTPAP 167
                          170
                   ....*....|....
gi 2208424302  421 RVSLFSLAFGDDAD 434
Cdd:cd01456    168 PIKVNVIDFGGDAD 181
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
283-481 4.19e-06

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


Pssm-ID: 225187 [Multi-domain]  Cd Length: 399  Bit Score: 50.72  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiWKAEGSIQATVQNIHSAKNYVSRmeADGWTDI 362
Cdd:COG2304     39 NLTLAIDTSGSMTGALLELAKSAAIELVNGLNPGDLLSIVTFAGSAD-VLIPPTGATNKESITAAIDQSLQ--AGGATAV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  363 naALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRLS 442
Cdd:COG2304    116 --EASLSLAVELAA-----KALPRGTLNRILLLTDGENNLGLVDPSRLSALAKLAAGKGIVLDTLGLGDDVNEDELTGIA 188
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2208424302  443 LENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDY 481
Cdd:COG2304    189 AAANGNLAFIYLSSLSEAQFVIALEKSQTVLLVIGVTDA 227
ChlD COG1240
Mg-chelatase subunit ChlD [Coenzyme transport and metabolism];
284-407 8.84e-06

Mg-chelatase subunit ChlD [Coenzyme transport and metabolism];


Pssm-ID: 224161 [Multi-domain]  Cd Length: 261  Bit Score: 48.90  E-value: 8.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  284 VVFVIDVSGSMFG-TKLQQTKKAMDTILSD-LQASDSFNIITFSDTvniwKAEGSIQATvQNIHSAKNYVSRMEADGWTD 361
Cdd:COG1240     81 IVFVVDASGSMAArRRMAAAKGAALSLLRDaYQRRDKVAVIAFRGE----KAELLLPPT-SSVELAERALERLPTGGKTP 155
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2208424302  362 INAALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTP 407
Cdd:COG1240    156 LADALRQAYEVLARE-----KRRGPDRRPVMVVITDGRANVPIPLG 196
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
690-905 1.78e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 427171 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  690 NSLTTSVQPKPQIPGQDS-STLALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPgiTSLVNSGTYILPLNPVSP-SQPK 767
Cdd:pfam03154  141 NRSTSPSIPSPQDNESDSdSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA--TAGPTPSAPSVPPQGSPAtSQPP 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  768 GGTMKHFNSFSPFKLPASSDAHPTPDTPSYLQPVSQE--PISQSSQSVPQPKYISTFQIPKHPLHLSskdlapktSPNLP 845
Cdd:pfam03154  219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPppPSQVSPQPLPQPSLHGQMPPMPHSLQTG--------PSHMQ 290
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  846 HSKPGNVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSL 905
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
699-945 2.44e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  699 KPQIPGQDSSTLALPTLKMKPLAHVPSNSNDPL----PRKPSTsthqnpgitslvnsgtyilPLNPVSPSQPKGGtmkhf 774
Cdd:PTZ00449   596 KPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPEspksPKRPPP-------------------PQRPSSPERPEGP----- 651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  775 nsfspfKLPASSDAHPTPDTPsyLQPVSQEPISQS-SQSVPQPKYISTFQIPKHPLHLSSKDLAPKTsPNLPHSKPGNVL 853
Cdd:PTZ00449   652 ------KIIKSPKPPKSPKPP--FDPKFKEKFYDDyLDAAAKSKETKTTVVLDESFESILKETLPET-PGTPFTTPRPLP 722
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  854 PKSPKIPSS-HEP--SVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSLNTFSNTLSSSTspsstvatsiPGEP 930
Cdd:PTZ00449   723 PKLPRDEEFpFEPigDPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGE----------PDEA 792
                          250
                   ....*....|....*
gi 2208424302  931 LPSPFTPTLTSLLPT 945
Cdd:PTZ00449   793 MKRPDSPSEHEDKPP 807
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
283-442 2.55e-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: 43.05  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDL-QASDS--FNIITFSDTVNIW------KAEGSIQATVQNIHSaknyvsr 353
Cdd:cd01450      2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdIGPDKtrVGLVQYSDDVRVEfslndyKSKDDLLKAVKNLKY------- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  354 MEADGwTDINAALLAaasVLNHSNQEPGKGRGVGQIplIMFLTDGEPTAGeTTPSVILSNIRQalaHRVSLFSLAFGdDA 433
Cdd:cd01450     75 LGGGG-TNTGKALQY---ALEQLFSESNARENVPKV--IIVLTDGRSDDG-GDPKEAAAKLKD---EGIKVFVVGVG-PA 143

                   ....*....
gi 2208424302  434 DFSLLRRLS 442
Cdd:cd01450    144 DEEELREIA 152
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
693-937 2.79e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 44.92  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  693 TTSVQPKPQIPGQDSSTLALPTLKMKPLAhvPSNSNDPLprKPSTSThqnpgitslvnsgtyilplnpvSPSQPKGGTMK 772
Cdd:PLN03209   344 TKPVTPEAPSPPIEEEPPQPKAVVPRPLS--PYTAYEDL--KPPTSP----------------------IPTPPSSSPAS 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  773 HfNSFSPFKLPASSDAHPTPDTPSylqpvsqepisqssqSVPQPKYISTFQIPKHPL--HLSSKDLAPKTSPN------- 843
Cdd:PLN03209   398 S-KSVDAVAKPAEPDVVPSPGSAS---------------NVPEVEPAQVEAKKTRPLspYARYEDLKPPTSPSptaptgv 461
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  844 LPHSKPGNVLPKSPKIP-------SSHEPSVSSHQTSPSLLLSKSRTPTTystqiPLPARPRPLVPQSLNTFSNTLSSST 916
Cdd:PLN03209   462 SPSVSSTSSVPAVPDTApataatdAAAPPPANMRPLSPYAVYDDLKPPTS-----PSPAAPVGKVAPSSTNEVVKVGNSA 536
                          250       260
                   ....*....|....*....|.
gi 2208424302  917 SPSSTVATSIPGEPLPSPFTP 937
Cdd:PLN03209   537 PPTALADEQHHAQPKPRPLSP 557
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
284-403 5.57e-04

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: 42.26  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  284 VVFVIDVSGSM-FGTKLQQTKKAMDTILSD-LQASDSFNIITFSDTvniwkaegsiQATV-----QNIHSAKNYVSRMEA 356
Cdd:cd01451      3 VIFVVDASGSMaARHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGT----------EAEVllpptRSVELAKRRLARLPT 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2208424302  357 DGWTDINAALLAAASVLNHSnqepgkGRGVGQIPLIMFLTDGEPTAG 403
Cdd:cd01451     73 GGGTPLAAGLLAAYELAAEQ------ARDPGQRPLIVVITDGRANVG 113
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
579-864 5.65e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 436069 [Multi-domain]  Cd Length: 480  Bit Score: 44.14  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  579 AKDTTTRRLLAAKALN--LSLEYNFVTPLTSLVVVHLEKTNEEAmtqPSTTAKTSTVTPSSSNrLGLGTGTAQPASVLKV 656
Cdd:pfam17823  102 AADGAASRALAAAASSspSSAAQSAPTTIAGLPSLASSAPMAAA---PRTNAASNAPTAAASS-TAAASGAPTTAASSAP 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  657 fSKSRPTKPTSTIIAPTMKVTSSKELGALGwwsNSLTTSVQPKPQIPGQDSSTLALPTLKMKPLAHV--PSNSNDPLPRK 734
Cdd:pfam17823  178 -ATLTPASGISTAATATGHPAAGTALAAVG---NSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAagTINTGDPHARR 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  735 PSTSTHQNPGITSlvnsgtyilpLNPVSPSQPKG-GTMKHFNSFSPFklpASSDAHPTPD-TPSYLQPVSQEPISQSSQS 812
Cdd:pfam17823  254 LSPAKHMPSDTSA----------RNPAAPSGAQAqGLIIQVSTDQPV---HNTAGEPTPSpSNTTLEPNTPKSVASTNLA 320
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2208424302  813 VPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKPGNVLPKS----PKIPSSHE 864
Cdd:pfam17823  321 VVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQgaagPGILLAPD 376
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
694-906 1.94e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  694 TSVQPKPQIPGQDSST-LALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPGITSlvnsgtyilPLNPVSPSQPKGGTMK 772
Cdd:NF033839   297 PGMQPSPQPEKKEVKPePETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK---------PEVKPQPEKPKPEVKP 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  773 HFNSFSPfklpassDAHPTPDTPSYL---QPVSQEPISQSSQSVPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKP 849
Cdd:NF033839   368 QPEKPKP-------EVKPQPETPKPEvkpQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKP 440
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2208424302  850 G-NVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARP-----RPLVPQSLN 906
Cdd:NF033839   441 EvKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPqaddkKPSTPNNLS 503
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
284-442 9.10e-03

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


Pssm-ID: 226696 [Multi-domain]  Cd Length: 207  Bit Score: 38.97  E-value: 9.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA------SDSFNIITFSDTVNiwkaegsiqaTVQNIHSAKN-YVSRMEA 356
Cdd:COG4245      6 CYLLLDTSGSMIGEPIEALNAGLQMMIDTLKQdpyaleRVELSIVTFGGPAR----------VIQPFTDAANfNPPILTA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  357 DGWTDINAALLAAASVLNHSNQEPgKGRGVGQI-PLIMFLTDGEPTaGETTPSVILSNIRQALAHRVSLFSLAfGDDADF 435
Cdd:COG4245     76 QGGTPLGAALTLALDMIEERKRKY-DANGKGDYrPWVFLITDGEPT-DDWQAGAALVFQGERRAKSVAAFSVG-VQGADN 152

                   ....*..
gi 2208424302  436 SLLRRLS 442
Cdd:COG4245    153 KTLNQIT 159
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
626-971 9.79e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.28  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  626 TTAKTSTVTPSSSNrlglGTGTAQPAsvlkVFSKSrptkPTSTIIAPTMKVTsskelgalGWWSNSLTTsvqpkpqipGQ 705
Cdd:pfam05109  398 TAPKTLIITRTATN----ATTTTHKV----IFSKA----PESTTTSPTLNTT--------GFAAPNTTT---------GL 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  706 DSSTlalptlkmkplaHVPSNSNDPLPRKPSTSTHQnpgITSLVNSGTY--ILPLNPvSPSQPKGGTmkhfNSFSP-FKL 782
Cdd:pfam05109  449 PSST------------HVPTNLTAPASTGPTVSTAD---VTSPTPAGTTsgASPVTP-SPSPRDNGT----ESKAPdMTS 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  783 PASSDAHPTPDTPSYLQPVSQEPISQSSQSVPQPKYISTFQIPKhPLHLSSKDLAPKTSPNLPHSKPGNVLPKSP-KIPS 861
Cdd:pfam05109  509 PTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT-PNATSPTPAVTTPTPNATIPTLGKTSPTSAvTTPT 587
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302  862 SHEPSVSSHQTSPSLLLSKSRTPTTYSTqiPLPARPRPLVPQSLNTFSNTLSSSTSPSSTVATSIPGEPLPSPFTPTLTS 941
Cdd:pfam05109  588 PNATSPTVGETSPQANTTNHTLGGTSST--PVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS 665
                          330       340       350
                   ....*....|....*....|....*....|
gi 2208424302  942 LLPTARRWHqqdPLLGPKSTSTLPEAITLH 971
Cdd:pfam05109  666 HMPLLTSAH---PTGGENITQVTPASTSTH 692
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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