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Conserved domains on  [gi|446152418|ref|WP_000230273|]
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MULTISPECIES: RidA family protein [Enterobacteriaceae]

Protein Classification

RidA family protein( domain architecture ID 10115180)

RidA (reactive intermediate/imine deaminase A) family protein similar to 2-iminobutanoate/2-iminopropanoate deaminase, which catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 19-128 7.33e-60

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


:

Pssm-ID: 100005  Cd Length: 111  Bit Score: 179.77  E-value: 7.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  19 HRYSAAIRSGDLLFVSGQVGSREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEKQFEDIMTVKNEI 98
Cdd:cd02198    1 FGYSPAVRVGDTLFVSGQVGSDADGSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAHLPAFAAVKDEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446152418  99 FSApPYPNWTAVGVTWLA--GFDFEIKVIARI 128
Cdd:cd02198   81 FKE-PYPAWTAVGVAWLArpGLLVEIKVVAVR 111
 
Name Accession Description Interval E-value
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 19-128 7.33e-60

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100005  Cd Length: 111  Bit Score: 179.77  E-value: 7.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  19 HRYSAAIRSGDLLFVSGQVGSREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEKQFEDIMTVKNEI 98
Cdd:cd02198    1 FGYSPAVRVGDTLFVSGQVGSDADGSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAHLPAFAAVKDEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446152418  99 FSApPYPNWTAVGVTWLA--GFDFEIKVIARI 128
Cdd:cd02198   81 FKE-PYPAWTAVGVAWLArpGLLVEIKVVAVR 111
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 13-126 1.38e-39

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 128.57  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418   13 HSLYAEHRYSAAIRSGDLLFVSGQVGSREDGTP--EPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPeKQFED 90
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKlvEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADM-NDFAE 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446152418   91 IMTVKNEIFSAPPYPNWTAVGVTWLA-GFDFEIKVIA 126
Cdd:pfam01042  80 VNEVYAEYFDADKAPARSAVGVAALPlGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 21-129 2.92e-33

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 112.96  E-value: 2.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  21 YSAAIRSGDLLFVSGQVGSRED-GTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEkQFEDIMTVKNEIF 99
Cdd:COG0251   17 YSQAVRVGNLVFVSGQVPLDPDtGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMA-DFAAVNEVYAEYF 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446152418 100 sAPPYPNWTAVGVTWLA-GFDFEIKVIARIP 129
Cdd:COG0251   96 -GEGRPARTAVGVAALPkGALVEIEAIAALP 125
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 21-126 3.49e-18

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 74.25  E-value: 3.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418   21 YSAAIRSGDLLFVSGQVG-SREDGT-PEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDpekqFEDIMTVkNEI 98
Cdd:TIGR00004  16 YSQAVKVGNTVYVSGQIPlDPSTGElVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD----LNDFAEV-NEV 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 446152418   99 FS---APPYPNWTAVGVTWLA-GFDFEIKVIA 126
Cdd:TIGR00004  91 YGqyfDEHYPARSAVQVAALPkGVLVEIEAIA 122
PRK11401 PRK11401
enamine/imine deaminase;
10-126 1.59e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 44.29  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  10 AGRHSLYAEHRYSAAIRSGDLLFVSGQVG-SREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDpEKQF 88
Cdd:PRK11401   6 ETQRAPGAIGPYVQGVDLGSMVFTSGQIPvCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD-LNDF 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446152418  89 EDIMTVKNEIFS--APPYPNWTAVGVTWL-AGFDFEIKVIA 126
Cdd:PRK11401  85 ATINEVYKQFFDehQATYPTRSCVQVARLpKDVKLEIEAIA 125
 
Name Accession Description Interval E-value
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 19-128 7.33e-60

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100005  Cd Length: 111  Bit Score: 179.77  E-value: 7.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  19 HRYSAAIRSGDLLFVSGQVGSREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEKQFEDIMTVKNEI 98
Cdd:cd02198    1 FGYSPAVRVGDTLFVSGQVGSDADGSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAHLPAFAAVKDEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446152418  99 FSApPYPNWTAVGVTWLA--GFDFEIKVIARI 128
Cdd:cd02198   81 FKE-PYPAWTAVGVAWLArpGLLVEIKVVAVR 111
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 13-126 1.38e-39

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 128.57  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418   13 HSLYAEHRYSAAIRSGDLLFVSGQVGSREDGTP--EPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPeKQFED 90
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKlvEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADM-NDFAE 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446152418   91 IMTVKNEIFSAPPYPNWTAVGVTWLA-GFDFEIKVIA 126
Cdd:pfam01042  80 VNEVYAEYFDADKAPARSAVGVAALPlGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 21-129 2.92e-33

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 112.96  E-value: 2.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  21 YSAAIRSGDLLFVSGQVGSRED-GTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEkQFEDIMTVKNEIF 99
Cdd:COG0251   17 YSQAVRVGNLVFVSGQVPLDPDtGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMA-DFAAVNEVYAEYF 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446152418 100 sAPPYPNWTAVGVTWLA-GFDFEIKVIARIP 129
Cdd:COG0251   96 -GEGRPARTAVGVAALPkGALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 21-126 5.47e-33

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 111.50  E-value: 5.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  21 YSAAIRSGDLLFVSGQVGSREDGTPEP-DFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEkQFEDIMTVKNEIF 99
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPgDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMA-DFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 446152418 100 SAPPYPNWTAVGVTWL-AGFDFEIKVIA 126
Cdd:cd00448   80 GEGPPPARTAVGVAALpPGALVEIEAIA 107
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 21-126 3.49e-18

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 74.25  E-value: 3.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418   21 YSAAIRSGDLLFVSGQVG-SREDGT-PEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDpekqFEDIMTVkNEI 98
Cdd:TIGR00004  16 YSQAVKVGNTVYVSGQIPlDPSTGElVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD----LNDFAEV-NEV 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 446152418   99 FS---APPYPNWTAVGVTWLA-GFDFEIKVIA 126
Cdd:TIGR00004  91 YGqyfDEHYPARSAVQVAALPkGVLVEIEAIA 122
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 21-126 5.89e-15

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100011  Cd Length: 119  Bit Score: 66.04  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  21 YSAAIRSGDLLFVSGQVGSREDGTPEP-DFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDPEkQFEDIMTVKNEIF 99
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGMVMPgDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIA-DFEAVGRAHGEVF 91

                         90       100
                 ....*....|....*....|....*....
gi 446152418 100 SAPPyPNWTAVGVTWLAGFDF--EIKVIA 126
Cdd:cd06154   92 GDIR-PAATMVVVSLLVDPEMlvEIEVTA 119
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 21-126 1.60e-14

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100009  Cd Length: 114  Bit Score: 64.64  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  21 YSAAIRSGDLLFVSGQVG-SREDGTPEPDFQQQVRLAFDNLHATLAAAGCT-FDDIIDVTSFHTD--PEKQFEdiMTVKN 96
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGwDPDTGKIPEDLEEEIDQAFDNVELALKAAGGKgWEQVYKVNSYHVDikNEEAFG--LMVEN 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446152418  97 EIFSAPPY-PNWTAVGVTWLA--GFDFEIKVIA 126
Cdd:cd06152   81 FKKWMPNHqPIWTCVGVTALGlpGMRVEIEVDA 113
PRK11401 PRK11401
enamine/imine deaminase;
10-126 1.59e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 44.29  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446152418  10 AGRHSLYAEHRYSAAIRSGDLLFVSGQVG-SREDGTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTDpEKQF 88
Cdd:PRK11401   6 ETQRAPGAIGPYVQGVDLGSMVFTSGQIPvCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD-LNDF 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446152418  89 EDIMTVKNEIFS--APPYPNWTAVGVTWL-AGFDFEIKVIA 126
Cdd:PRK11401  85 ATINEVYKQFFDehQATYPTRSCVQVARLpKDVKLEIEAIA 125
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-83 1.78e-04

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100007  Cd Length: 105  Bit Score: 38.29  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446152418  20 RYSAAIRSGDLLFVSGQVGSredgTPEPDFQQQVRLAFDNLHATLAAAGCTFDDIIDVTSFHTD 83
Cdd:cd06150    2 RMSQAVVHNGTVYLAGQVAD----DTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLAD 61
Rad60-SLD pfam11976
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ...
 46-77 3.14e-03

Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localization, or by protecting substrates from ubiquitination. Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). Despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9)), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. Structural analysis of PDB:2uyz reveals a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating SUMOylation. The Rad60 branch of this family is also known as RENi (Rad60-Esc2-Nip45), and biologically it should be two distinct families SUMO and RENi (Rad60-Esc2-Nip45).


Pssm-ID: 403255 [Multi-domain]  Cd Length: 72  Bit Score: 34.07  E-value: 3.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446152418   46 EPDFQQQVRLAFD----NLHATLAAAGCTFDDIIDV 77
Cdd:pfam11976  35 GIPPSQQVRLIFDgerlDPNSTVEDLDIEDGDTIDV 70
PRK14093 PRK14093
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ...
 7-40 6.23e-03

UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional


Pssm-ID: 184501 [Multi-domain]  Cd Length: 479  Bit Score: 35.14  E-value: 6.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446152418   7 VFPAGRHSLYAEH------RYSAAIRSGDLLFVSGQVGSR 40
Cdd:PRK14093 417 ALSSGKRGGYAEDaaalesQVVAAIRAGDVIMVKGSLGSR 456
 
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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