NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|506420102|ref|WP_015939821|]
View 

myo-inosose-2 dehydratase [Glaesserella parasuis]

Protein Classification

IolE/MocC family protein( domain architecture ID 1001934)

IolE/MocC family similar to Salmonella enterica inosose dehydratase (IolE) and Sinorhizobium meliloti rhizopine catabolism protein MocC

CATH:  3.20.20.150

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
VpdB_C super family cl30226
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
5-296 1.88e-161

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


The actual alignment was detected with superfamily member TIGR04379:

Pssm-ID: 421976  Cd Length: 290  Bit Score: 450.57  E-value: 1.88e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102    5 NIQLGIAPIGWTNDDLPELGAENTFEQCVSEMALAGYTGCEVGNKYPRDVAVLKHKLDVRGIQICNAWFSTFFVDGKREE 84
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   85 TIQEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTKAVFKEKPIFNDEDWQRLAEGYNELAKLAAEKGMKVSLHHHMGTGIQ 164
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  165 TPEEVDRYMSVVNDD-VYLLFDSGHLYYSEGcqkAMLAVLEKYIHRIVHVHLKDVRDEVVAEVKAKDLSFLEGVKKGTFT 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPElVGLLYDTGHATFAGG---DPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFT 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506420102  244 VPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPALANPFEYALKGRKYIREVA 296
Cdd:TIGR04379 238 VPGDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
5-296 1.88e-161

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 450.57  E-value: 1.88e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102    5 NIQLGIAPIGWTNDDLPELGAENTFEQCVSEMALAGYTGCEVGNKYPRDVAVLKHKLDVRGIQICNAWFSTFFVDGKREE 84
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   85 TIQEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTKAVFKEKPIFNDEDWQRLAEGYNELAKLAAEKGMKVSLHHHMGTGIQ 164
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  165 TPEEVDRYMSVVNDD-VYLLFDSGHLYYSEGcqkAMLAVLEKYIHRIVHVHLKDVRDEVVAEVKAKDLSFLEGVKKGTFT 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPElVGLLYDTGHATFAGG---DPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFT 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506420102  244 VPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPALANPFEYALKGRKYIREVA 296
Cdd:TIGR04379 238 VPGDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
6-295 2.60e-57

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 184.83  E-value: 2.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   6 IQLGIAPIGWTNDDLpelgaentfEQCVSEMALAGYTGCEVGNKY--PRDVAVLKHKLDVRGIQICNAWFSTFFV---DG 80
Cdd:COG1082    1 MKLGLSTYSLPDLDL---------EEALRAAAELGYDGVELAGGDldEADLAELRAALADHGLEISSLHAPGLNLapdPE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  81 KREETIQEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTkavfkekpifNDEDWQRLAEGYNELAKLAAEKGMKVSLHHHMG 160
Cdd:COG1082   72 VREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLP----------PEEAWDRLAERLRELAELAEEAGVTLALENHEG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 161 TGIQTPEEVDRYMSVVN-DDVYLLFDSGHLYYSEGcqkAMLAVLEKYIHRIVHVHLKDVRDEvvaevkakdlsflegvkk 239
Cdd:COG1082  142 TFVNTPEEALRLLEAVDsPNVGLLLDTGHALLAGE---DPVELLRKLGDRIKHVHLKDADGD------------------ 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506420102 240 gTFTVPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPalANPFEYALKGRKYIREV 295
Cdd:COG1082  201 -QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDP--DDPEEAARESLEYLRKL 253
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
39-294 2.41e-30

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 114.39  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   39 AGYTGCEV-------GNKYPRDVAVLKHKLDVRGIQICnaWFSTFFVDG-------KREETIQEFIKHRDFLHAMGAKVI 104
Cdd:pfam01261   7 LGFDGVELftrrwfrPPLSDEEAEELKAALKEHGLEIV--VHAPYLGDNlaspdeeEREKAIDRLKRAIELAAALGAKLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  105 gcseqsRSIQGTTKAVFKEkpifndEDWQRLAEGYNELAKLAAEKGMKVSLHHHMGTGIQ---TPEEVDRYMSVVNDD-V 180
Cdd:pfam01261  85 ------VFHPGSDLGDDPE------EALARLAESLRELADLAEREGVRLALEPLAGKGTNvgnTFEEALEIIDEVDSPnV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  181 YLLFDSGHLYYSEGCQKAMLAVLEKYIHrivHVHLKDVRDEvvaevkakdlsflEGVKKGTFTVPGDGVIDFKPIFDILE 260
Cdd:pfam01261 153 GVCLDTGHLFAAGDGDLFELRLGDRYIG---HVHLKDSKNP-------------LGSGPDRHVPIGEGVIDFEALFRALK 216
                         250       260       270
                  ....*....|....*....|....*....|....
gi 506420102  261 KYDYKGWMVVEAEQDPalaNPFEYALKGRKYIRE 294
Cdd:pfam01261 217 EIGYDGPLSLETFNDG---PPEEGAREGLEWLRE 247
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
202-284 1.59e-08

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 52.28  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 202 VLEKYIHRIVHVHLKDVRDEVVAEVKAKDLSFLEGVKKGtfTVPGDGVIDFKPIFDILEKY----DYKGWMVVEAEQDPA 277
Cdd:cd22304   31 HVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLREFNYALLISPLVsnqqEINFSKEIRKEIDSL 108

                 ....*..
gi 506420102 278 LANPFEY 284
Cdd:cd22304  109 KRLPGLY 115
PRK13210 PRK13210
L-ribulose-5-phosphate 3-epimerase;
203-271 5.81e-04

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237308  Cd Length: 284  Bit Score: 40.66  E-value: 5.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506420102 203 LEKYIHRIVHVHLKDVRdEVVAEVKAK--DLSFlegvkkgtftvpGDGVIDFKPIFDILEKYDYKGWMVVE 271
Cdd:PRK13210 197 LKLGIDHIAAIHLKDTY-AVTETSKGQfrDVPF------------GEGCVDFVGIFKTLKELNYRGPFLIE 254
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
5-296 1.88e-161

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 450.57  E-value: 1.88e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102    5 NIQLGIAPIGWTNDDLPELGAENTFEQCVSEMALAGYTGCEVGNKYPRDVAVLKHKLDVRGIQICNAWFSTFFVDGKREE 84
Cdd:TIGR04379   1 KVKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   85 TIQEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTKAVFKEKPIFNDEDWQRLAEGYNELAKLAAEKGMKVSLHHHMGTGIQ 164
Cdd:TIGR04379  81 EIEAFRPHLEFLKAMGAKVIVVCETGGSIQGDPDTPLSDRPVLTDEEWERLGEGLNRLGEIAAEQGMKLAYHHHMGTVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  165 TPEEVDRYMSVVNDD-VYLLFDSGHLYYSEGcqkAMLAVLEKYIHRIVHVHLKDVRDEVVAEVKAKDLSFLEGVKKGTFT 243
Cdd:TIGR04379 161 TEEEIDRLMAMTDPElVGLLYDTGHATFAGG---DPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFT 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506420102  244 VPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPALANPFEYALKGRKYIREVA 296
Cdd:TIGR04379 238 VPGDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
6-295 2.60e-57

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 184.83  E-value: 2.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   6 IQLGIAPIGWTNDDLpelgaentfEQCVSEMALAGYTGCEVGNKY--PRDVAVLKHKLDVRGIQICNAWFSTFFV---DG 80
Cdd:COG1082    1 MKLGLSTYSLPDLDL---------EEALRAAAELGYDGVELAGGDldEADLAELRAALADHGLEISSLHAPGLNLapdPE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  81 KREETIQEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTkavfkekpifNDEDWQRLAEGYNELAKLAAEKGMKVSLHHHMG 160
Cdd:COG1082   72 VREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLP----------PEEAWDRLAERLRELAELAEEAGVTLALENHEG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 161 TGIQTPEEVDRYMSVVN-DDVYLLFDSGHLYYSEGcqkAMLAVLEKYIHRIVHVHLKDVRDEvvaevkakdlsflegvkk 239
Cdd:COG1082  142 TFVNTPEEALRLLEAVDsPNVGLLLDTGHALLAGE---DPVELLRKLGDRIKHVHLKDADGD------------------ 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506420102 240 gTFTVPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPalANPFEYALKGRKYIREV 295
Cdd:COG1082  201 -QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDP--DDPEEAARESLEYLRKL 253
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
39-294 2.41e-30

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 114.39  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102   39 AGYTGCEV-------GNKYPRDVAVLKHKLDVRGIQICnaWFSTFFVDG-------KREETIQEFIKHRDFLHAMGAKVI 104
Cdd:pfam01261   7 LGFDGVELftrrwfrPPLSDEEAEELKAALKEHGLEIV--VHAPYLGDNlaspdeeEREKAIDRLKRAIELAAALGAKLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  105 gcseqsRSIQGTTKAVFKEkpifndEDWQRLAEGYNELAKLAAEKGMKVSLHHHMGTGIQ---TPEEVDRYMSVVNDD-V 180
Cdd:pfam01261  85 ------VFHPGSDLGDDPE------EALARLAESLRELADLAEREGVRLALEPLAGKGTNvgnTFEEALEIIDEVDSPnV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  181 YLLFDSGHLYYSEGCQKAMLAVLEKYIHrivHVHLKDVRDEvvaevkakdlsflEGVKKGTFTVPGDGVIDFKPIFDILE 260
Cdd:pfam01261 153 GVCLDTGHLFAAGDGDLFELRLGDRYIG---HVHLKDSKNP-------------LGSGPDRHVPIGEGVIDFEALFRALK 216
                         250       260       270
                  ....*....|....*....|....*....|....
gi 506420102  261 KYDYKGWMVVEAEQDPalaNPFEYALKGRKYIRE 294
Cdd:pfam01261 217 EIGYDGPLSLETFNDG---PPEEGAREGLEWLRE 247
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
202-284 1.59e-08

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 52.28  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 202 VLEKYIHRIVHVHLKDVRDEVVAEVKAKDLSFLEGVKKGtfTVPGDGVIDFKPIFDILEKY----DYKGWMVVEAEQDPA 277
Cdd:cd22304   31 HVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLREFNYALLISPLVsnqqEINFSKEIRKEIDSL 108

                 ....*..
gi 506420102 278 LANPFEY 284
Cdd:cd22304  109 KRLPGLY 115
SgaU COG3623
L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];
111-294 8.10e-06

L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];


Pssm-ID: 442841  Cd Length: 277  Bit Score: 46.38  E-value: 8.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 111 RSIQGTTKAVFKEKPifNDEDWQRLAEGYNELAKLAAEKGmkVSL------HHHMGTgiqtpeeVDRYMSVVND------ 178
Cdd:COG3623  107 RTIQLAGYDVYYEPS--DEETRQRFIEGLKKAVELAARAG--VMLaieimdTPFMNS-------ISKAMELVKEidspwl 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 179 ----DVYLLFDSGHLYYSEgcqkamlavLEKYIHRIVHVHLKDVRdevvaevkakdlsflegvkKGTF-TVP-GDGVIDF 252
Cdd:COG3623  176 qvypDIGNLSAWGNDVADE---------LELGIGHIVAIHLKDTL-------------------PGQFrDVPfGEGCVDF 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 506420102 253 KPIFDILEKYDYKGWMVVE--AEQDPalaNPFEYALKGRKYIRE 294
Cdd:COG3623  228 VAAFKTLKRLGYRGPFLIEmwNEDAE---DWVAEIRQARDFLEQ 268
PRK13210 PRK13210
L-ribulose-5-phosphate 3-epimerase;
203-271 5.81e-04

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237308  Cd Length: 284  Bit Score: 40.66  E-value: 5.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506420102 203 LEKYIHRIVHVHLKDVRdEVVAEVKAK--DLSFlegvkkgtftvpGDGVIDFKPIFDILEKYDYKGWMVVE 271
Cdd:PRK13210 197 LKLGIDHIAAIHLKDTY-AVTETSKGQfrDVPF------------GEGCVDFVGIFKTLKELNYRGPFLIE 254
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
81-266 3.57e-03

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 38.46  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102  81 KREETIQEFIKHRDFLHAMGAKVIgcseqsrsiqgttkaVF---KEKPIFNDEDWQRLAEGYNELAKLAAEKGMKVSL-- 155
Cdd:cd00019   79 KREKSIERLKDEIERCEELGIRLL---------------VFhpgSYLGQSKEEGLKRVIEALNELIDKAETKGVVIALet 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 156 ----HHHMGTGIqtpEEVDRYMSVVNDDVYLLF--DSGHLY---YSEGCQKAMLAVLEKYIH-----RIVHVHLKDVRDE 221
Cdd:cd00019  144 magqGNEIGSSF---EELKEIIDLIKEKPRVGVciDTCHIFaagYDISTVEGFEKVLEEFDKvigleYLKAIHLNDSKGE 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 506420102 222 VVAEVKaKDLSFlegvkkgtftvpGDGVIDFKPIFDILEKYDYKG 266
Cdd:cd00019  221 LGSGKD-RHEPI------------GEGDIDGEELFKELKKDPYQN 252
PRK13209 PRK13209
L-ribulose-5-phosphate 3-epimerase;
209-294 7.87e-03

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237307  Cd Length: 283  Bit Score: 37.28  E-value: 7.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420102 209 RIVHVHLKDVRDEVVaevkaKDLSFlegvkkgtftvpGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPAlANPFEYALKG 288
Cdd:PRK13209 208 HIVAFHVKDTKPGVF-----KNVPF------------GEGVVDFERCFKTLKQSGYCGPYLIEMWSETA-EDPAAEVAKA 269

                 ....*.
gi 506420102 289 RKYIRE 294
Cdd:PRK13209 270 RDFVKA 275
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH