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Conserved domains on  [gi|54112397|ref|NP_060868|]
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voltage-dependent calcium channel subunit alpha-2/delta-3 precursor [Homo sapiens]

Protein Classification

VWA_N and vWA_VGCC_like domain-containing protein( domain architecture ID 13750241)

protein containing domains VWA_N, vWA_VGCC_like, dCache_1, and PDC2_MCP_like

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 ...
 242-425 5.11e-97

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: 305.47  E-value: 5.11e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  242 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPCLNGTLVQADRTNKE 321
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  322 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 395
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112397  396 LIGREAAFADNLKWMACANKGFFTQISTLA 425
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 113-229 2.54e-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: 181.73  E-value: 2.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    113 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 187
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 54112397    188 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 229
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 655-1068 2.81e-22

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: 100.92  E-value: 2.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    655 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 733
Cdd:pfam08473   22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    734 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIPGSFVYSIPFSTGPV-----NKSNVVTASTSIQLLD 808
Cdd:pfam08473   96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRpneeeDDTSGILVSAAVELII 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    809 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEIEG 883
Cdd:pfam08473  163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    884 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDGAHGL---LDPYNAFL-------SAVKWIMTELVLFLVEFNlcsWW-- 951
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    952 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 1031
Cdd:pfam08473  317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 54112397   1032 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 1068
Cdd:pfam08473  396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 508-622 3.21e-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: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  508 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrllyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 587
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54112397  588 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 622
Cdd:cd12912   65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 439-569 1.80e-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: 50.41  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    439 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLTDDQGPVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 511
Cdd:pfam02743   83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 54112397    512 TIPKYKLGIHGYAFAITNNGYILTHPELRLLYEEGKKRRKPNYSSVDLSEVEWEDRDD 569
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 ...
 242-425 5.11e-97

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: 305.47  E-value: 5.11e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  242 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPCLNGTLVQADRTNKE 321
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  322 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 395
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112397  396 LIGREAAFADNLKWMACANKGFFTQISTLA 425
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 113-229 2.54e-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: 181.73  E-value: 2.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    113 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 187
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 54112397    188 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 229
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 655-1068 2.81e-22

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: 100.92  E-value: 2.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    655 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 733
Cdd:pfam08473   22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    734 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIPGSFVYSIPFSTGPV-----NKSNVVTASTSIQLLD 808
Cdd:pfam08473   96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRpneeeDDTSGILVSAAVELII 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    809 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEIEG 883
Cdd:pfam08473  163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    884 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDGAHGL---LDPYNAFL-------SAVKWIMTELVLFLVEFNlcsWW-- 951
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    952 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 1031
Cdd:pfam08473  317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 54112397   1032 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 1068
Cdd:pfam08473  396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 256-426 7.54e-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: 87.90  E-value: 7.54e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397     256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIIAYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKL-- 330
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN-------DSRSKDALLEALASLsy 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397     331 FAKGIGMLDIALNEAFNILSDFNHTGQGSIcSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIG-REAAFADNLKW 409
Cdd:smart00327   74 KLGGGTNLGAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                           170
                    ....*....|....*..
gi 54112397     410 MACANKGFFTQISTLAD 426
Cdd:smart00327  153 LASAPGGVYVFLPELLD 169
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 250-445 3.23e-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: 83.59  E-value: 3.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    250 AATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPclngTLVQADRTNKEHFREHLDK 329
Cdd:TIGR03788  267 AQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVTLLFP----VPVPATAHNLARARQFVAG 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    330 LFAKG----IGMLDIALNEAfnilsdfnhTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGReaafAD 405
Cdd:TIGR03788  343 LQADGgtemAGALSAALRDD---------GPESSGALRQVVFLTDGAVGNEDALFQLIRTKLGDSRLFTVGIGS----AP 409

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 54112397    406 NLKWM---ACANKGFFTQISTLADVQENVMEYLHVLSRPKVID 445
Cdd:TIGR03788  410 NSYFMrkaAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTD 452
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 249-429 1.08e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 78.99  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  249 QAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNeelHYVEPCLNGTLVqadrTNKEHFREHLD 328
Cdd:COG2304   86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFA---GDARVLLPPTPA----TDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  329 KLFAKGiGM-LDIALNEAFNILSDfnHTGQGSIcsQAIMLITDGAVD---TYDTIFAKY--NWPDRKVRIFTYLIGREaa 402
Cdd:COG2304  159 RLQAGG-GTaLGAGLELAYELARK--HFIPGRV--NRVILLTDGDANvgiTDPEELLKLaeEAREEGITLTTLGVGSD-- 231

                        170       180
                 ....*....|....*....|....*...
gi 54112397  403 FADN-LKWMACANKGFFTQISTLADVQE 429
Cdd:COG2304  232 YNEDlLERLADAGGGNYYYIDDPEEAEK 259
VWA_3 pfam13768
von Willebrand factor type A domain;
255-417 2.27e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 63.18  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    255 KDVVILVDVSGSMKGLRLTIaKQTVSSILDTLGDDDFFNIIAYNEelhYVEPCLNGTLVQADRtnkehfreHLDKLFAKg 334
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGT---LPRPLFPGWRVVSPR--------SLQEAFQF- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    335 IGMLDI---------ALNEAFnilSDFNHTGqgsiCSQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAfA 404
Cdd:pfam13768   68 IKTLQPplggsdllgALKEAV---RAPASPG----YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-A 139

                          170
                   ....*....|...
gi 54112397    405 DNLKWMACANKGF 417
Cdd:pfam13768  140 PMLQLLAEASNGT 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 508-622 3.21e-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: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  508 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrllyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 587
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54112397  588 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 622
Cdd:cd12912   65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 439-569 1.80e-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: 50.41  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    439 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLTDDQGPVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 511
Cdd:pfam02743   83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 54112397    512 TIPKYKLGIHGYAFAITNNGYILTHPELRLLYEEGKKRRKPNYSSVDLSEVEWEDRDD 569
Cdd:pfam02743  157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD 214
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 446-506 2.23e-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: 42.51  E-value: 2.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54112397  446 QEHDVVWTEAYIDStlpqaqkltdDQGPVLMTTVAMPVFskqnetrSKGILLGVVGTDVPV 506
Cdd:cd12913   96 ETGKPVWTEPYIDE----------VGTGVLMITISVPIY-------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 ...
 242-425 5.11e-97

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: 305.47  E-value: 5.11e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  242 RNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPCLNGTLVQADRTNKE 321
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  322 HFREHLDKLFAKGIGMLDIALNEAFNILSD---FNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDR---KVRIFTY 395
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 54112397  396 LIGREAAFADNLKWMACANKGFFTQISTLA 425
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 113-229 2.54e-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: 181.73  E-value: 2.54e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    113 AEEAHLKHEFDAD--LQYEYFNAVLINERDKD---GNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVN 187
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEDyekGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 54112397    188 GVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKW 229
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 655-1068 2.81e-22

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: 100.92  E-value: 2.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    655 YCNTDLHPEHRHLSQLEAIKLYLKGKEP-LLQCDKELIQEVLFDAVVSAPIEAYWtslalNKSENSDkGVEVAFLGTRTG 733
Cdd:pfam08473   22 YYCKDLKPSNNNTEFLEFFNYIIDKTTPnPPCCNNLLNNLLLLDGGITQLLVKWW-----KKQLLNG-GLLAVFAATDGG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    734 LSRInlfvgaeqltnqdFLKAGDKENIFNADHFPLWYRRAAEQIPGSFVYSIPFSTGPV-----NKSNVVTASTSIQLLD 808
Cdd:pfam08473   96 ITRV-------------PPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRpneeeDDTSGILVSAAVELII 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    809 ERKSPVVAAVGIQMKLEFFQRKFWTASR--QCASLDGKCSISCDDetvNCYLIDNNGFILVS---EDYTQTGDFFGEIEG 883
Cdd:pfam08473  163 DGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGNDDL---LCCVLDDDGGFLMMsnqDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    884 AVMNKLLTMGSFKRITLYDYQAMCRANKESSDGAHGL---LDPYNAFL-------SAVKWIMTELVLFLVEFNlcsWW-- 951
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsvVVPTIADLlnlwwwtSAAAWSIQQQLLVSLTFP---SFla 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    952 HSDMTAKAQKLKQTlEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIE 1031
Cdd:pfam08473  317 AEDVADEIMDAMKE-ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSSCDSMLLQQAE 395

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 54112397   1032 IRYNESLKCERLKAQKIRRRPESCHGFHPEENARECG 1068
Cdd:pfam08473  396 QSSDGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 256-426 7.54e-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: 87.90  E-value: 7.54e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397     256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIIAYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKL-- 330
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN-------DSRSKDALLEALASLsy 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397     331 FAKGIGMLDIALNEAFNILSDFNHTGQGSIcSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIG-REAAFADNLKW 409
Cdd:smart00327   74 KLGGGTNLGAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                           170
                    ....*....|....*..
gi 54112397     410 MACANKGFFTQISTLAD 426
Cdd:smart00327  153 LASAPGGVYVFLPELLD 169
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 254-432 1.06e-19

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: 87.66  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  254 PKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPClngtLVQADRTNKEHFREHLDKLFAK 333
Cdd:cd01461    2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS----SVSATAENVAAAIEYVNRLQAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  334 GiG--MLDiALNEAFNILSdfnhTGQGSIcsQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAFAdNLKWM 410
Cdd:cd01461   78 G-GtnMND-ALEAALELLN----SSPGSV--PQIILLTDGEVTNESQILKNVrEALSGRIRLFTFGIGSDVNTY-LLERL 148

                        170       180
                 ....*....|....*....|..
gi 54112397  411 ACANKGFFTQISTLADVQENVM 432
Cdd:cd01461  149 AREGRGIARRIYETDDIESQLL 170
marine_srt_targ TIGR03788
marine proteobacterial sortase target protein; Members of this protein family are restricted ...
 250-445 3.23e-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: 83.59  E-value: 3.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    250 AATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPclngTLVQADRTNKEHFREHLDK 329
Cdd:TIGR03788  267 AQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVTLLFP----VPVPATAHNLARARQFVAG 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    330 LFAKG----IGMLDIALNEAfnilsdfnhTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGReaafAD 405
Cdd:TIGR03788  343 LQADGgtemAGALSAALRDD---------GPESSGALRQVVFLTDGAVGNEDALFQLIRTKLGDSRLFTVGIGS----AP 409

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 54112397    406 NLKWM---ACANKGFFTQISTLADVQENVMEYLHVLSRPKVID 445
Cdd:TIGR03788  410 NSYFMrkaAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTD 452
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 249-429 1.08e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 78.99  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  249 QAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNeelHYVEPCLNGTLVqadrTNKEHFREHLD 328
Cdd:COG2304   86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFA---GDARVLLPPTPA----TDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  329 KLFAKGiGM-LDIALNEAFNILSDfnHTGQGSIcsQAIMLITDGAVD---TYDTIFAKY--NWPDRKVRIFTYLIGREaa 402
Cdd:COG2304  159 RLQAGG-GTaLGAGLELAYELARK--HFIPGRV--NRVILLTDGDANvgiTDPEELLKLaeEAREEGITLTTLGVGSD-- 231

                        170       180
                 ....*....|....*....|....*...
gi 54112397  403 FADN-LKWMACANKGFFTQISTLADVQE 429
Cdd:COG2304  232 YNEDlLERLADAGGGNYYYIDDPEEAEK 259
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 256-411 4.17e-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: 74.14  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIIAYNEELHYVEPCLngtlvqaDRTNKEHFREHLDKLFA 332
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLT-------TDTDKADLLEAIDALKK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  333 KGIGMLDI--ALNEAFNILSDFNHTGQGSIcsqaIMLITDGAVDTYDTIFAKY--NWPDRKVRIFTYLIGREAAFaDNLK 408
Cdd:cd00198   75 GLGGGTNIgaALRLALELLKSAKRPNARRV----IILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANE-DELK 149


                 ...
gi 54112397  409 WMA 411
Cdd:cd00198  150 EIA 152
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 253-429 3.56e-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: 3.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  253 SPKDVVILVDVSGSMKGL-RLTIAKQTVSSILDTLGDDDFFNIIAYNeelHYVEPCLNGTlvqadrTNKEHFREHLDKLF 331
Cdd:COG1240   91 RGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFG---GEAEVLLPLT------RDREALKRALDELP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  332 AKG---IGMldiALNEAFNILSDFNHTGqgsicSQAIMLITDGA--VDTYDTIFAKYNWPDRKVRIFTYLIGREAAFADN 406
Cdd:COG1240  162 PGGgtpLGD---ALALALELLKRADPAR-----RKVIVLLTDGRdnAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGL 233

                        170       180
                 ....*....|....*....|...
gi 54112397  407 LKWMACANKGFFTQISTLADVQE 429
Cdd:COG1240  234 LREIAEATGGRYFRADDLSELAA 256
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 254-404 4.04e-13

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 70.86  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  254 PKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPclngtlVQADRTNKEhFREHLDKLFAK 333
Cdd:COG2425  118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLP------LTADDGLED-AIEFLSGLFAG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54112397  334 GIGMLDIALNEAFNILSDFNHTgqgsicSQAIMLITDGAVDTYDT-IFAKYNWPDRKVRIFTYLIGREAAFA 404
Cdd:COG2425  191 GGTDIAPALRAALELLEEPDYR------NADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPG 256
VWA_3 pfam13768
von Willebrand factor type A domain;
255-417 2.27e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 63.18  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    255 KDVVILVDVSGSMKGLRLTIaKQTVSSILDTLGDDDFFNIIAYNEelhYVEPCLNGTLVQADRtnkehfreHLDKLFAKg 334
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGT---LPRPLFPGWRVVSPR--------SLQEAFQF- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    335 IGMLDI---------ALNEAFnilSDFNHTGqgsiCSQAIMLITDGAVDTYDTIFAKY-NWPDRKVRIFTYLIGREAAfA 404
Cdd:pfam13768   68 IKTLQPplggsdllgALKEAV---RAPASPG----YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-A 139

                          170
                   ....*....|...
gi 54112397    405 DNLKWMACANKGF 417
Cdd:pfam13768  140 PMLQLLAEASNGT 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 508-622 3.21e-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: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  508 ELLKTIPKYKLGIHGYAFAITNNGYILTHpelrllyeegkkrrkPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEv 587
Cdd:cd12912    1 ELSEIISSIKIGETGYAFLVDKDGTIIAH---------------PDKELVGKKISDDEAAEEELAKKMLAGKSGSVEYT- 64

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54112397  588 kktvDKGKRVLVmtndyYYTDIKGTPFSLGVALSR 622
Cdd:cd12912   65 ----FNGEKKYV-----AYAPIPGTGWSLVVVVPE 90
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 258-429 2.84e-08

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: 54.59  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  258 VILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNeelHYVEPCLNGTLVqadrTNKEHFREHLDKLFAKGIGM 337
Cdd:cd01465    4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYD---GAAETVLPATPV----RDKAAILAAIDRLTAGGSTA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  338 LDIALNEAFNILSdfNHTGQGSIcsQAIMLITDG--------AVDTYDTIFAKynwpdRKVRIFTYLIGreaaFADN--- 406
Cdd:cd01465   77 GGAGIQLGYQEAQ--KHFVPGGV--NRILLATDGdfnvgetdPDELARLVAQK-----RESGITLSTLG----FGDNyne 143

                        170       180
                 ....*....|....*....|....*
gi 54112397  407 --LKWMACANKGFFTQISTLADVQE 429
Cdd:cd01465  144 dlMEAIADAGNGNTAYIDNLAEARK 168
VWA pfam00092
von Willebrand factor type A domain;
256-429 5.06e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 53.82  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLG---DDDFFNIIAYNEELHyVEPCLNgtlvqaDRTNKEHFREHLDKLFA 332
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR-TEFPLN------DYSSKEELLSAVDNLRY 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    333 KGIGMLDI--ALNEAFNILsdFNHT-GQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTylIGREAAFADNLKW 409
Cdd:pfam00092   74 LGGGTTNTgkALKYALENL--FSSAaGARPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFA--VGVGNADDEELRK 149

                          170       180
                   ....*....|....*....|.
gi 54112397    410 MAC-ANKGFFTQISTLADVQE 429
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 ...
 256-419 6.58e-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: 53.16  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPclngtLVQADRTNKEHFREHLDKLFAKGI 335
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGLQAGGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  336 GMLDIALNEAFNILSDFNHTGQGSicsqAIMLITDGAvDTYDTIFAKYNWPdrKVRIFTYLIGREAAfADNLKWMACANK 415
Cdd:cd01466   77 TNVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQ-DNHGAVVLRADNA--PIPIHTFGLGASHD-PALLAFIAEITG 148


                 ....
gi 54112397  416 GFFT 419
Cdd:cd01466  149 GTFS 152
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 439-569 1.80e-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: 50.41  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    439 SRPKVIDQEHDVVWTEAYID-------STLPQAQKLTDDQGPVLMTTVAMPVFSKQNEtrskgiLLGVVGTDVPVKELLK 511
Cdd:pfam02743   83 SDESPSYPGLDVSERPWYKEalkggggIIWVFSSPYPSSESGEPVLTIARPIYDDDGE------VIGVLVADLDLDTLQE 156

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 54112397    512 TIPKYKLGIHGYAFAITNNGYILTHPELRLLYEEGKKRRKPNYSSVDLSEVEWEDRDD 569
Cdd:pfam02743  157 LLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVD 214
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 508-622 7.57e-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: 7.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  508 ELLKTIPKYKLGIHGYAFAITNNGYILTHPELRLLyeeGKKRRkpnyssvdlsevewEDRDDVLRNAMVNRKTGKFSMev 587
Cdd:cd18774    1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELV---GKGKS--------------LDDLALLAALLLAGESGTFEY-- 61

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 54112397  588 kkTVDKGKRVLvmtndYYYTDIKGTPFSLGVALSR 622
Cdd:cd18774   62 --TSDDGVERL-----VAYRPVPGTPWVVVVGVPE 89
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 256-371 8.14e-06

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: 47.29  E-value: 8.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTL---GDDDFFNIIAYNEElHYVEPCLNgtlvqaDRTNKEHFREHLDKL-F 331
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDD-VRVEFSLN------DYKSKDDLLKAVKNLkY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 54112397  332 AKGIG-MLDIALNEAFNILsdFNHTGQGSICSQAIMLITDG 371
Cdd:cd01450   75 LGGGGtNTGKALQYALEQL--FSESNARENVPKVIIVLTDG 113
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
256-401 5.68e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 45.30  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  256 DVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDD------FFNIIAYNEElhyVEpclngtlVQADRTNKEHFreHLDK 329
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGE---AK-------VLLPLTDLEDF--QPPD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  330 LFAKGIGMLDIALNEAFNILSD----FNHTGQGSiCSQAIMLITDGAV--DTYDTIFAKY--NWPDRKVRIFTYLIGREA 401
Cdd:COG4245   75 LSASGGTPLGAALELLLDLIERrvqkYTAEGKGD-WRPVVFLITDGEPtdSDWEAALQRLkdGEAAKKANIFAIGVGPDA 153
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 446-506 2.23e-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: 42.51  E-value: 2.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54112397  446 QEHDVVWTEAYIDStlpqaqkltdDQGPVLMTTVAMPVFskqnetrSKGILLGVVGTDVPV 506
Cdd:cd12913   96 ETGKPVWTEPYIDE----------VGTGVLMITISVPIY-------DNGKFIGVVGVDISL 139
VWA_2 pfam13519
von Willebrand factor type A domain;
257-351 7.34e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.97  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397    257 VVILVDVSGSM-----KGLRLTIAKQTVSSILDTLgDDDFFNIIAYNEELHyvepclngtLVQADRTNKEHFREHLDKLF 331
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPE---------VLIPLTKDRAKILRALRRLE 70

                           90       100
                   ....*....|....*....|.
gi 54112397    332 AKGIGM-LDIALNEAFNILSD 351
Cdd:pfam13519   71 PKGGGTnLAAALQLARAALKH 91
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 255-371 1.62e-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: 40.02  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54112397  255 KDVVILVDVSGSMKGLRLTIAKQTVSSILDTlgdddffnIIAYNEELHYVepCLNGTLVQADRTNKEHFREHLDKLFA-K 333
Cdd:cd01462    1 GPVILLVDQSGSMYGAPEEVAKAVALALLRI--------ALAENRDTYLI--LFDSEFQTKIVDKTDDLEEPVEFLSGvQ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 54112397  334 GIGMLDI--ALNEAFNILSdfNHTGQGSIcsqaIMLITDG 371
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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