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Conserved domains on  [gi|573987141|ref|XP_006671491|]
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APAF1-interacting protein [Cordyceps militaris CM01]

Protein Classification

class II aldolase/adducin head domain-containing protein( domain architecture ID 842)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
22-278 1.23e-61

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


The actual alignment was detected with superfamily member TIGR03328:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 192  Bit Score: 193.64  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   22 IPALCAKFWTLGWVTGTGGGCSIR---DECVIphpstassfprphprpplplprsaqsthmltappksdlvylAPSGVQK 98
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARldeDEILI-----------------------------------------TPSGVDK 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   99 ELMKPADIYVLSLSAQdptqPLRSYLRsppsyrPSQCTPLFLAAFTRRGAGCCIHTHSQWAVLVTLLLEQHEEanrnvFE 178
Cdd:TIGR03328  40 GRLTPEDFLVVDLQGK----PVSGGLK------PSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGG-----FE 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  179 VNNIEQIKGFgrgpgrAGNLGYHDTLRIPVIENTPHEEDLTEYLEEAMEAYPDTYAVLVRRHGVYVWGDNVHKAKTQCEs 258
Cdd:TIGR03328 105 LEGYEMLKGL------PGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLE- 177
                         250       260
                  ....*....|....*....|
gi 573987141  259 vcvgySLDYLFQLAVEMKKL 278
Cdd:TIGR03328 178 -----ALEFLFECELEMLKL 192
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
22-278 1.23e-61

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 193.64  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   22 IPALCAKFWTLGWVTGTGGGCSIR---DECVIphpstassfprphprpplplprsaqsthmltappksdlvylAPSGVQK 98
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARldeDEILI-----------------------------------------TPSGVDK 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   99 ELMKPADIYVLSLSAQdptqPLRSYLRsppsyrPSQCTPLFLAAFTRRGAGCCIHTHSQWAVLVTLLLEQHEEanrnvFE 178
Cdd:TIGR03328  40 GRLTPEDFLVVDLQGK----PVSGGLK------PSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGG-----FE 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  179 VNNIEQIKGFgrgpgrAGNLGYHDTLRIPVIENTPHEEDLTEYLEEAMEAYPDTYAVLVRRHGVYVWGDNVHKAKTQCEs 258
Cdd:TIGR03328 105 LEGYEMLKGL------PGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLE- 177
                         250       260
                  ....*....|....*....|
gi 573987141  259 vcvgySLDYLFQLAVEMKKL 278
Cdd:TIGR03328 178 -----ALEFLFECELEMLKL 192
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
22-273 3.54e-32

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 117.35  E-value: 3.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141    22 IPALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappKSDLVYLAPSGVQKELM 101
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-------------------------------------EEDLFLITPSGVDFGEL 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   102 KPADIYVLSLSAQdptqplrsYLRSPPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLleqheeanRNVFEVN 180
Cdd:smart01007  44 TASDLVVVDLDGN--------VVEGGGGPKPSSETPLHLAIYRARpDVGAVVHTHSPYATALAAL--------GKPLPLL 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   181 NIEQIKGFGrgpgrAGNLGYHDtLRIPVIENTPHEEDLTEYLEEAMEAYPdtyAVLVRRHGVYVWGDNVHKAKTQCEsvc 260
Cdd:smart01007 108 PTEQAAAFL-----GGEIPYAP-YAGPGTELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAE--- 175
                          250
                   ....*....|...
gi 573987141   261 vgySLDYLFQLAV 273
Cdd:smart01007 176 ---ELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
20-273 4.06e-32

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 116.88  E-value: 4.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   20 NLIPALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappkSDLVYLAPSGVQKE 99
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP--------------------------------------GDGFLITPSGVDFG 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  100 LMKPADIYVLSLSAQDPTQPLRsylrsppsyrPSQCTPLFLAAF-TRRGAGCCIHTHSQWAVLVTLLleqheeanrnvfe 178
Cdd:pfam00596  43 ELTPEDLVVVDLDGNVVEGGLK----------PSSETPLHLAIYrARPDAGAVVHTHSPYATALSLA------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  179 vnnIEQIKGFGRGPGRAGnlgyhdTLRIPVIEN-TPHEEDLTEYLEEAMEAypDTYAVLVRRHGVYVWGDNVHKAKTQCE 257
Cdd:pfam00596 100 ---KEGLPPITQEAADFL------GGDIPIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAE 168
                         250
                  ....*....|....*.
gi 573987141  258 svcvgySLDYLFQLAV 273
Cdd:pfam00596 169 ------ELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
17-289 2.81e-22

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 92.04  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  17 HPANLIPALCAKFWTLGWVTGTGGGCSIRDecviphpstassfprphprpplplprsaqsthmltapPKSDLVYLAPSGV 96
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARD-------------------------------------RDRGYFLITPSGV 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  97 QKELMKPADIYVLSLSAQdptqplrsylrSPPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLLEQHEEANRN 175
Cdd:cd00398   45 DYEEMTASDLVVVDAQGK-----------VVEGKKPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEGLIPAGHT 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 176 VFEVnnieqikgfgrgpgragnlgyHDTLRIPVIENT---PHEEDLTEYLEEAMeayPDTYAVLVRRHGVYVWGDNVHKA 252
Cdd:cd00398  114 ACAV---------------------YFTGDIPCTPYMtpeTGEDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEA 169
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 573987141 253 ktqcesVCVGYSLDYLFQLAVEMKKLGiPWISDIPRI 289
Cdd:cd00398  170 ------FHLAVVLEVAAEIQLKALSMG-GQLPPISLE 199
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
24-281 1.09e-18

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 82.19  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  24 ALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappkSDLVYLAPSGVQKELMKP 103
Cdd:COG0235   12 AAGRRLARRGLVDGTAGNISVRLD--------------------------------------DDRFLITPSGVDFGELTP 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 104 ADIYVLSLSAQDPTqplrsylrspPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLLEqheeanrnvfEVNNI 182
Cdd:COG0235   54 EDLVVVDLDGNVVE----------GDLKPSSETPLHLAIYRARpDVGAVVHTHSPYATALSALGE----------PLPPL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 183 EQIKGFGRGPgragnlgyhdtlRIPVIE-NTPHEEDLTEYLEEAMEAYPdtyAVLVRRHGVYVWGDNVHKAKTQCEsvcv 261
Cdd:COG0235  114 EQTEAAAFLG------------DVPVVPyAGPGTEELAEAIAEALGDRP---AVLLRNHGVVVWGKDLAEAFDRAE---- 174
                        250       260
                 ....*....|....*....|
gi 573987141 262 gySLDYLFQLAVEMKKLGIP 281
Cdd:COG0235  175 --VLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
131-279 2.88e-15

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 72.78  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 131 RPSQCTPLFLAAFTRRGAGCCIHTHSQWAVLVTLLLEQHEEanrnvFEVNNIEQIKGFGRGPGRAgnlgyhdTLRIPVIE 210
Cdd:PRK06754  75 KPSAETLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGA-----VTFQGQEIIKALGIWEENA-------EIHIPIIE 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573987141 211 NTPHEEDLTEYLEEAMEayPDTYAVLVRRHGVYVWGDNVHKAKTQCEsvcvgySLDYLFQLAVEMKKLG 279
Cdd:PRK06754 143 NHADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLE------AYEFLFSYHIKLLSIQ 203
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
22-278 1.23e-61

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 193.64  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   22 IPALCAKFWTLGWVTGTGGGCSIR---DECVIphpstassfprphprpplplprsaqsthmltappksdlvylAPSGVQK 98
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARldeDEILI-----------------------------------------TPSGVDK 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   99 ELMKPADIYVLSLSAQdptqPLRSYLRsppsyrPSQCTPLFLAAFTRRGAGCCIHTHSQWAVLVTLLLEQHEEanrnvFE 178
Cdd:TIGR03328  40 GRLTPEDFLVVDLQGK----PVSGGLK------PSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGG-----FE 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  179 VNNIEQIKGFgrgpgrAGNLGYHDTLRIPVIENTPHEEDLTEYLEEAMEAYPDTYAVLVRRHGVYVWGDNVHKAKTQCEs 258
Cdd:TIGR03328 105 LEGYEMLKGL------PGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLE- 177
                         250       260
                  ....*....|....*....|
gi 573987141  259 vcvgySLDYLFQLAVEMKKL 278
Cdd:TIGR03328 178 -----ALEFLFECELEMLKL 192
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
22-273 3.54e-32

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 117.35  E-value: 3.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141    22 IPALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappKSDLVYLAPSGVQKELM 101
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-------------------------------------EEDLFLITPSGVDFGEL 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   102 KPADIYVLSLSAQdptqplrsYLRSPPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLleqheeanRNVFEVN 180
Cdd:smart01007  44 TASDLVVVDLDGN--------VVEGGGGPKPSSETPLHLAIYRARpDVGAVVHTHSPYATALAAL--------GKPLPLL 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   181 NIEQIKGFGrgpgrAGNLGYHDtLRIPVIENTPHEEDLTEYLEEAMEAYPdtyAVLVRRHGVYVWGDNVHKAKTQCEsvc 260
Cdd:smart01007 108 PTEQAAAFL-----GGEIPYAP-YAGPGTELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAE--- 175
                          250
                   ....*....|...
gi 573987141   261 vgySLDYLFQLAV 273
Cdd:smart01007 176 ---ELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
20-273 4.06e-32

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 116.88  E-value: 4.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141   20 NLIPALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappkSDLVYLAPSGVQKE 99
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP--------------------------------------GDGFLITPSGVDFG 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  100 LMKPADIYVLSLSAQDPTQPLRsylrsppsyrPSQCTPLFLAAF-TRRGAGCCIHTHSQWAVLVTLLleqheeanrnvfe 178
Cdd:pfam00596  43 ELTPEDLVVVDLDGNVVEGGLK----------PSSETPLHLAIYrARPDAGAVVHTHSPYATALSLA------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  179 vnnIEQIKGFGRGPGRAGnlgyhdTLRIPVIEN-TPHEEDLTEYLEEAMEAypDTYAVLVRRHGVYVWGDNVHKAKTQCE 257
Cdd:pfam00596 100 ---KEGLPPITQEAADFL------GGDIPIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAE 168
                         250
                  ....*....|....*.
gi 573987141  258 svcvgySLDYLFQLAV 273
Cdd:pfam00596 169 ------ELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
17-289 2.81e-22

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 92.04  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  17 HPANLIPALCAKFWTLGWVTGTGGGCSIRDecviphpstassfprphprpplplprsaqsthmltapPKSDLVYLAPSGV 96
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARD-------------------------------------RDRGYFLITPSGV 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  97 QKELMKPADIYVLSLSAQdptqplrsylrSPPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLLEQHEEANRN 175
Cdd:cd00398   45 DYEEMTASDLVVVDAQGK-----------VVEGKKPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEGLIPAGHT 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 176 VFEVnnieqikgfgrgpgragnlgyHDTLRIPVIENT---PHEEDLTEYLEEAMeayPDTYAVLVRRHGVYVWGDNVHKA 252
Cdd:cd00398  114 ACAV---------------------YFTGDIPCTPYMtpeTGEDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEA 169
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 573987141 253 ktqcesVCVGYSLDYLFQLAVEMKKLGiPWISDIPRI 289
Cdd:cd00398  170 ------FHLAVVLEVAAEIQLKALSMG-GQLPPISLE 199
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
24-281 1.09e-18

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 82.19  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  24 ALCAKFWTLGWVTGTGGGCSIRDEcviphpstassfprphprpplplprsaqsthmltappkSDLVYLAPSGVQKELMKP 103
Cdd:COG0235   12 AAGRRLARRGLVDGTAGNISVRLD--------------------------------------DDRFLITPSGVDFGELTP 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 104 ADIYVLSLSAQDPTqplrsylrspPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLLEqheeanrnvfEVNNI 182
Cdd:COG0235   54 EDLVVVDLDGNVVE----------GDLKPSSETPLHLAIYRARpDVGAVVHTHSPYATALSALGE----------PLPPL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 183 EQIKGFGRGPgragnlgyhdtlRIPVIE-NTPHEEDLTEYLEEAMEAYPdtyAVLVRRHGVYVWGDNVHKAKTQCEsvcv 261
Cdd:COG0235  114 EQTEAAAFLG------------DVPVVPyAGPGTEELAEAIAEALGDRP---AVLLRNHGVVVWGKDLAEAFDRAE---- 174
                        250       260
                 ....*....|....*....|
gi 573987141 262 gySLDYLFQLAVEMKKLGIP 281
Cdd:COG0235  175 --VLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
131-279 2.88e-15

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 72.78  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 131 RPSQCTPLFLAAFTRRGAGCCIHTHSQWAVLVTLLLEQHEEanrnvFEVNNIEQIKGFGRGPGRAgnlgyhdTLRIPVIE 210
Cdd:PRK06754  75 KPSAETLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGA-----VTFQGQEIIKALGIWEENA-------EIHIPIIE 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573987141 211 NTPHEEDLTEYLEEAMEayPDTYAVLVRRHGVYVWGDNVHKAKTQCEsvcvgySLDYLFQLAVEMKKLG 279
Cdd:PRK06754 143 NHADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLE------AYEFLFSYHIKLLSIQ 203
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
94-278 1.29e-11

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 62.65  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  94 SGVQKELMKPADIYVLSLSaqdpTQPLrsylrsPPSYRPSQCTPLFLAAFTRR-GAGCCIHTHSQWAVLVTLLleqhEEA 172
Cdd:PRK09220  44 SGKDKGSLTAEDFLQVDIA----GNAV------PSGRKPSAETLLHTQLYRLFpEIGAVLHTHSVNATVLSRV----EKS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 173 NRNVFEvnNIEQIKGFgrgpgrAGNLGYHDTLRIPVIENTPHEEDLTEYLEEAMEAYPDTYAVLVRRHGVYVWGDNVHKA 252
Cdd:PRK09220 110 DALVLE--GYELQKAF------AGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPLRYGYLIRGHGLYCWGRDMAEA 181
                        170       180
                 ....*....|....*....|....*.
gi 573987141 253 KTQCEsvcvgySLDYLFQLAVEMKKL 278
Cdd:PRK09220 182 RRHLE------GLEFLFECELERRLL 201
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
88-252 2.30e-05

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 44.79  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  88 LVYLAPSGVQKELMKPADIYVLSLSAQdptqplrsylRSPPSYRPSQCTPLFLAAFTR-RGAGCCIHTHSQWAVlvtlll 166
Cdd:PRK12348  37 LVVIKPSGVAYETMKADDMVVVDMSGK----------VVEGEYRPSSDTATHLELYRRyPSLGGIVHTHSTHAT------ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 167 eQHEEANRNVFEVNNIEQIKGFGrgpgragnlgyhdtlRIPVIENTPHEEDLTEY--------LEEAMEAYP-DTYAVLV 237
Cdd:PRK12348 101 -AWAQAGLAIPALGTTHADYFFG---------------DIPCTRGLSEEEVQGEYelntgkviIETLGNAEPlHTPGIVV 164
                        170
                 ....*....|....*
gi 573987141 238 RRHGVYVWGDNVHKA 252
Cdd:PRK12348 165 YQHGPFAWGKDAHDA 179
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
93-252 4.18e-03

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 37.89  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141  93 PSGVQKELMKPADIYVLSLSAQdptqplrsylRSPPSYRPSQCTP--LFL-AAFTRRGAgcCIHTHSQWAVL-------- 161
Cdd:PRK08193  43 PSGVDYDKMTAEDMVVVDLEGN----------VVEGKLKPSSDTPthLVLyKAFPEIGG--IVHTHSRHATAwaqagrdi 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573987141 162 ----------------VTLLLEQhEEANRNvFEVNnieqikgfgrgpgrAGNlgyhdtlripVIENTPHEEDLTeyleea 225
Cdd:PRK08193 111 palgtthadyfygdipCTRKMTD-EEINGE-YEWE--------------TGK----------VIVETFEKRGID------ 158
                        170       180
                 ....*....|....*....|....*..
gi 573987141 226 meaYPDTYAVLVRRHGVYVWGDNVHKA 252
Cdd:PRK08193 159 ---PAAVPGVLVHSHGPFTWGKDAEDA 182
 
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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