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Conserved domains on  [gi|1720377989|ref|XP_030103476|]
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voltage-dependent calcium channel subunit alpha-2/delta-3 isoform X4 [Mus musculus]

Protein Classification

calcium channel subunit alpha-2/delta family protein; methyl-accepting chemotaxis protein( domain architecture ID 13750241)

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| methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior; contains double cache and HAMP domains

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 ...
 148-331 6.52e-98

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: 306.24  E-value: 6.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 148 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPCLNGTLVQADRTNKE 227
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 228 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 301
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720377989 302 LIGREAAFADNLKWMACANKGFFTQISTLA 331
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 19-135 4.58e-53

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: 180.96  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  19 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 93
Cdd:pfam08399   1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720377989  94 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 135
Cdd:pfam08399  81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 561-974 2.31e-23

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: 104.38  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 561 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 639
Cdd:pfam08473  22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 640 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIAGSFVYSIPFSTG-----TVNKSNVVTASTSIQLLD 714
Cdd:pfam08473  96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSyrpneEEDDTSGILVSAAVELII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 715 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEVEG 789
Cdd:pfam08473 163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 790 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDSAHGL---LDPYKAFL-------SAAKWIMTELVLFLVEFNlcsWW-- 857
Cdd:pfam08473 240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 858 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 937
Cdd:pfam08473 317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720377989 938 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 974
Cdd:pfam08473 396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 414-528 2.84e-09

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: 55.08  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 414 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrplyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 493
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720377989 494 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 528
Cdd:cd12912    65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 345-475 3.91e-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: 49.26  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 345 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLADDQGLVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 417
Cdd:pfam02743  83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720377989 418 TIPKYKLGIHGYAFAITNNGYILTHPELRPLYEEGKKRRKPNYSSVDLSEVEWEDRDD 475
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD 214
 
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 ...
 148-331 6.52e-98

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: 306.24  E-value: 6.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 148 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPCLNGTLVQADRTNKE 227
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 228 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 301
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720377989 302 LIGREAAFADNLKWMACANKGFFTQISTLA 331
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 19-135 4.58e-53

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: 180.96  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  19 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 93
Cdd:pfam08399   1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720377989  94 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 135
Cdd:pfam08399  81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 561-974 2.31e-23

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: 104.38  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 561 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 639
Cdd:pfam08473  22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 640 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIAGSFVYSIPFSTG-----TVNKSNVVTASTSIQLLD 714
Cdd:pfam08473  96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSyrpneEEDDTSGILVSAAVELII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 715 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEVEG 789
Cdd:pfam08473 163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 790 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDSAHGL---LDPYKAFL-------SAAKWIMTELVLFLVEFNlcsWW-- 857
Cdd:pfam08473 240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 858 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 937
Cdd:pfam08473 317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720377989 938 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 974
Cdd:pfam08473 396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 162-332 2.43e-20

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: 89.44  E-value: 2.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIITYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKL-- 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN-------DSRSKDALLEALASLsy 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  237 FAKGIGMLDIALNEAFNILSDFNHTGQGSIcSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIG-REAAFADNLKW 315
Cdd:smart00327  74 KLGGGTNLGAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                          170
                   ....*....|....*..
gi 1720377989  316 MACANKGFFTQISTLAD 332
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 155-335 5.16e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 79.76  E-value: 5.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 155 QAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNeelHYVEPCLNGTLVqadrTNKEHFREHLD 234
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFA---GDARVLLPPTPA----TDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 235 KLFAKGiGM-LDIALNEAFNILSDfnHTGQGSIcsQAIMLITDGAVD---TYDTIFAKY--NWPDRKVRIFTYLIGREaa 308
Cdd:COG2304   159 RLQAGG-GTaLGAGLELAYELARK--HFIPGRV--NRVILLTDGDANvgiTDPEELLKLaeEAREEGITLTTLGVGSD-- 231

                         170       180
                  ....*....|....*....|....*...
gi 1720377989 309 FADN-LKWMACANKGFFTQISTLADVQE 335
Cdd:COG2304   232 YNEDlLERLADAGGGNYYYIDDPEEAEK 259
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 156-351 7.23e-16

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


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 82.04  E-value: 7.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 156 AATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPclngTLVQADRTNKEHFREHLDK 235
Cdd:TIGR03788 267 AQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVTLLFP----VPVPATAHNLARARQFVAG 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 236 LFAKG----IGMLDIALNEAfnilsdfnhTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGReaafAD 311
Cdd:TIGR03788 343 LQADGgtemAGALSAALRDD---------GPESSGALRQVVFLTDGAVGNEDALFQLIRTKLGDSRLFTVGIGS----AP 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720377989 312 NLKWM---ACANKGFFTQISTLADVQENVMEYLHVLSRPKVID 351
Cdd:TIGR03788 410 NSYFMrkaAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTD 452
VWA_3 pfam13768
von Willebrand factor type A domain;
161-323 4.74e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 62.03  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 161 KDVVILVDVSGSMKGLRLTIaKQTVSSILDTLGDDDFFNIITYNEelhYVEPCLNGTLVQADRtnkehfreHLDKLFAKg 240
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGT---LPRPLFPGWRVVSPR--------SLQEAFQF- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 241 IGMLDI---------ALNEAFnilSDFNHTGqgsiCSQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAfA 310
Cdd:pfam13768  68 IKTLQPplggsdllgALKEAV---RAPASPG----YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-A 139

                         170
                  ....*....|...
gi 1720377989 311 DNLKWMACANKGF 323
Cdd:pfam13768 140 PMLQLLAEASNGT 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 414-528 2.84e-09

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: 55.08  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 414 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrplyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 493
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720377989 494 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 528
Cdd:cd12912    65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 345-475 3.91e-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: 49.26  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 345 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLADDQGLVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 417
Cdd:pfam02743  83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720377989 418 TIPKYKLGIHGYAFAITNNGYILTHPELRPLYEEGKKRRKPNYSSVDLSEVEWEDRDD 475
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD 214
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 352-412 5.85e-04

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: 40.97  E-value: 5.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720377989 352 QEHDVVWTEAYIDSTLPQaqkladdqglVLMTTVAMPVFskqnetrSKGILLGVVGTDVPV 412
Cdd:cd12913    96 ETGKPVWTEPYIDEVGTG----------VLMITISVPIY-------DNGKFIGVVGVDISL 139
 
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 ...
 148-331 6.52e-98

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: 306.24  E-value: 6.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 148 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPCLNGTLVQADRTNKE 227
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 228 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 301
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720377989 302 LIGREAAFADNLKWMACANKGFFTQISTLA 331
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 19-135 4.58e-53

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: 180.96  E-value: 4.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  19 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 93
Cdd:pfam08399   1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720377989  94 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 135
Cdd:pfam08399  81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 561-974 2.31e-23

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: 104.38  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 561 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 639
Cdd:pfam08473  22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 640 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIAGSFVYSIPFSTG-----TVNKSNVVTASTSIQLLD 714
Cdd:pfam08473  96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSyrpneEEDDTSGILVSAAVELII 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 715 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEVEG 789
Cdd:pfam08473 163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 790 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDSAHGL---LDPYKAFL-------SAAKWIMTELVLFLVEFNlcsWW-- 857
Cdd:pfam08473 240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 858 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 937
Cdd:pfam08473 317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720377989 938 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 974
Cdd:pfam08473 396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 162-332 2.43e-20

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: 89.44  E-value: 2.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIITYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKL-- 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN-------DSRSKDALLEALASLsy 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989  237 FAKGIGMLDIALNEAFNILSDFNHTGQGSIcSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIG-REAAFADNLKW 315
Cdd:smart00327  74 KLGGGTNLGAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                          170
                   ....*....|....*..
gi 1720377989  316 MACANKGFFTQISTLAD 332
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 160-338 6.59e-20

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: 88.04  E-value: 6.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 160 PKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPClngtLVQADRTNKEHFREHLDKLFAK 239
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS----SVSATAENVAAAIEYVNRLQAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 240 GiG--MLDiALNEAFNILSdfnhTGQGSIcsQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAFAdNLKWM 316
Cdd:cd01461    78 G-GtnMND-ALEAALELLN----SSPGSV--PQIILLTDGEVTNESQILKNVrEALSGRIRLFTFGIGSDVNTY-LLERL 148

                         170       180
                  ....*....|....*....|..
gi 1720377989 317 ACANKGFFTQISTLADVQENVM 338
Cdd:cd01461   149 AREGRGIARRIYETDDIESQLL 170
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 155-335 5.16e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 79.76  E-value: 5.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 155 QAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNeelHYVEPCLNGTLVqadrTNKEHFREHLD 234
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFA---GDARVLLPPTPA----TDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 235 KLFAKGiGM-LDIALNEAFNILSDfnHTGQGSIcsQAIMLITDGAVD---TYDTIFAKY--NWPDRKVRIFTYLIGREaa 308
Cdd:COG2304   159 RLQAGG-GTaLGAGLELAYELARK--HFIPGRV--NRVILLTDGDANvgiTDPEELLKLaeEAREEGITLTTLGVGSD-- 231

                         170       180
                  ....*....|....*....|....*...
gi 1720377989 309 FADN-LKWMACANKGFFTQISTLADVQE 335
Cdd:COG2304   232 YNEDlLERLADAGGGNYYYIDDPEEAEK 259
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 156-351 7.23e-16

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


Pssm-ID: 274782 [Multi-domain]  Cd Length: 596  Bit Score: 82.04  E-value: 7.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 156 AATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPclngTLVQADRTNKEHFREHLDK 235
Cdd:TIGR03788 267 AQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVTLLFP----VPVPATAHNLARARQFVAG 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 236 LFAKG----IGMLDIALNEAfnilsdfnhTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGReaafAD 311
Cdd:TIGR03788 343 LQADGgtemAGALSAALRDD---------GPESSGALRQVVFLTDGAVGNEDALFQLIRTKLGDSRLFTVGIGS----AP 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720377989 312 NLKWM---ACANKGFFTQISTLADVQENVMEYLHVLSRPKVID 351
Cdd:TIGR03788 410 NSYFMrkaAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTD 452
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 162-317 2.59e-15

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 74.52  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIITYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKLFA 238
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLT-------TDTDKADLLEAIDALKK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 239 KGIGMLDI--ALNEAFNILSDFNHTGQGSIcsqaIMLITDGAVDTYDTIFAKY--NWPDRKVRIFTYLIGREAAFaDNLK 314
Cdd:cd00198    75 GLGGGTNIgaALRLALELLKSAKRPNARRV----IILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANE-DELK 149


                  ...
gi 1720377989 315 WMA 317
Cdd:cd00198   150 EIA 152
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 159-335 3.82e-14

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: 73.82  E-value: 3.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 159 SPKDVVILVDVSGSMKGL-RLTIAKQTVSSILDTLGDDDFFNIITYNeelHYVEPCLNGTlvqadrTNKEHFREHLDKLF 237
Cdd:COG1240    91 RGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFG---GEAEVLLPLT------RDREALKRALDELP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 238 AKG---IGMldiALNEAFNILSDFNHTGqgsicSQAIMLITDGA--VDTYDTIFAKYNWPDRKVRIFTYLIGREAAFADN 312
Cdd:COG1240   162 PGGgtpLGD---ALALALELLKRADPAR-----RKVIVLLTDGRdnAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGL 233

                         170       180
                  ....*....|....*....|...
gi 1720377989 313 LKWMACANKGFFTQISTLADVQE 335
Cdd:COG1240   234 LREIAEATGGRYFRADDLSELAA 256
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 160-310 1.00e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 69.32  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 160 PKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPclngtlVQADRTNKEhFREHLDKLFAK 239
Cdd:COG2425   118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLP------LTADDGLED-AIEFLSGLFAG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720377989 240 GIGMLDIALNEAFNILSDFNHTgqgsicSQAIMLITDGAVDTYDT-IFAKYNWPDRKVRIFTYLIGREAAFA 310
Cdd:COG2425   191 GGTDIAPALRAALELLEEPDYR------NADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPG 256
VWA_3 pfam13768
von Willebrand factor type A domain;
161-323 4.74e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 62.03  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 161 KDVVILVDVSGSMKGLRLTIaKQTVSSILDTLGDDDFFNIITYNEelhYVEPCLNGTLVQADRtnkehfreHLDKLFAKg 240
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGT---LPRPLFPGWRVVSPR--------SLQEAFQF- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 241 IGMLDI---------ALNEAFnilSDFNHTGqgsiCSQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAfA 310
Cdd:pfam13768  68 IKTLQPplggsdllgALKEAV---RAPASPG----YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-A 139

                         170
                  ....*....|...
gi 1720377989 311 DNLKWMACANKGF 323
Cdd:pfam13768 140 PMLQLLAEASNGT 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 414-528 2.84e-09

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: 55.08  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 414 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrplyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 493
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720377989 494 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 528
Cdd:cd12912    65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 164-335 9.01e-09

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: 55.74  E-value: 9.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 164 VILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNeelHYVEPCLNGTLVqadrTNKEHFREHLDKLFAKGIGM 243
Cdd:cd01465     4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYD---GAAETVLPATPV----RDKAAILAAIDRLTAGGSTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 244 LDIALNEAFNILSdfNHTGQGSIcsQAIMLITDG--------AVDTYDTIFAKynwpdRKVRIFTYLIGreaaFADN--- 312
Cdd:cd01465    77 GGAGIQLGYQEAQ--KHFVPGGV--NRILLATDGdfnvgetdPDELARLVAQK-----RESGITLSTLG----FGDNyne 143

                         170       180
                  ....*....|....*....|....*
gi 1720377989 313 --LKWMACANKGFFTQISTLADVQE 335
Cdd:cd01465   144 dlMEAIADAGNGNTAYIDNLAEARK 168
VWA pfam00092
von Willebrand factor type A domain;
162-335 1.02e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 55.74  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLG---DDDFFNIITYNEELHyVEPCLNgtlvqaDRTNKEHFREHLDKLFA 238
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR-TEFPLN------DYSSKEELLSAVDNLRY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 239 KGIGMLDI--ALNEAFNILsdFNHT-GQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTylIGREAAFADNLKW 315
Cdd:pfam00092  74 LGGGTTNTgkALKYALENL--FSSAaGARPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFA--VGVGNADDEELRK 149

                         170       180
                  ....*....|....*....|.
gi 1720377989 316 MAC-ANKGFFTQISTLADVQE 335
Cdd:pfam00092 150 IASePGEGHVFTVSDFEALED 170
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 162-325 2.74e-08

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: 53.93  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIITYNEELHYVEPclngtLVQADRTNKEHFREHLDKLFAKGI 241
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGLQAGGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 242 GMLDIALNEAFNILSDFNHTGQGSicsqAIMLITDGAvDTYDTIFAKYNWPdrKVRIFTYLIGREAAfADNLKWMACANK 321
Cdd:cd01466    77 TNVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQ-DNHGAVVLRADNA--PIPIHTFGLGASHD-PALLAFIAEITG 148


                  ....
gi 1720377989 322 GFFT 325
Cdd:cd01466   149 GTFS 152
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 162-277 6.03e-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: 50.37  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIITYNEElHYVEPCLNgtlvqaDRTNKEHFREHLDKL-F 237
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDD-VRVEFSLN------DYKSKDDLLKAVKNLkY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720377989 238 AKGIG-MLDIALNEAFNILsdFNHTGQGSICSQAIMLITDG 277
Cdd:cd01450    75 LGGGGtNTGKALQYALEQL--FSESNARENVPKVIIVLTDG 113
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 345-475 3.91e-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: 49.26  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 345 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLADDQGLVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 417
Cdd:pfam02743  83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720377989 418 TIPKYKLGIHGYAFAITNNGYILTHPELRPLYEEGKKRRKPNYSSVDLSEVEWEDRDD 475
Cdd:pfam02743 157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD 214
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 414-528 7.46e-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: 45.13  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 414 ELLKTIPKYKLGIHGYAFAITNNGYILTHPelrPLYEEGKKRRkpnyssvdlsevewEDRDDVLRNAMVNRKTGKFSMev 493
Cdd:cd18774     1 YLSDLLSSIKLGETGYAFLVDSDGTILAHP---PKELVGKGKS--------------LDDLALLAALLLAGESGTFEY-- 61

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720377989 494 kkTVDKGKRVLvmtndYYYTDIKGTPFSLGVALSR 528
Cdd:cd18774    62 --TSDDGVERL-----VAYRPVPGTPWVVVVGVPE 89
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
162-307 1.84e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.46  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 162 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDD------FFNIITYNEElhyVEpclngtlVQADRTNKEHFreHLDK 235
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGE---AK-------VLLPLTDLEDF--QPPD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 236 LFAKGIGMLDIALNEAFNILSD----FNHTGQGSiCSQAIMLITDGAV--DTYDTIFAKY--NWPDRKVRIFTYLIGREA 307
Cdd:COG4245    75 LSASGGTPLGAALELLLDLIERrvqkYTAEGKGD-WRPVVFLITDGEPtdSDWEAALQRLkdGEAAKKANIFAIGVGPDA 153
VWA_2 pfam13519
von Willebrand factor type A domain;
163-257 4.27e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.74  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 163 VVILVDVSGSM-----KGLRLTIAKQTVSSILDTLgDDDFFNIITYNEELHyvepclngtLVQADRTNKEHFREHLDKLF 237
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPE---------VLIPLTKDRAKILRALRRLE 70

                          90       100
                  ....*....|....*....|.
gi 1720377989 238 AKGIGM-LDIALNEAFNILSD 257
Cdd:pfam13519  71 PKGGGTnLAAALQLARAALKH 91
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 352-412 5.85e-04

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: 40.97  E-value: 5.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720377989 352 QEHDVVWTEAYIDSTLPQaqkladdqglVLMTTVAMPVFskqnetrSKGILLGVVGTDVPV 412
Cdd:cd12913    96 ETGKPVWTEPYIDEVGTG----------VLMITISVPIY-------DNGKFIGVVGVDISL 139
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 161-277 2.49e-03

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 39.64  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720377989 161 KDVVILVDVSGSMKGLRLTIAKQTVSSILDTlgdddffnIITYNEELHYVepCLNGTLVQADRTNKEHFREHLDKLFA-K 239
Cdd:cd01462     1 GPVILLVDQSGSMYGAPEEVAKAVALALLRI--------ALAENRDTYLI--LFDSEFQTKIVDKTDDLEEPVEFLSGvQ 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720377989 240 GIGMLDI--ALNEAFNILSdfNHTGQGSIcsqaIMLITDG 277
Cdd:cd01462    71 LGGGTDInkALRYALELIE--RRDPRKAD----IVLITDG 104
 
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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