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Conserved domains on  [gi|54112394|ref|NP_006021|]
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voltage-dependent calcium channel subunit alpha-2/delta-2 isoform b precursor [Homo sapiens]

Protein Classification

vWA_VGCC_like and VGCC_alpha2 domain-containing protein( domain architecture ID 13750239)

protein containing domains VWA_N, vWA_VGCC_like, HK_sensor, and VGCC_alpha2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 662-1104 0e+00

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: 689.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    662 YFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVErVWRDQ 741
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    742 DLNtYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAV 821
Cdd:pfam08473   80 LLN-GGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEEDDTSGILVSAAV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    822 ELSLGRRTLRPAVVGVKLDLEAWAEKFkvLASNRTHQDQPQKCGpnshcemdCEVNNEDLLCVLIDDGGFLVLSNQNHQW 901
Cdd:pfam08473  159 ELIIDGTLLKPAVVGVKLDDSWWMEFF--SNTTRKDQCDEECCG--------CKGNDDLLCCVLDDDGGFLMMSNQDDYI 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    902 DQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYG 981
Cdd:pfam08473  229 EQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVS 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    982 LIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAE-KPLCSQCEA 1060
Cdd:pfam08473  309 LTFPSFLAAEDVADEIMDAMKEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADaKGTCSSCDS 388

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 54112394   1061 GRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCG 1104
Cdd:pfam08473  389 MLLQQAEQSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 277-456 1.14e-77

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: 253.47  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  277 RRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQP-VSCFTH-LVQANVRNKK 354
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  355 VFKEAVQGMVAKGTTGYKAGFEYAFDQLQ-----NSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRT---VRVFTF 426
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSeipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112394  427 SVGQHNYDVTPLQWMACANKGYYFEIPSIG 456
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 141-265 7.76e-50

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: 172.10  E-value: 7.76e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    141 AENFQKAHRWQDNIkEEDIVYYDAKADAELDDPESEDVERGSkasTLRLDFIEDPNFKNK-VNYSYAAVQIPTDIYKGST 219
Cdd:pfam08399    1 AEKAAEDHEWNDNV-PNDFQYYNAKYSNDVGEDYEKGNNVPL---SKEFVLTPNPHFYNIpVNTNYSAVHVPTNVYDRAP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 54112394    220 VILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPW 265
Cdd:pfam08399   77 DVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 533-642 1.60e-07

Sensor domains of Histidine Kinase receptors; 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.


The actual alignment was detected with superfamily member cd12912:

Pssm-ID: 365792 [Multi-domain]  Cd Length: 92  Bit Score: 50.07  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  533 DIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNfrepvtldfldAELEDENKEEIRRSMIDGNKGHKQIRtlvks 612
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPDKELVGKK-----------ISDDEAAEEELAKKMLAGKSGSVEYT----- 64

                         90       100       110
                 ....*....|....*....|....*....|
gi 54112394  613 lderyIDEVTRNYTWVPIRSTNYSLGLVLP 642
Cdd:cd12912   65 -----FNGEKKYVAYAPIPGTGWSLVVVVP 89
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 448-531 7.94e-03

Sensor domains of Histidine Kinase receptors; 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.


The actual alignment was detected with superfamily member cd12913:

Pssm-ID: 365792  Cd Length: 139  Bit Score: 37.89  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  448 YYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLG-LVVTGTLPVFnltqdgpgeKKNQLIlGVMG 526
Cdd:cd12913   65 PYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGvLMITISVPIY---------DNGKFI-GVVG 134


                 ....*
gi 54112394  527 IDVAL 531
Cdd:cd12913  135 VDISL 139
 
Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 662-1104 0e+00

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: 689.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    662 YFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVErVWRDQ 741
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    742 DLNtYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAV 821
Cdd:pfam08473   80 LLN-GGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEEDDTSGILVSAAV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    822 ELSLGRRTLRPAVVGVKLDLEAWAEKFkvLASNRTHQDQPQKCGpnshcemdCEVNNEDLLCVLIDDGGFLVLSNQNHQW 901
Cdd:pfam08473  159 ELIIDGTLLKPAVVGVKLDDSWWMEFF--SNTTRKDQCDEECCG--------CKGNDDLLCCVLDDDGGFLMMSNQDDYI 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    902 DQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYG 981
Cdd:pfam08473  229 EQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVS 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    982 LIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAE-KPLCSQCEA 1060
Cdd:pfam08473  309 LTFPSFLAAEDVADEIMDAMKEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADaKGTCSSCDS 388

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 54112394   1061 GRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCG 1104
Cdd:pfam08473  389 MLLQQAEQSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 277-456 1.14e-77

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: 253.47  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  277 RRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQP-VSCFTH-LVQANVRNKK 354
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  355 VFKEAVQGMVAKGTTGYKAGFEYAFDQLQ-----NSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRT---VRVFTF 426
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSeipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112394  427 SVGQHNYDVTPLQWMACANKGYYFEIPSIG 456
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 141-265 7.76e-50

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: 172.10  E-value: 7.76e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    141 AENFQKAHRWQDNIkEEDIVYYDAKADAELDDPESEDVERGSkasTLRLDFIEDPNFKNK-VNYSYAAVQIPTDIYKGST 219
Cdd:pfam08399    1 AEKAAEDHEWNDNV-PNDFQYYNAKYSNDVGEDYEKGNNVPL---SKEFVLTPNPHFYNIpVNTNYSAVHVPTNVYDRAP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 54112394    220 VILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPW 265
Cdd:pfam08399   77 DVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 291-455 9.25e-19

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: 84.81  E-value: 9.25e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394     291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMV--A 365
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLSykL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394     366 KGTTGYKAGFEYAFDQLQNSNIT-RANCNKMIMMFTDG----GEDRVQDVFEKYNwpNRTVRVFTFSVGQHnYDVTPLQW 440
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAGsRRGAPKVVILITDGesndGPKDLLKAAKELK--RSGVKVFVVGVGND-VDEEELKK 152

                           170
                    ....*....|....*
gi 54112394     441 MACANKGYYFEIPSI 455
Cdd:smart00327  153 LASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 289-488 4.74e-17

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 82.84  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  289 PKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHlvqanVRNKKVFKEAVQGMVAKGT 368
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRLQAGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  369 TGYKAGFEYAFDQLQNSNITRANcNKMIMMfTDG-------GEDRVQDVFEKYNwpNRTVRVFTFSVGQhNYDVTPLQWM 441
Cdd:COG2304  166 TALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvgitDPEELLKLAEEAR--EEGITLTTLGVGS-DYNEDLLERL 240

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 54112394  442 ACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNV 488
Cdd:COG2304  241 ADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPYGTL 287
VWA pfam00092
von Willebrand factor type A domain;
291-458 9.96e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.69  E-value: 9.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMVAK- 366
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLg 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    367 -GTTGYKAGFEYAFDQLQNSNI-TRANCNKMIMMFTDG--GEDRVQDVFEKYNwpNRTVRVFTFSVGQHnyDVTPLQWMA 442
Cdd:pfam00092   76 gGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGrsQDGDPEEVARELK--SAGVTVFAVGVGNA--DDEELRKIA 151

                          170
                   ....*....|....*..
gi 54112394    443 C-ANKGYYFEIPSIGAI 458
Cdd:pfam00092  152 SePGEGHVFTVSDFEAL 168
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 533-642 1.60e-07

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: 50.07  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  533 DIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNfrepvtldfldAELEDENKEEIRRSMIDGNKGHKQIRtlvks 612
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPDKELVGKK-----------ISDDEAAEEELAKKMLAGKSGSVEYT----- 64

                         90       100       110
                 ....*....|....*....|....*....|
gi 54112394  613 lderyIDEVTRNYTWVPIRSTNYSLGLVLP 642
Cdd:cd12912   65 -----FNGEKKYVAYAPIPGTGWSLVVVVP 89
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 474-612 3.57e-06

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: 49.64  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    474 VLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFnltqDGPGEkknqlILGVMGIDVALNDIKRLTPNYTLGANGYVFAID 553
Cdd:pfam02743  103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIY----DDDGE-----VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVD 173

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 54112394    554 LNGYVLLHPNLKPQTTnfrepVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKS 612
Cdd:pfam02743  174 SDGRILAHPLGKNLRS-----LLAPFLGKSLADALPGSGITEIAVDLDGEDYLVAYAPI 227
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 289-409 9.88e-04

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 42.68  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    289 PKDMVIIVDVSGSVSGLtLKLMKTSVCEMLDT-LSDDDYVNVASFNEKAQPVSCFTH--------LVQANVRNKKVFKEA 359
Cdd:TIGR03436   53 PLTVGLVIDTSGSMRND-LDRARAAAIRFLKTvLRPNDRVFVVTFNTRLRLLQDFTSdprlleaaLNRLKPPLRTDYNSS 131

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 54112394    360 VQGMVAKGTTG-YKAGFEYAFDQLQNSNiTRANCNKMIMMFTDGGEDRVQD 409
Cdd:TIGR03436  132 GAFVRDGGGTAlYDAITLAALEQLANAL-AGIPGRKALIVISDGGDNRSRD 181
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 448-531 7.94e-03

first 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 first 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: 350338  Cd Length: 139  Bit Score: 37.89  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  448 YYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLG-LVVTGTLPVFnltqdgpgeKKNQLIlGVMG 526
Cdd:cd12913   65 PYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGvLMITISVPIY---------DNGKFI-GVVG 134


                 ....*
gi 54112394  527 IDVAL 531
Cdd:cd12913  135 VDISL 139
 
Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 662-1104 0e+00

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: 689.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    662 YFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVErVWRDQ 741
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    742 DLNtYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAV 821
Cdd:pfam08473   80 LLN-GGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEEDDTSGILVSAAV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    822 ELSLGRRTLRPAVVGVKLDLEAWAEKFkvLASNRTHQDQPQKCGpnshcemdCEVNNEDLLCVLIDDGGFLVLSNQNHQW 901
Cdd:pfam08473  159 ELIIDGTLLKPAVVGVKLDDSWWMEFF--SNTTRKDQCDEECCG--------CKGNDDLLCCVLDDDGGFLMMSNQDDYI 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    902 DQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYG 981
Cdd:pfam08473  229 EQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVS 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    982 LIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAE-KPLCSQCEA 1060
Cdd:pfam08473  309 LTFPSFLAAEDVADEIMDAMKEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADaKGTCSSCDS 388

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 54112394   1061 GRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCG 1104
Cdd:pfam08473  389 MLLQQAEQSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 277-456 1.14e-77

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: 253.47  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  277 RRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQP-VSCFTH-LVQANVRNKK 354
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  355 VFKEAVQGMVAKGTTGYKAGFEYAFDQLQ-----NSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRT---VRVFTF 426
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSeipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112394  427 SVGQHNYDVTPLQWMACANKGYYFEIPSIG 456
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 141-265 7.76e-50

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: 172.10  E-value: 7.76e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    141 AENFQKAHRWQDNIkEEDIVYYDAKADAELDDPESEDVERGSkasTLRLDFIEDPNFKNK-VNYSYAAVQIPTDIYKGST 219
Cdd:pfam08399    1 AEKAAEDHEWNDNV-PNDFQYYNAKYSNDVGEDYEKGNNVPL---SKEFVLTPNPHFYNIpVNTNYSAVHVPTNVYDRAP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 54112394    220 VILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPW 265
Cdd:pfam08399   77 DVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 291-455 9.25e-19

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: 84.81  E-value: 9.25e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394     291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMV--A 365
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLSykL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394     366 KGTTGYKAGFEYAFDQLQNSNIT-RANCNKMIMMFTDG----GEDRVQDVFEKYNwpNRTVRVFTFSVGQHnYDVTPLQW 440
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAGsRRGAPKVVILITDGesndGPKDLLKAAKELK--RSGVKVFVVGVGND-VDEEELKK 152

                           170
                    ....*....|....*
gi 54112394     441 MACANKGYYFEIPSI 455
Cdd:smart00327  153 LASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 289-488 4.74e-17

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 82.84  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  289 PKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHlvqanVRNKKVFKEAVQGMVAKGT 368
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRLQAGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  369 TGYKAGFEYAFDQLQNSNITRANcNKMIMMfTDG-------GEDRVQDVFEKYNwpNRTVRVFTFSVGQhNYDVTPLQWM 441
Cdd:COG2304  166 TALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvgitDPEELLKLAEEAR--EEGITLTTLGVGS-DYNEDLLERL 240

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 54112394  442 ACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNV 488
Cdd:COG2304  241 ADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPYGTL 287
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 291-450 9.02e-17

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: 78.76  E-value: 9.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMV--A 365
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLT-----TDTDKADLLEAIDALKkgL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  366 KGTTGYKAGFEYAFDQLQNSNitRANCNKMIMMFTDG----GEDRVQDVFEKYNWPNrtVRVFTFSVGQhNYDVTPLQWM 441
Cdd:cd00198   77 GGGTNIGAALRLALELLKSAK--RPNARRVIILLTDGepndGPELLAEAARELRKLG--ITVYTIGIGD-DANEDELKEI 151

                        170
                 ....*....|
gi 54112394  442 A-CANKGYYF 450
Cdd:cd00198  152 AdKTTGGAVF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 261-459 8.98e-13

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: 69.58  E-value: 8.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  261 PATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLT-LKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPV 339
Cdd:COG1240   64 AALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  340 SCFThlvqanvRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRancNKMIMMFTDG----GEDRVQDVFEKYN 415
Cdd:COG1240  144 LPLT-------RDREALKRALDELPPGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGrdnaGRIDPLEAAELAA 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 54112394  416 wpNRTVRVFTFSVGQHNYDVTPLQWMACANKGYYFEIPSIGAIR 459
Cdd:COG1240  214 --AAGIRIYTIGVGTEAVDEGLLREIAEATGGRYFRADDLSELA 255
VWA pfam00092
von Willebrand factor type A domain;
291-458 9.96e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.69  E-value: 9.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMVAK- 366
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLg 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    367 -GTTGYKAGFEYAFDQLQNSNI-TRANCNKMIMMFTDG--GEDRVQDVFEKYNwpNRTVRVFTFSVGQHnyDVTPLQWMA 442
Cdd:pfam00092   76 gGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGrsQDGDPEEVARELK--SAGVTVFAVGVGNA--DDEELRKIA 151

                          170
                   ....*....|....*..
gi 54112394    443 C-ANKGYYFEIPSIGAI 458
Cdd:pfam00092  152 SePGEGHVFTVSDFEAL 168
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 291-450 2.96e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 65.78  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLS---DDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGMVAKG 367
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSLN-----DYKSKDDLLKAVKNLKYLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  368 TTG--YKAGFEYAFDQLQNSNITRANCNKMIMMFTDG---GEDRVQDVFEKYNwpNRTVRVFTFSVGQHNYDvtPLQWMA 442
Cdd:cd01450   77 GGGtnTGKALQYALEQLFSESNARENVPKVIIVLTDGrsdDGGDPKEAAAKLK--DEGIKVFVVGVGPADEE--ELREIA 152


                 ....*....
gi 54112394  443 -CANKGYYF 450
Cdd:cd01450  153 sCPSERHVF 161
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 292-459 9.47e-12

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: 64.60  E-value: 9.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  292 MVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVscfthLVQANVRNKKVFKEAVQGMVAKGTTGY 371
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETV-----LPATPVRDKAAILAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  372 KAGFEYAFDQLQNSNITRA-NCnkmIMMFTDG----GEDRVQDVFEKYNWPNRT-VRVFTFSVGQhNYDVTPLQWMACAN 445
Cdd:cd01465   78 GAGIQLGYQEAQKHFVPGGvNR---ILLATDGdfnvGETDPDELARLVAQKRESgITLSTLGFGD-NYNEDLMEAIADAG 153

                        170
                 ....*....|....
gi 54112394  446 KGYYFEIPSIGAIR 459
Cdd:cd01465  154 NGNTAYIDNLAEAR 167
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 289-449 9.55e-11

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: 61.85  E-value: 9.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  289 PKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQpvSCFTHLVQANVRNKKVFKEAVQGMVAKGT 368
Cdd:cd01461    2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVE--EFSPSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  369 TGYKAGFEYAFDQLQNSNitraNCNKMIMMFTDGGEDRVQDVFEKY-NWPNRTVRVFTFSVGQH-NYDVtpLQWMACANK 446
Cdd:cd01461   80 TNMNDALEAALELLNSSP----GSVPQIILLTDGEVTNESQILKNVrEALSGRIRLFTFGIGSDvNTYL--LERLAREGR 153


                 ...
gi 54112394  447 GYY 449
Cdd:cd01461  154 GIA 156
VWA_3 pfam13768
von Willebrand factor type A domain;
290-449 1.26e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 60.87  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    290 KDMVIIVDVSGSVSGLTlKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPvsCFTHLVQANVRNKK-VFKEAVQGMVAKGT 368
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP-KLQKDALSVALRQLPTGDKFAVLGFGTLPRP--LFPGWRVVSPRSLQeAFQFIKTLQPPLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    369 TGYKAGFEYAFDQLQnsnitRANCNKMIMMFTDGGEDRVQDVFEKY-NWPNRTVRVFTFSVGQhNYDVTPLQWMACANKG 447
Cdd:pfam13768   78 SDLLGALKEAVRAPA-----SPGYIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGA-SISAPMLQLLAEASNG 151


                   ..
gi 54112394    448 YY 449
Cdd:pfam13768  152 TY 153
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 291-449 4.12e-10

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: 59.33  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  291 DMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVScftHLVQANVRNKKVFKEAVQGMVAKGTTG 370
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLS---PLRRMTAKGKRSAKRVVDGLQAGGGTN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  371 YKAGFEYAFDQLQNsnitRANCNKM--IMMFTDGGEDRVQDVFEKYNWPnrtVRVFTFSVGqHNYDVTPLQWMACANKGY 448
Cdd:cd01466   79 VVGGLKKALKVLGD----RRQKNPVasIMLLSDGQDNHGAVVLRADNAP---IPIHTFGLG-ASHDPALLAFIAEITGGT 150


                 .
gi 54112394  449 Y 449
Cdd:cd01466  151 F 151
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 239-432 1.04e-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: 60.46  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  239 RRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEML 318
Cdd:COG2425   68 VLLALDALLLAALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  319 DTLSDDDYVNVASFNekAQPVSCFTHLVQANVRNkkvFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANcnkmIMM 398
Cdd:COG2425  148 RALRPNRRFGVILFD--TEVVEDLPLTADDGLED---AIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNAD----IVL 218

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 54112394  399 FTDGGEDRV-QDVFEKYNWPNRTVRVFTFSVGQHN 432
Cdd:COG2425  219 ITDGEAGVSpEELLREVRAKESGVRLFTVAIGDAG 253
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 533-642 1.60e-07

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: 50.07  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  533 DIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNfrepvtldfldAELEDENKEEIRRSMIDGNKGHKQIRtlvks 612
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPDKELVGKK-----------ISDDEAAEEELAKKMLAGKSGSVEYT----- 64

                         90       100       110
                 ....*....|....*....|....*....|
gi 54112394  613 lderyIDEVTRNYTWVPIRSTNYSLGLVLP 642
Cdd:cd12912   65 -----FNGEKKYVAYAPIPGTGWSLVVVVP 89
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 290-402 1.28e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 49.71  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  290 KDMVIIVDVSGSVSGLTLKLMK--TSVCEMLDTLSDDDYVNVASFnekAQPVSCFTHLVQANVRNKKVFKEAVQGMVA-K 366
Cdd:cd01476    1 LDLLFVLDSSGSVRGKFEKYKKyiERIVEGLEIGPTATRVALITY---SGRGRQRVRFNLPKHNDGEELLEKVDNLRFiG 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 54112394  367 GTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDG 402
Cdd:cd01476   78 GTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG 113
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 533-642 3.30e-06

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: 46.28  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  533 DIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNfrepvtldfldaeLEDENKEEIRRSMIDGNKGhkqirtlvkS 612
Cdd:cd18774    1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKG-------------KSLDDLALLAALLLAGESG---------T 58

                         90       100       110
                 ....*....|....*....|....*....|
gi 54112394  613 LDERYIDEVTRNYTWVPIRSTNYSLGLVLP 642
Cdd:cd18774   59 FEYTSDDGVERLVAYRPVPGTPWVVVVGVP 88
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 474-612 3.57e-06

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: 49.64  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    474 VLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFnltqDGPGEkknqlILGVMGIDVALNDIKRLTPNYTLGANGYVFAID 553
Cdd:pfam02743  103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIY----DDDGE-----VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVD 173

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 54112394    554 LNGYVLLHPNLKPQTTnfrepVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKS 612
Cdd:pfam02743  174 SDGRILAHPLGKNLRS-----LLAPFLGKSLADALPGSGITEIAVDLDGEDYLVAYAPI 227
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 288-442 4.86e-06

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 48.92  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  288 SPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLsdddyvnvaSFNEKAQPVScfthLVQ--ANVRN---------KKVF 356
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSL---------DVGPDATRVG----LVQysSTVKQefplgrfksKADL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  357 KEAVQGMV--AKGT-TGY--KAGFEYAFDQLQNSNITRANCNKMIMMFTDG-GEDRVQDVFEKynwpNRTVRVFTFSVGQ 430
Cdd:cd01475   68 KRAVRRMEylETGTmTGLaiQYAMNNAFSEAEGARPGSERVPRVGIVVTDGrPQDDVSEVAAK----ARALGIEMFAVGV 143

                        170
                 ....*....|..
gi 54112394  431 HNYDVTPLQWMA 442
Cdd:cd01475  144 GRADEEELREIA 155
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 288-402 8.35e-06

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 47.77  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  288 SPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVScFTHLVQ------ANVRNKKVFKEAVQ 361
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQ-YSDQQEveagflRDIRNYTSLKEAVD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 54112394  362 GM--VAKGTTGYKAgFEYAFDQLQNSniTRANCNKMIMMFTDG 402
Cdd:cd01480   80 NLeyIGGGTFTDCA-LKYATEQLLEG--SHQKENKFLLVITDG 119
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 290-443 3.52e-05

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: 45.30  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  290 KDMVIIVDVSGSVSGLTLKLMKTSVC---EMLDTLSDDDYVNVASFNEKAQPVSCFThlvqaNVRNKKVFKEAVQGM--V 364
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKrvvERLDIGPDGVRVGVVQYSDDPRTEFYLN-----TYRSKDDVLEAVKNLryI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  365 AKGT-TGykAGFEYAFDQL-QNSNITRANCNKMIMMFTDGGEdrvQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMA 442
Cdd:cd01472   76 GGGTnTG--KALKYVRENLfTEASGSREGVPKVLVVITDGKS---QDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150


                 .
gi 54112394  443 C 443
Cdd:cd01472  151 S 151
VWA_2 pfam13519
von Willebrand factor type A domain;
292-399 2.01e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.51  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    292 MVIIVDVSGSVSG-----LTLKLMKTSVCEMLDTLsDDDYVNVASFNEKAQPVSCFThlvqanvRNKKVFKEAVQGMVAK 366
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEVLIPLT-------KDRAKILRALRRLEPK 72

                           90       100       110
                   ....*....|....*....|....*....|....
gi 54112394    367 -GTTGYKAGFEYAFDQLQNsniTRANCNKMIMMF 399
Cdd:pfam13519   73 gGGTNLAAALQLARAALKH---RRKNQPRRIVLI 103
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 289-409 9.88e-04

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 42.68  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394    289 PKDMVIIVDVSGSVSGLtLKLMKTSVCEMLDT-LSDDDYVNVASFNEKAQPVSCFTH--------LVQANVRNKKVFKEA 359
Cdd:TIGR03436   53 PLTVGLVIDTSGSMRND-LDRARAAAIRFLKTvLRPNDRVFVVTFNTRLRLLQDFTSdprlleaaLNRLKPPLRTDYNSS 131

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 54112394    360 VQGMVAKGTTG-YKAGFEYAFDQLQNSNiTRANCNKMIMMFTDGGEDRVQD 409
Cdd:TIGR03436  132 GAFVRDGGGTAlYDAITLAALEQLANAL-AGIPGRKALIVISDGGDNRSRD 181
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 448-531 7.94e-03

first 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 first 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: 350338  Cd Length: 139  Bit Score: 37.89  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112394  448 YYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLG-LVVTGTLPVFnltqdgpgeKKNQLIlGVMG 526
Cdd:cd12913   65 PYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGvLMITISVPIY---------DNGKFI-GVVG 134


                 ....*
gi 54112394  527 IDVAL 531
Cdd:cd12913  135 VDISL 139
 
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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