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Conserved domains on  [gi|1907101985|ref|XP_036014573|]
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protein mono-ADP-ribosyltransferase PARP4 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 144-308 1.14e-18

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


:

Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  144 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 223
Cdd:COG2425    100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  224 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 299
Cdd:COG2425    176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                   ....*....
gi 1907101985  300 RHILRTLSQ 308
Cdd:COG2425    255 PGLLEALAD 263
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 669-812 2.62e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


:

Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  669 PPHPLGGTHPPPPLPLPDGTHLPSPLFGSTH--PPPPLFGGTLIPPPSSlfggthlppppplpggthipppppIPGGTLI 746
Cdd:pfam06346    2 PPPPLPGDSSTIPLPPGACIPTPPPLPGGGGppPPPPLPGSAAIPPPPP------------------------LPGGTSI 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907101985  747 PPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGthlppppllpAGTHIPPPPPITGSTHPPPPSSL 812
Cdd:pfam06346   58 PPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGG----------AGIPPPPPPLPGGAGVPPPPPPL 113
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 746-915 2.72e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


:

Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  746 IPPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLfggthlppppplp 825
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPL------------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  826 ggthipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPi 905
Cdd:pfam06346   88 ----------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP- 133

                          170
                   ....*....|
gi 1907101985  906 gfIPPKLGPP 915
Cdd:pfam06346  134 --PPPGMGMP 141
VIT super family cl48021
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-23 5.57e-06

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 pfam08487:

Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 46.32  E-value: 5.57e-06
                           10        20
                   ....*....|....*....|...
gi 1907101985    1 MDVFTVSVGNLPPRAKVLIKITY 23
Cdd:pfam08487   89 PDVFTTSVGNIPPGEKVTVELTY 111
 
Name Accession Description Interval E-value
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 144-308 1.14e-18

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  144 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 223
Cdd:COG2425    100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  224 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 299
Cdd:COG2425    176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                   ....*....
gi 1907101985  300 RHILRTLSQ 308
Cdd:COG2425    255 PGLLEALAD 263
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-323 1.93e-17

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: 81.35  E-value: 1.93e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985   167 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKCiTDSKMATEFIMSAAPSM-GNTD 242
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdrVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985   243 FWKVLRYLS--LLYPSEGFRN-----ILLISDGHLQSESLTLQLVKRNIQHTRV--FTCAVGSTANRHILRTLSQCGAGV 313
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKDLLKAAKELKRSGVkvFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 1907101985   314 FEYFNSKSKH 323
Cdd:smart00327  161 YVFLPELLDL 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 167-316 3.06e-15

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: 74.52  E-value: 3.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  167 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQ---KVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDF 243
Cdd:cd00198      3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907101985  244 WKVLRYLSLLYPSEGFRN----ILLISDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 316
Cdd:cd00198     83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARELRklGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
VWA_3 pfam13768
von Willebrand factor type A domain;
165-315 6.42e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 67.81  E-value: 6.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  165 NEVIICLDCSSSMEGVTFTQAKqvalyALSL----LGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFIMSAAPSM 238
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKD-----ALSValrqLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPL 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907101985  239 GNTDFWKVLRY-LSLLYPSEGFRNILLISDGH-LQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFE 315
Cdd:pfam13768   76 GGSDLLGALKEaVRAPASPGYIRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 669-812 2.62e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  669 PPHPLGGTHPPPPLPLPDGTHLPSPLFGSTH--PPPPLFGGTLIPPPSSlfggthlppppplpggthipppppIPGGTLI 746
Cdd:pfam06346    2 PPPPLPGDSSTIPLPPGACIPTPPPLPGGGGppPPPPLPGSAAIPPPPP------------------------LPGGTSI 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907101985  747 PPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGthlppppllpAGTHIPPPPPITGSTHPPPPSSL 812
Cdd:pfam06346   58 PPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGG----------AGIPPPPPPLPGGAGVPPPPPPL 113
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 746-915 2.72e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  746 IPPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLfggthlppppplp 825
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPL------------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  826 ggthipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPi 905
Cdd:pfam06346   88 ----------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP- 133

                          170
                   ....*....|
gi 1907101985  906 gfIPPKLGPP 915
Cdd:pfam06346  134 --PPPGMGMP 141
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-23 5.57e-06

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.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 46.32  E-value: 5.57e-06
                           10        20
                   ....*....|....*....|...
gi 1907101985    1 MDVFTVSVGNLPPRAKVLIKITY 23
Cdd:pfam08487   89 PDVFTTSVGNIPPGEKVTVELTY 111
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-25 3.04e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 39.26  E-value: 3.04e-03
                            10        20
                    ....*....|....*....|....*
gi 1907101985     1 MDVFTVSVgNLPPRAKVLIKITYIT 25
Cdd:smart00609  107 MEQFTVSV-NVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 144-308 1.14e-18

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  144 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 223
Cdd:COG2425    100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  224 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 299
Cdd:COG2425    176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                   ....*....
gi 1907101985  300 RHILRTLSQ 308
Cdd:COG2425    255 PGLLEALAD 263
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-323 1.93e-17

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: 81.35  E-value: 1.93e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985   167 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKCiTDSKMATEFIMSAAPSM-GNTD 242
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdrVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985   243 FWKVLRYLS--LLYPSEGFRN-----ILLISDGHLQSESLTLQLVKRNIQHTRV--FTCAVGSTANRHILRTLSQCGAGV 313
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKDLLKAAKELKRSGVkvFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 1907101985   314 FEYFNSKSKH 323
Cdd:smart00327  161 YVFLPELLDL 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 167-316 3.06e-15

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: 74.52  E-value: 3.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  167 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQ---KVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDF 243
Cdd:cd00198      3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907101985  244 WKVLRYLSLLYPSEGFRN----ILLISDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 316
Cdd:cd00198     83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARELRklGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 166-335 2.18e-14

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: 72.25  E-value: 2.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFI--MSAapsMGNT 241
Cdd:cd01461      4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVaaAIEYVnrLQA---LGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  242 DFWKVL-RYLSLLYPSEG-FRNILLISDGHLQSESLTLQLVKRNIQHT-RVFTCAVGSTANRHILRTLSQCGAGVFEYFN 318
Cdd:cd01461     81 NMNDALeAALELLNSSPGsVPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                          170
                   ....*....|....*..
gi 1907101985  319 SKSkhswkkQIEAQMTR 335
Cdd:cd01461    161 ETD------DIESQLLR 171
VWA_3 pfam13768
von Willebrand factor type A domain;
165-315 6.42e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 67.81  E-value: 6.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  165 NEVIICLDCSSSMEGVTFTQAKqvalyALSL----LGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFIMSAAPSM 238
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKD-----ALSValrqLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPL 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907101985  239 GNTDFWKVLRY-LSLLYPSEGFRNILLISDGH-LQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFE 315
Cdd:pfam13768   76 GGSDLLGALKEaVRAPASPGYIRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 166-338 6.23e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 67.82  E-value: 6.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSyPKCITDSKMATEFIMSAAPSmGNTDFWK 245
Cdd:COG2304     93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATDRAKILAAIDRLQAG-GGTALGA 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  246 VLRY-LSLL--YPSEGFRN-ILLISDGH----LQSESLTLQLVKRNIQ-HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 316
Cdd:COG2304    171 GLELaYELArkHFIPGRVNrVILLTDGDanvgITDPEELLKLAEEAREeGITLTTLGVGSDYNEDLLERLADAGGGNYYY 250

                          170       180
                   ....*....|....*....|..
gi 1907101985  317 FNSKSkhswkkQIEAQMTRIRS 338
Cdd:COG2304    251 IDDPE------EAEKVFVREFS 266
VWA pfam00092
von Willebrand factor type A domain;
166-322 3.37e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 63.45  E-value: 3.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKcITDSKMATEFIMSAAPSMGNTD 242
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDgtrVGLVQYSSDVRTEFPLND-YSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  243 F-WKVLRYL--SLLYPSEGFR-----NILLISDGHLQSESLT--LQLVKRniQHTRVFTCAVGSTANRHiLRTLSQCGAG 312
Cdd:pfam00092   80 NtGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKS--AGVTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 1907101985  313 VFEYFNSKSK 322
Cdd:pfam00092  157 GHVFTVSDFE 166
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 669-812 2.62e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  669 PPHPLGGTHPPPPLPLPDGTHLPSPLFGSTH--PPPPLFGGTLIPPPSSlfggthlppppplpggthipppppIPGGTLI 746
Cdd:pfam06346    2 PPPPLPGDSSTIPLPPGACIPTPPPLPGGGGppPPPPLPGSAAIPPPPP------------------------LPGGTSI 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907101985  747 PPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGthlppppllpAGTHIPPPPPITGSTHPPPPSSL 812
Cdd:pfam06346   58 PPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGG----------AGIPPPPPPLPGGAGVPPPPPPL 113
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 746-915 2.72e-07

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 51.41  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  746 IPPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLfggthlppppplp 825
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPL------------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  826 ggthipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPi 905
Cdd:pfam06346   88 ----------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP- 133

                          170
                   ....*....|
gi 1907101985  906 gfIPPKLGPP 915
Cdd:pfam06346  134 --PPPGMGMP 141
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 110-318 3.60e-07

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: 53.02  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  110 EGSSLDSGGFSLHIGLRDAYLPRMWVEKHPEKESEACMLVFQPELADVLPDLRGKNEVIICLDCSSSMEGVT-FTQAKQV 188
Cdd:COG1240     38 LLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  189 ALYALSLLGEEQKVNIMQFGTGYKELFSYPkciTDSKMATEFIMSAAPSmGNTDFWKVLRY-LSLL--YPSEGFRNILLI 265
Cdd:COG1240    118 LLDFLDDYRPRDRVGLVAFGGEAEVLLPLT---RDREALKRALDELPPG-GGTPLGDALALaLELLkrADPARRKVIVLL 193

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907101985  266 SDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTA-NRHILRTLSQCGAGvfEYFN 318
Cdd:COG1240    194 TDGRDNAGRIDPLEAAELAAaaGIRIYTIGVGTEAvDEGLLREIAEATGG--RYFR 247
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
166-307 3.71e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.15  E-value: 3.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQV------ALYALSLLGEEQKVNIMQFGTGYKELfsYPkcITDskmATEFIMSAAPSMG 239
Cdd:COG4245      7 PVYLLLDTSGSMSGEPIEALNEGlqalidELRQDPYALETVEVSVITFDGEAKVL--LP--LTD---LEDFQPPDLSASG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  240 NTDFWKVLRYL-------SLLYPSEGFRN----ILLISDGHLQSESLT--LQLVKRNIQHTRV--FTCAVGSTANRHILR 304
Cdd:COG4245     80 GTPLGAALELLldlierrVQKYTAEGKGDwrpvVFLITDGEPTDSDWEaaLQRLKDGEAAKKAniFAIGVGPDADTEVLK 159


                   ...
gi 1907101985  305 TLS 307
Cdd:COG4245    160 QLT 162
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-23 5.57e-06

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.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 46.32  E-value: 5.57e-06
                           10        20
                   ....*....|....*....|...
gi 1907101985    1 MDVFTVSVGNLPPRAKVLIKITY 23
Cdd:pfam08487   89 PDVFTTSVGNIPPGEKVTVELTY 111
VWA_2 pfam13519
von Willebrand factor type A domain;
167-265 3.70e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.82  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  167 VIICLDCSSSMEGVT-----FTQAKQVALYALSLLGeEQKVNIMQFGTGYkELFSYPKciTDSKMATEFIMSAAPSMGNT 241
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLP-GDRVGLVTFGDGP-EVLIPLT--KDRAKILRALRRLEPKGGGT 76

                           90       100
                   ....*....|....*....|....*..
gi 1907101985  242 DFWKVLRYLSLLYPSEGFRN---ILLI 265
Cdd:pfam13519   77 NLAAALQLARAALKHRRKNQprrIVLI 103
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 166-299 4.00e-04

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 42.33  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQVAL-YALSLLGEEQKVNIMQFGTGYkELFSYPKCITDSKmATEFIMsAAPSMGNTDFW 244
Cdd:cd01462      2 PVILLVDQSGSMYGAPEEVAKAVALaLLRIALAENRDTYLILFDSEF-QTKIVDKTDDLEE-PVEFLS-GVQLGGGTDIN 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  245 KVLRYLSLLYPSEGFRN--ILLISDGH---LQSESLTLQLVKRNIQHtRVFTCAVGSTAN 299
Cdd:cd01462     79 KALRYALELIERRDPRKadIVLITDGYeggVSDELLREVELKRSRVA-RFVALALGDHGN 137
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 166-298 4.07e-04

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: 42.77  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  166 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGtgyKELFSYPKCITDSKMA------TEFI--MSAAPS 237
Cdd:cd01463     15 DIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFS---NEVNPVVPCFNDTLVQattsnkKVLKeaLDMLEA 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907101985  238 MGNTDFWKVLRY-LSLLYP----------SEGFRNILLISDGhlQSESLTLQLVKRNIQH-----TRVFTCAVGSTA 298
Cdd:cd01463     92 KGIANYTKALEFaFSLLLKnlqsnhsgsrSQCNQAIMLITDG--VPENYKEIFDKYNWDKnseipVRVFTYLIGREV 166
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 664-779 1.42e-03

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  664 IPSSLPPHPLGGTHPPPPLPLPDGTHLPSPLFGSTH--PPPPLFGGTLIPPPSSLfggthlppppplPGGTHIPPPPPIP 741
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSipPPPPLPGAASIPPPPPL------------PGSTGIPPPPPLP 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907101985  742 GGTLI-PPSSSLFGGTHL-PPPPLLSAGTHIPPPPLLSAG 779
Cdd:pfam06346   89 GGAGIpPPPPPLPGGAGVpPPPPPLPGGPGIPPPPPFPGG 128
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 842-938 2.19e-03

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 40.24  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  842 IPSPSSLFGGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPagtqfsLSPIGFIPPklgPPKLShsh 921
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPP------LPGSTGIPP---PPPLP--- 88

                           90
                   ....*....|....*..
gi 1907101985  922 klvGDTNIHDSEPPLLG 938
Cdd:pfam06346   89 ---GGAGIPPPPPPLPG 102
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-25 3.04e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 39.26  E-value: 3.04e-03
                            10        20
                    ....*....|....*....|....*
gi 1907101985     1 MDVFTVSVgNLPPRAKVLIKITYIT 25
Cdd:smart00609  107 MEQFTVSV-NVAPGSKVTFELTYEE 130
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 167-316 7.24e-03

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: 38.52  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907101985  167 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDFWKV 246
Cdd:cd01466      3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907101985  247 LRY-LSLLypseGFR-------NILLISDGhlqSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFEY 316
Cdd:cd01466     83 LKKaLKVL----GDRrqknpvaSIMLLSDG---QDNHGAVVLRADNAPIPIHTFGLGASHDPALLAFIAEITGGTFSY 153
 
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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