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Conserved domains on  [gi|746156574|ref|WP_039217148|]
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type III secretion system inner membrane ring subunit SctD [Burkholderia multivorans]

Protein Classification

EscD/YscD/HrpQ family type III secretion system inner membrane ring protein( domain architecture ID 11494372)

EscD/YscD/HrpQ family type III secretion system inner membrane ring protein similar to Escherichia coli Pas, a novel protein required for protein secretion and attaching and effacing activities of enterohemorrhagic Escherichia coli

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type_III_yscD TIGR02500
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved ...
 29-392 1.58e-94

type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


:

Pssm-ID: 274166 [Multi-domain]  Cd Length: 410  Bit Score: 290.88  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574   29 WNLCFLSGPMYGRTMSLARGANWVGTAA-DCEVILPDREIGAKQVCLQVGALAVTVQN----HGGESGAPVLLNDEPLGS 103
Cdd:TIGR02500   1 WKLRVLSGPHRGAELPLPEGNLVLGTDAaDCDIVLSDGGIAAVHVSLHVRLEGVTLAGavepAWEEGGVLPDEEGTPLPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  104 GRRSLTPQDVVTVGS---------------------------------------IRFGIARHAQASVAVPDDTGAPDVAP 144
Cdd:TIGR02500  81 GTPLLVAGVAFALGEvddalpdtevtprqsaepappprrartslpllllalfllLSGATASGLWPSVAAPPVTDPPADVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  145 ---AAPWLGWLTGGLRRLGSRRLvIALVALWVGVLLGALGYGFVAWSGRLPWQHESVLARTHRLQRLLHAYP--ELAVAP 219
Cdd:TIGR02500 161 aqlAEAGLHAVRAEWRERGNLLL-SGLVADSTQKLPLALWLKSLGIRYRLEVICDDELRREVRDVLSLMGYHdaEVSVGP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  220 RDDGVIVSGYVADPAARERVAQIVSGVDN-AALGTVYVVSDLVATAQTYFSDTALTVAYLGRgrIELTGTAPRAQLEPRI 298
Cdd:TIGR02500 240 EPGGLLISGYVADGKQWLKVADLLRAIVPlAGWRIVRVASDVIAQLASLLSDAGLLGVVTVT--ESGREIALSGQLDSEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  299 RNYMKDARPALEVVDHVrDAQADAPRTTTTLGGSAGIPEITTVFAGDGDQRYIETVDGSRYFEGARLKEGPTVVSIGPDE 378
Cdd:TIGR02500 318 RSRLQELLAAFKQRDGV-IPDVVLQNIPAADGTSDELPFPVVSISGSGPNPYVVLADGQRLFVGARLPGGYRIVAISPDG 396

                         410
                  ....*....|....
gi 746156574  379 VVFERNGQRITMPL 392
Cdd:TIGR02500 397 LTLEKGGRLIRIPL 410
 
Name Accession Description Interval E-value
type_III_yscD TIGR02500
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved ...
 29-392 1.58e-94

type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274166 [Multi-domain]  Cd Length: 410  Bit Score: 290.88  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574   29 WNLCFLSGPMYGRTMSLARGANWVGTAA-DCEVILPDREIGAKQVCLQVGALAVTVQN----HGGESGAPVLLNDEPLGS 103
Cdd:TIGR02500   1 WKLRVLSGPHRGAELPLPEGNLVLGTDAaDCDIVLSDGGIAAVHVSLHVRLEGVTLAGavepAWEEGGVLPDEEGTPLPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  104 GRRSLTPQDVVTVGS---------------------------------------IRFGIARHAQASVAVPDDTGAPDVAP 144
Cdd:TIGR02500  81 GTPLLVAGVAFALGEvddalpdtevtprqsaepappprrartslpllllalfllLSGATASGLWPSVAAPPVTDPPADVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  145 ---AAPWLGWLTGGLRRLGSRRLvIALVALWVGVLLGALGYGFVAWSGRLPWQHESVLARTHRLQRLLHAYP--ELAVAP 219
Cdd:TIGR02500 161 aqlAEAGLHAVRAEWRERGNLLL-SGLVADSTQKLPLALWLKSLGIRYRLEVICDDELRREVRDVLSLMGYHdaEVSVGP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  220 RDDGVIVSGYVADPAARERVAQIVSGVDN-AALGTVYVVSDLVATAQTYFSDTALTVAYLGRgrIELTGTAPRAQLEPRI 298
Cdd:TIGR02500 240 EPGGLLISGYVADGKQWLKVADLLRAIVPlAGWRIVRVASDVIAQLASLLSDAGLLGVVTVT--ESGREIALSGQLDSEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  299 RNYMKDARPALEVVDHVrDAQADAPRTTTTLGGSAGIPEITTVFAGDGDQRYIETVDGSRYFEGARLKEGPTVVSIGPDE 378
Cdd:TIGR02500 318 RSRLQELLAAFKQRDGV-IPDVVLQNIPAADGTSDELPFPVVSISGSGPNPYVVLADGQRLFVGARLPGGYRIVAISPDG 396

                         410
                  ....*....|....
gi 746156574  379 VVFERNGQRITMPL 392
Cdd:TIGR02500 397 LTLEKGGRLIRIPL 410
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 33-121 1.82e-09

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 54.57  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574   33 FLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGgeSGAPVLLNDEPLGSGRRSLTPQD 112
Cdd:pfam16697   2 VLSGPHAGAEFPLEGGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLG--SGNGTLVNGQRVTELGIALRPGD 79


                  ....*....
gi 746156574  113 VVTVGSIRF 121
Cdd:pfam16697  80 RIELGQTEF 88
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 31-121 7.99e-09

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 52.66  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  31 LCFLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGgeSGAPVLLNDEPLgSGRRSLTP 110
Cdd:cd00060    2 LIVLDGDGGGREFPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLG--STNGTFVNGKRI-TPPVPLQD 78

                         90
                 ....*....|.
gi 746156574 111 QDVVTVGSIRF 121
Cdd:cd00060   79 GDVIRLGDTTF 89
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
31-121 4.43e-06

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.95  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  31 LCFLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGGESGapVLLNDEPLgSGRRSLTP 110
Cdd:COG1716    4 LVVLEGPLAGRRFPLDGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNG--TFVNGQRV-TEPAPLRD 80

                         90
                 ....*....|.
gi 746156574 111 QDVVTVGSIRF 121
Cdd:COG1716   81 GDVIRLGKTEL 91
 
Name Accession Description Interval E-value
type_III_yscD TIGR02500
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved ...
 29-392 1.58e-94

type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274166 [Multi-domain]  Cd Length: 410  Bit Score: 290.88  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574   29 WNLCFLSGPMYGRTMSLARGANWVGTAA-DCEVILPDREIGAKQVCLQVGALAVTVQN----HGGESGAPVLLNDEPLGS 103
Cdd:TIGR02500   1 WKLRVLSGPHRGAELPLPEGNLVLGTDAaDCDIVLSDGGIAAVHVSLHVRLEGVTLAGavepAWEEGGVLPDEEGTPLPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  104 GRRSLTPQDVVTVGS---------------------------------------IRFGIARHAQASVAVPDDTGAPDVAP 144
Cdd:TIGR02500  81 GTPLLVAGVAFALGEvddalpdtevtprqsaepappprrartslpllllalfllLSGATASGLWPSVAAPPVTDPPADVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  145 ---AAPWLGWLTGGLRRLGSRRLvIALVALWVGVLLGALGYGFVAWSGRLPWQHESVLARTHRLQRLLHAYP--ELAVAP 219
Cdd:TIGR02500 161 aqlAEAGLHAVRAEWRERGNLLL-SGLVADSTQKLPLALWLKSLGIRYRLEVICDDELRREVRDVLSLMGYHdaEVSVGP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  220 RDDGVIVSGYVADPAARERVAQIVSGVDN-AALGTVYVVSDLVATAQTYFSDTALTVAYLGRgrIELTGTAPRAQLEPRI 298
Cdd:TIGR02500 240 EPGGLLISGYVADGKQWLKVADLLRAIVPlAGWRIVRVASDVIAQLASLLSDAGLLGVVTVT--ESGREIALSGQLDSEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  299 RNYMKDARPALEVVDHVrDAQADAPRTTTTLGGSAGIPEITTVFAGDGDQRYIETVDGSRYFEGARLKEGPTVVSIGPDE 378
Cdd:TIGR02500 318 RSRLQELLAAFKQRDGV-IPDVVLQNIPAADGTSDELPFPVVSISGSGPNPYVVLADGQRLFVGARLPGGYRIVAISPDG 396

                         410
                  ....*....|....
gi 746156574  379 VVFERNGQRITMPL 392
Cdd:TIGR02500 397 LTLEKGGRLIRIPL 410
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 33-121 1.82e-09

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 54.57  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574   33 FLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGgeSGAPVLLNDEPLGSGRRSLTPQD 112
Cdd:pfam16697   2 VLSGPHAGAEFPLEGGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLG--SGNGTLVNGQRVTELGIALRPGD 79


                  ....*....
gi 746156574  113 VVTVGSIRF 121
Cdd:pfam16697  80 RIELGQTEF 88
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 31-121 7.99e-09

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 52.66  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  31 LCFLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGgeSGAPVLLNDEPLgSGRRSLTP 110
Cdd:cd00060    2 LIVLDGDGGGREFPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLG--STNGTFVNGKRI-TPPVPLQD 78

                         90
                 ....*....|.
gi 746156574 111 QDVVTVGSIRF 121
Cdd:cd00060   79 GDVIRLGDTTF 89
T2SSB pfam16537
Type II secretion system protein B; This is the B protein from some operons of bacterial ...
 341-391 1.10e-08

Type II secretion system protein B; This is the B protein from some operons of bacterial secretion systems of type II. The exact function of the B protein is not known, though in the case of Vibrio cholerae there is a fusion protein between proteins A and B that includes an AAA domain, a PG_binding domains well as this domain at the C-terminus. Many of the other species have no A or B domain genes in this operon. The type II secretion pathway is conserved in Gram-negative bacteria that are prevalent in bacterial pathogens of plants (Pseudomonas fluorescens, Erwinia or Xanthomonas species), animals (Aeromonas hydrophila) and humans (Klebsiella oxytoca, Pseudomonas aeruginosa, Vibrio cholerae or Legionella pneumophila). Typical type II secretion systems (T2SSs) are encoded by a set of 12 to 16 gsp (general secretion pathway) genes organized into large operons including the conserved 'core' genes denoted C to O and in some bacterial species, as indicated above, extra gsp genes such as gspAB, gspN or gspS. A different nomenclature is used for Pseudomonas T2SSs, so the B gene is referred to as the P protein.


Pssm-ID: 435407  Cd Length: 60  Bit Score: 51.41  E-value: 1.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 746156574  341 VFAGDGDQRYIeTVDGSRYFEGARLKEGPTVVSIGPDEVVFERNGQRITMP 391
Cdd:pfam16537  10 VYSSNPANRWV-IINGQELREGDTIAPGLTLEEIRPDGVVLRFDGQRFRLP 59
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
31-121 4.43e-06

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.95  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  31 LCFLSGPMYGRTMSLARGANWVGTAADCEVILPDREIGAKQVCLQVGALAVTVQNHGGESGapVLLNDEPLgSGRRSLTP 110
Cdd:COG1716    4 LVVLEGPLAGRRFPLDGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNG--TFVNGQRV-TEPAPLRD 80

                         90
                 ....*....|.
gi 746156574 111 QDVVTVGSIRF 121
Cdd:COG1716   81 GDVIRLGKTEL 91
FHA_YscD-like cd22710
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation ...
 33-123 5.80e-06

forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation protein D (YscD) and similar proteins; YscD protein is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD protein contains an N-terminal cytoplasmic domain, a transmembrane linker and a large periplasmic domain. The cytoplasmic domain consists of a forkhead-associated (FHA) fold. The FHA domain is a small phosphopeptide recognition module. Due to the lack of the conserved residues that are required for binding phosphothreonine, the cytoplasmic domain of YscD protein is therefore unlikely to function as a true FHA domain.


Pssm-ID: 438762 [Multi-domain]  Cd Length: 94  Bit Score: 44.70  E-value: 5.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  33 FLSGPMYGRTMSLARGANWVGT-AADCEVILPDREIGAKQVCLQVGALAVTVQNhggeSGAPVLLNDEPLGSGRRsLTPQ 111
Cdd:cd22710    4 ILSGNHRGAEVPLPPGRYVLGSdPLQCDLVLTDSGISPVHLVLEVDDGGVRLLD----SAEPLYQNGEPVVLGVL-LNAF 78

                         90
                 ....*....|..
gi 746156574 112 DVVTVGSIRFGI 123
Cdd:cd22710   79 SIISVGFLFWTI 90
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 52-148 1.50e-03

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 40.52  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746156574  52 VGTAADCEVILPDREigakqvcLQVGALAVTVQNHGGE------SGAPVLLN--DEPLGSGRR-SLTPQDVVTVGSIRFG 122
Cdd:COG3456   30 IGRSADCDWVLPDPD-------RSVSRRHAEIRFRDGAfcltdlSTNGTFLNgsDHPLGPGRPvRLRDGDRLRIGDYEIR 102

                         90       100
                 ....*....|....*....|....*.
gi 746156574 123 IARHAQASVAVPDDTGAPDVAPAAPW 148
Cdd:COG3456  103 VEISGEDEGADDPLAAAPEPAVSSPS 128
 
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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