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Conserved domains on  [gi|665408191|ref|NP_001285963|]
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stolid, isoform M [Drosophila melanogaster]

Protein Classification

calcium channel subunit alpha-2/delta family protein( domain architecture ID 13750223)

calcium channel subunit alpha-2/delta family protein similar to Homo sapiens voltage-dependent calcium channel subunit alpha-2/delta-4 that regulates calcium current density and activation/inactivation kinetics of the calcium channel

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
245-428 8.35e-92

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: 293.53  E-value: 8.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  245 RTHNWFVQAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPCFKDRMVRATPDNIQ 324
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  325 EIKSAVKAIKLQDTANFTAGLEYAFSLLHK---YNQSGAGSQCNQAIMLITESTSESHKDVIKQYNWPH---MPVRIFTY 398
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 665408191  399 LIGSDSGSRSNLHDMACSNKGFFVQINDYD 428
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N super family cl07136
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
130-230 4.54e-22

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


The actual alignment was detected with superfamily member pfam08399:

Pssm-ID: 462464  Cd Length: 122  Bit Score: 92.75  E-value: 4.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   130 QHYDARRINEYNADGKLADGARhMDIRFMR----RFERLPVNLSLSSILVPHGVDLDEPDVKSALQWSGHLDPLFQNNLE 205
Cdd:pfam08399   19 QYYNAKYSNDVGEDYEKGNNVP-LSKEFVLtpnpHFYNIPVNTNYSAVHVPTNVYDRAPDVLNGINWSEALDDVFRDNYE 97
                           90       100
                   ....*....|....*....|....*
gi 665408191   206 QDPALSWQYFGSSTGFLRRFPGTAW 230
Cdd:pfam08399   98 EDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
775-1037 1.92e-13

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


The actual alignment was detected with superfamily member pfam08473:

Pssm-ID: 462488  Cd Length: 432  Bit Score: 73.95  E-value: 1.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   775 CDRALLQSLVRDAMVTDGLDRNTTgsssgKEDKQQGYQKFVVATSFVATR----SGLLRWidhvkrpEDTPEPHFSednv 850
Cdd:pfam08473   54 CNNLLNNLLLLDGGITQLLVKWWK-----KQLLNGGLLAVFAATDGGITRvppkSAGDWW-------EEAEETYES---- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   851 ramdtSWYKRAIDQHSVepdsFVYSVPFGSGYAI--KSNAT---LVTASHAIFVEHRGHKAAAGVVGLQFQhdSLAKHFI 925
Cdd:pfam08473  118 -----SFYRRSLDNDYY----FFTPPYFNSSYRPneEEDDTsgiLVSAAVELIIDGTLLKPAVVGVKLDDS--WWMEFFS 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   926 NIT--SACTGMTGCKRtcASDNLDCYVLDNSGFVIISEEMEH----TGKFFGQIDGTIMDSLVQDRIYKRVTVNDYQGVC 999
Cdd:pfam08473  187 NTTrkDQCDEECCGCK--GNDDLLCCVLDDDGGFLMMSNQDDyieqIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC 264
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 665408191  1000 sDADNPYTAAGG-------ILKPNRLGSWffnhllALSAAWLSLM 1037
Cdd:pfam08473  265 -PPKESSKAAAGrrsvvvpTIADLLNLWW------WTSAAAWSIQ 302
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
511-643 2.37e-12

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 63.94  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  511 EIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDlrplgdaNQYIdqlkpkyasvditelelpetefGNNNEPIEINKNLLNE 590
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-------KELV----------------------GKKISDDEAAEEELAK 51
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665408191  591 MrgdMIKPKEGETEFTvmnhYDDSKRVstrthrYFYGPIEDTPFTLAIVLPEK 643
Cdd:cd12912    52 K---MLAGKSGSVEYT----FNGEKKY------VAYAPIPGTGWSLVVVVPES 91
 
Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
245-428 8.35e-92

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: 293.53  E-value: 8.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  245 RTHNWFVQAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPCFKDRMVRATPDNIQ 324
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  325 EIKSAVKAIKLQDTANFTAGLEYAFSLLHK---YNQSGAGSQCNQAIMLITESTSESHKDVIKQYNWPH---MPVRIFTY 398
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 665408191  399 LIGSDSGSRSNLHDMACSNKGFFVQINDYD 428
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
130-230 4.54e-22

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


Pssm-ID: 462464  Cd Length: 122  Bit Score: 92.75  E-value: 4.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   130 QHYDARRINEYNADGKLADGARhMDIRFMR----RFERLPVNLSLSSILVPHGVDLDEPDVKSALQWSGHLDPLFQNNLE 205
Cdd:pfam08399   19 QYYNAKYSNDVGEDYEKGNNVP-LSKEFVLtpnpHFYNIPVNTNYSAVHVPTNVYDRAPDVLNGINWSEALDDVFRDNYE 97
                           90       100
                   ....*....|....*....|....*
gi 665408191   206 QDPALSWQYFGSSTGFLRRFPGTAW 230
Cdd:pfam08399   98 EDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
259-436 4.02e-15

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: 74.80  E-value: 4.02e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191    259 DIMILLDASSSMTEKSFDLGMATAFNILDTL---GEDDFVNLITFSEVVKTPVPCfkdrmvrATPDNIQEIKSAVKAIKL 335
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191    336 QDT--ANFTAGLEYAFSLLHKYNQsGAGSQCNQAIMLIT--ESTSESH--KDVIKQYNwpHMPVRIFTYLIGSDsGSRSN 409
Cdd:smart00327   74 KLGggTNLGAALQYALENLFSKSA-GSRRGAPKVVILITdgESNDGPKdlLKAAKELK--RSGVKVFVVGVGND-VDEEE 149
                           170       180
                    ....*....|....*....|....*..
gi 665408191    410 LHDMACSNKGFFVqinDYDEARRKVID 436
Cdd:smart00327  150 LKKLASAPGGVYV---FLPELLDLLID 173
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
775-1037 1.92e-13

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


Pssm-ID: 462488  Cd Length: 432  Bit Score: 73.95  E-value: 1.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   775 CDRALLQSLVRDAMVTDGLDRNTTgsssgKEDKQQGYQKFVVATSFVATR----SGLLRWidhvkrpEDTPEPHFSednv 850
Cdd:pfam08473   54 CNNLLNNLLLLDGGITQLLVKWWK-----KQLLNGGLLAVFAATDGGITRvppkSAGDWW-------EEAEETYES---- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   851 ramdtSWYKRAIDQHSVepdsFVYSVPFGSGYAI--KSNAT---LVTASHAIFVEHRGHKAAAGVVGLQFQhdSLAKHFI 925
Cdd:pfam08473  118 -----SFYRRSLDNDYY----FFTPPYFNSSYRPneEEDDTsgiLVSAAVELIIDGTLLKPAVVGVKLDDS--WWMEFFS 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   926 NIT--SACTGMTGCKRtcASDNLDCYVLDNSGFVIISEEMEH----TGKFFGQIDGTIMDSLVQDRIYKRVTVNDYQGVC 999
Cdd:pfam08473  187 NTTrkDQCDEECCGCK--GNDDLLCCVLDDDGGFLMMSNQDDyieqIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC 264
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 665408191  1000 sDADNPYTAAGG-------ILKPNRLGSWffnhllALSAAWLSLM 1037
Cdd:pfam08473  265 -PPKESSKAAAGrrsvvvpTIADLLNLWW------WTSAAAWSIQ 302
VWA pfam00092
von Willebrand factor type A domain;
259-429 4.77e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 4.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   259 DIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDF---VNLITFSEVVKTPVPcFKDrmvratPDNIQEIKSAVKAIKL 335
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDgtrVGLVQYSSDVRTEFP-LND------YSSKEELLSAVDNLRY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   336 QD--TANFTAGLEYAfslLHKYNQSGAGSQCN--QAIMLIT--ESTSESHKDVI---KQYNwphmpVRIFTylIGSDSGS 406
Cdd:pfam00092   74 LGggTTNTGKALKYA---LENLFSSAAGARPGapKVVVLLTdgRSQDGDPEEVArelKSAG-----VTVFA--VGVGNAD 143
                          170       180
                   ....*....|....*....|....
gi 665408191   407 RSNLHDMACS-NKGFFVQINDYDE 429
Cdd:pfam00092  144 DEELRKIASEpGEGHVFTVSDFEA 167
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
511-643 2.37e-12

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 63.94  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  511 EIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDlrplgdaNQYIdqlkpkyasvditelelpetefGNNNEPIEINKNLLNE 590
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-------KELV----------------------GKKISDDEAAEEELAK 51
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665408191  591 MrgdMIKPKEGETEFTvmnhYDDSKRVstrthrYFYGPIEDTPFTLAIVLPEK 643
Cdd:cd12912    52 K---MLAGKSGSVEYT----FNGEKKY------VAYAPIPGTGWSLVVVVPES 91
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
252-434 5.31e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 65.12  E-value: 5.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  252 QAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrMVRATpdNIQEIKSAVK 331
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPAT--DRAKILAAID 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  332 AIKLQDTANFTAGLEYAFSLLHKYNQSGAgsqcNQAIMLIT------ESTSESH-KDVIKQYNWPHmpVRIFTYLIGSDS 404
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTdgdanvGITDPEElLKLAEEAREEG--ITLTTLGVGSDY 232
                         170       180       190
                  ....*....|....*....|....*....|
gi 665408191  405 GsRSNLHDMACSNKGFFVQINDYDEARRKV 434
Cdd:COG2304   233 N-EDLLERLADAGGGNYYYIDDPEEAEKVF 261
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
472-562 1.63e-10

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 62.74  E-value: 1.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   472 SEYQRRLVTTVSTPVFDRRNhsvrvaNLLGVVGTDVPIEEIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDLRPL-GDANQ 550
Cdd:pfam02743  120 SSESGEPVLTIARPIYDDDG------EVIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLrSLLAP 193
                           90
                   ....*....|..
gi 665408191   551 YIDQLKPKYASV 562
Cdd:pfam02743  194 FLGKSLADALPG 205
 
Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
245-428 8.35e-92

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: 293.53  E-value: 8.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  245 RTHNWFVQAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPCFKDRMVRATPDNIQ 324
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  325 EIKSAVKAIKLQDTANFTAGLEYAFSLLHK---YNQSGAGSQCNQAIMLITESTSESHKDVIKQYNWPH---MPVRIFTY 398
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 665408191  399 LIGSDSGSRSNLHDMACSNKGFFVQINDYD 428
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
130-230 4.54e-22

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


Pssm-ID: 462464  Cd Length: 122  Bit Score: 92.75  E-value: 4.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   130 QHYDARRINEYNADGKLADGARhMDIRFMR----RFERLPVNLSLSSILVPHGVDLDEPDVKSALQWSGHLDPLFQNNLE 205
Cdd:pfam08399   19 QYYNAKYSNDVGEDYEKGNNVP-LSKEFVLtpnpHFYNIPVNTNYSAVHVPTNVYDRAPDVLNGINWSEALDDVFRDNYE 97
                           90       100
                   ....*....|....*....|....*
gi 665408191   206 QDPALSWQYFGSSTGFLRRFPGTAW 230
Cdd:pfam08399   98 EDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
259-436 4.02e-15

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: 74.80  E-value: 4.02e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191    259 DIMILLDASSSMTEKSFDLGMATAFNILDTL---GEDDFVNLITFSEVVKTPVPCfkdrmvrATPDNIQEIKSAVKAIKL 335
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191    336 QDT--ANFTAGLEYAFSLLHKYNQsGAGSQCNQAIMLIT--ESTSESH--KDVIKQYNwpHMPVRIFTYLIGSDsGSRSN 409
Cdd:smart00327   74 KLGggTNLGAALQYALENLFSKSA-GSRRGAPKVVILITdgESNDGPKdlLKAAKELK--RSGVKVFVVGVGND-VDEEE 149
                           170       180
                    ....*....|....*....|....*..
gi 665408191    410 LHDMACSNKGFFVqinDYDEARRKVID 436
Cdd:smart00327  150 LKKLASAPGGVYV---FLPELLDLLID 173
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
775-1037 1.92e-13

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


Pssm-ID: 462488  Cd Length: 432  Bit Score: 73.95  E-value: 1.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   775 CDRALLQSLVRDAMVTDGLDRNTTgsssgKEDKQQGYQKFVVATSFVATR----SGLLRWidhvkrpEDTPEPHFSednv 850
Cdd:pfam08473   54 CNNLLNNLLLLDGGITQLLVKWWK-----KQLLNGGLLAVFAATDGGITRvppkSAGDWW-------EEAEETYES---- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   851 ramdtSWYKRAIDQHSVepdsFVYSVPFGSGYAI--KSNAT---LVTASHAIFVEHRGHKAAAGVVGLQFQhdSLAKHFI 925
Cdd:pfam08473  118 -----SFYRRSLDNDYY----FFTPPYFNSSYRPneEEDDTsgiLVSAAVELIIDGTLLKPAVVGVKLDDS--WWMEFFS 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   926 NIT--SACTGMTGCKRtcASDNLDCYVLDNSGFVIISEEMEH----TGKFFGQIDGTIMDSLVQDRIYKRVTVNDYQGVC 999
Cdd:pfam08473  187 NTTrkDQCDEECCGCK--GNDDLLCCVLDDDGGFLMMSNQDDyieqIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC 264
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 665408191  1000 sDADNPYTAAGG-------ILKPNRLGSWffnhllALSAAWLSLM 1037
Cdd:pfam08473  265 -PPKESSKAAAGrrsvvvpTIADLLNLWW------WTSAAAWSIQ 302
VWA pfam00092
von Willebrand factor type A domain;
259-429 4.77e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 4.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   259 DIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDF---VNLITFSEVVKTPVPcFKDrmvratPDNIQEIKSAVKAIKL 335
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDgtrVGLVQYSSDVRTEFP-LND------YSSKEELLSAVDNLRY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   336 QD--TANFTAGLEYAfslLHKYNQSGAGSQCN--QAIMLIT--ESTSESHKDVI---KQYNwphmpVRIFTylIGSDSGS 406
Cdd:pfam00092   74 LGggTTNTGKALKYA---LENLFSSAAGARPGapKVVVLLTdgRSQDGDPEEVArelKSAG-----VTVFA--VGVGNAD 143
                          170       180
                   ....*....|....*....|....
gi 665408191   407 RSNLHDMACS-NKGFFVQINDYDE 429
Cdd:pfam00092  144 DEELRKIASEpGEGHVFTVSDFEA 167
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
257-436 1.32e-12

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: 67.24  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  257 PKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTpvpcFKDRMVRATPDNIQEIKSAVKAIKLQ 336
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEE----FSPSSVSATAENVAAAIEYVNRLQAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  337 DTANFTAGLEYAFSLLhkYNQSGAGSQcnqaIMLIT--ESTSESH--KDVIKQYNWPHmpvRIFTYLIGSDSgSRSNLHD 412
Cdd:cd01461    78 GGTNMNDALEAALELL--NSSPGSVPQ----IILLTdgEVTNESQilKNVREALSGRI---RLFTFGIGSDV-NTYLLER 147
                         170       180
                  ....*....|....*....|....
gi 665408191  413 MACSNKGFFVQINDYDEARRKVID 436
Cdd:cd01461   148 LAREGRGIARRIYETDDIESQLLR 171
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
511-643 2.37e-12

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 63.94  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  511 EIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDlrplgdaNQYIdqlkpkyasvditelelpetefGNNNEPIEINKNLLNE 590
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-------KELV----------------------GKKISDDEAAEEELAK 51
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665408191  591 MrgdMIKPKEGETEFTvmnhYDDSKRVstrthrYFYGPIEDTPFTLAIVLPEK 643
Cdd:cd12912    52 K---MLAGKSGSVEYT----FNGEKKY------VAYAPIPGTGWSLVVVVPES 91
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
259-422 2.42e-12

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: 66.05  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  259 DIMILLDASSSMTEKSFDLGMATAFNILDTL---GEDDFVNLITFSEVVKTPVPCFKDRmvraTPDNIQEIKSAVKAIKL 335
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDT----DKADLLEAIDALKKGLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  336 QDTaNFTAGLEYAFSLLHKYNQSGAGsqcnQAIMLITESTSESH----KDVIKQYNWPHmpVRIFTYLIGSDsGSRSNLH 411
Cdd:cd00198    78 GGT-NIGAALRLALELLKSAKRPNAR----RVIILLTDGEPNDGpellAEAARELRKLG--ITVYTIGIGDD-ANEDELK 149
                         170
                  ....*....|..
gi 665408191  412 DMA-CSNKGFFV 422
Cdd:cd00198   150 EIAdKTTGGAVF 161
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
252-434 5.31e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 65.12  E-value: 5.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  252 QAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrMVRATpdNIQEIKSAVK 331
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPAT--DRAKILAAID 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  332 AIKLQDTANFTAGLEYAFSLLHKYNQSGAgsqcNQAIMLIT------ESTSESH-KDVIKQYNWPHmpVRIFTYLIGSDS 404
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTdgdanvGITDPEElLKLAEEAREEG--ITLTTLGVGSDY 232
                         170       180       190
                  ....*....|....*....|....*....|
gi 665408191  405 GsRSNLHDMACSNKGFFVQINDYDEARRKV 434
Cdd:COG2304   233 N-EDLLERLADAGGGNYYYIDDPEEAEKVF 261
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
472-562 1.63e-10

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 62.74  E-value: 1.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   472 SEYQRRLVTTVSTPVFDRRNhsvrvaNLLGVVGTDVPIEEIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDLRPL-GDANQ 550
Cdd:pfam02743  120 SSESGEPVLTIARPIYDDDG------EVIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLrSLLAP 193
                           90
                   ....*....|..
gi 665408191   551 YIDQLKPKYASV 562
Cdd:pfam02743  194 FLGKSLADALPG 205
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
511-642 3.85e-10

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 57.84  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  511 EIRKVIPQHKLGPNGYSFIVDNNGRVLYHPDLRPLGdanqyidqlkpkyasvditelelpetefgnnnepIEINKNLLNE 590
Cdd:cd18774     1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVG----------------------------------KGKSLDDLAL 46
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665408191  591 MRGDMIKPKEGETEFTVmnhYDDSKRVstrthrYFYGPIEDTPFTLAIVLPE 642
Cdd:cd18774    47 LAALLLAGESGTFEYTS---DDGVERL------VAYRPVPGTPWVVVVGVPE 89
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
240-406 2.03e-09

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 60.08  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  240 LIHDFRTHNWFVQAASSPKDIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrmvRAT 319
Cdd:COG2425   101 AALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLP-------LTA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  320 PDNIQEIKSAVKAIKLQDTANFTAGLEYAFSLLHKYNQSGAgsqcnqAIMLIT--ESTSEShKDVIKQYNWPHMPVRIFT 397
Cdd:COG2425   174 DDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNA------DIVLITdgEAGVSP-EELLREVRAKESGVRLFT 246

                  ....*....
gi 665408191  398 YLIGSDSGS 406
Cdd:COG2425   247 VAIGDAGNP 255
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
180-429 5.24e-09

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: 58.80  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  180 DLDEPDVKSALQWSGHLDPLFQNNLEQDPALSWQYFGSSTGFLRRFPGTAWPPEGSKGSKLIHDFRTHNWFVQAASSPKD 259
Cdd:COG1240    15 LALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  260 IMILLDASSSMTEKS-FDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrmvraTPDNIQEIKSAVKAIKLQDT 338
Cdd:COG1240    95 VVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP---------LTRDREALKRALDELPPGGG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  339 ANFTAGLEYAFSLLHKYNQSGagsqcNQAIMLIT--ESTSESH--KDVIKQYNwpHMPVRIFTYLIGSDSGSRSNLHDMA 414
Cdd:COG1240   166 TPLGDALALALELLKRADPAR-----RKVIVLLTdgRDNAGRIdpLEAAELAA--AAGIRIYTIGVGTEAVDEGLLREIA 238
                         250
                  ....*....|....*
gi 665408191  415 CSNKGFFVQINDYDE 429
Cdd:COG1240   239 EATGGRYFRADDLSE 253
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
263-372 1.95e-07

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: 52.28  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  263 LLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrMVRATpdNIQEIKSAVKAIKLQDTANFT 342
Cdd:cd01465     6 VIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLP-----ATPVR--DKAAILAAIDRLTAGGSTAGG 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 665408191  343 AGLEYAFsllhKYNQSGAGSQCNQAIMLIT 372
Cdd:cd01465    79 AGIQLGY----QEAQKHFVPGGVNRILLAT 104
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
259-421 4.83e-07

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: 50.85  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  259 DIMILLDASSSMTEKSFDLGMATAFNILDTLGEDDFVNLITFSEVVKTPVPcfkdrMVRATPDNIQEIKSAVKAIKLQDT 338
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGLQAGGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  339 ANFTAGLEYAFSLLHKYNQSGAGSqcnqAIMLITESTSESHKDVIKQYNwphMPVRIFTYLIGSDSGSrSNLHDMACSNK 418
Cdd:cd01466    77 TNVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQDNHGAVVLRADN---APIPIHTFGLGASHDP-ALLAFIAEITG 148

                  ...
gi 665408191  419 GFF 421
Cdd:cd01466   149 GTF 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
259-384 6.02e-07

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: 50.75  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  259 DIMILLDASSSMTEKSFDLGMATAFNILDTL---GEDDFVNLITFSEVVKTPVPcFKDrmvratPDNIQEIKSAVKAIKL 335
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVRVEFS-LND------YKSKDDLLKAVKNLKY 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665408191  336 QD-TANFT-AGLEYAFSLLhkYNQSGAGSQCNQAIMLITESTSESHKDVIK 384
Cdd:cd01450    75 LGgGGTNTgKALQYALEQL--FSESNARENVPKVIIVLTDGRSDDGGDPKE 123
VWA_2 pfam13519
von Willebrand factor type A domain;
260-354 3.63e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.90  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   260 IMILLDASSSMTEKSFD---LGMATAF--NILDTLGEdDFVNLITFSEVVKTPVPCFKDRmvratpdniQEIKSAVKAIK 334
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGptrLEAAKDAvlALLKSLPG-DRVGLVTFGDGPEVLIPLTKDR---------AKILRALRRLE 70
                           90       100
                   ....*....|....*....|.
gi 665408191   335 -LQDTANFTAGLEYAFSLLHK 354
Cdd:pfam13519   71 pKGGGTNLAAALQLARAALKH 91
VWA_3 pfam13768
von Willebrand factor type A domain;
258-422 5.49e-06

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 47.78  E-value: 5.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   258 KDIMILLDASSSMteKSFDLGMATAFNILD-TLGEDDFVNLITFSEvvkTPVPCFKDRMVrATPDNIQEIKSAVKAIKLQ 336
Cdd:pfam13768    1 GDVVIVVDVSSSM--SGEPKLQKDALSVALrQLPTGDKFAVLGFGT---LPRPLFPGWRV-VSPRSLQEAFQFIKTLQPP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191   337 DTA-NFTAGLEYAFSLLHKynqsgagSQCNQAIMLITESTSESHKDVIKQYNWPHM-PVRIFTYLIGSdSGSRSNLHDMA 414
Cdd:pfam13768   75 LGGsDLLGALKEAVRAPAS-------PGYIRHVLLLTDGSPMQGETRVSDLISRAPgKIRFFAYGLGA-SISAPMLQLLA 146

                   ....*...
gi 665408191   415 CSNKGFFV 422
Cdd:pfam13768  147 EASNGTYE 154
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
258-377 2.49e-03

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 39.90  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408191  258 KDIMILLDASSSM------TEKSFDLGMATAFNIldtlGEDDF-VNLITFSEVVKTPVPcfkdrmvRATPDNIQEIKSAV 330
Cdd:cd01472     1 ADIVFLVDGSESIglsnfnLVKDFVKRVVERLDI----GPDGVrVGVVQYSDDPRTEFY-------LNTYRSKDDVLEAV 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 665408191  331 KAIKLQDTANFT-AGLEYAF-SLLHKynQSGAGSQCNQAIMLITESTSE 377
Cdd:cd01472    70 KNLRYIGGGTNTgKALKYVReNLFTE--ASGSREGVPKVLVVITDGKSQ 116
 
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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