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Conserved domains on  [gi|1056595005|ref|WP_068026128|]
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hypothetical protein [Rhodoplanes sp. Z2-YC6860]

Protein Classification

COG3473 family protein( domain architecture ID 10007441)

COG3473 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3473 COG3473
Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];
6-238 1.25e-54

Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442696  Cd Length: 242  Bit Score: 175.39  E-value: 1.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005   6 WRGVVGLVRPTRRPGTLEELIRILPEGIGVIPLLLNFKAGSNEEFLNSI-PLYEQYVAELAEQAVDLIILSGAPPFMLLG 84
Cdd:COG3473     8 WRARIGLIVPSSNTTVEPEFPRMLPEGVTLHFSRIPVPEIVTPEELAAMaDDLDAAARLLADARVDVIAYACTSGSFLIG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005  85 PEKEAALTRRLEDKFGIPVVTDPQLQVAGLHAMKIKKF-IGASYSALQNKIVLDYMTQAGFTALSMEPIDVPFD-QVAQI 162
Cdd:COG3473    88 PDGDRELCARITEATGVPVTTSAGALVAALRALGARRIaLVTPYTDEVNERVVAYLEAAGFEVVAVRGLGLPDNaEIARV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056595005 163 SVETLYAHVKGLyrKHPEADGVYIQGGGWQTARVVELLENDLQIPVVHATICEAWRIHKQLSVRTTTPGFGRLLAE 238
Cdd:COG3473   168 SPEELRDLAREV--DAPDADAIFISCTNLRTLDVIAELEAELGKPVLSSNQATAWHALRLAGLDDRVPGWGRLLRE 241
 
Name Accession Description Interval E-value
COG3473 COG3473
Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];
6-238 1.25e-54

Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442696  Cd Length: 242  Bit Score: 175.39  E-value: 1.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005   6 WRGVVGLVRPTRRPGTLEELIRILPEGIGVIPLLLNFKAGSNEEFLNSI-PLYEQYVAELAEQAVDLIILSGAPPFMLLG 84
Cdd:COG3473     8 WRARIGLIVPSSNTTVEPEFPRMLPEGVTLHFSRIPVPEIVTPEELAAMaDDLDAAARLLADARVDVIAYACTSGSFLIG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005  85 PEKEAALTRRLEDKFGIPVVTDPQLQVAGLHAMKIKKF-IGASYSALQNKIVLDYMTQAGFTALSMEPIDVPFD-QVAQI 162
Cdd:COG3473    88 PDGDRELCARITEATGVPVTTSAGALVAALRALGARRIaLVTPYTDEVNERVVAYLEAAGFEVVAVRGLGLPDNaEIARV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056595005 163 SVETLYAHVKGLyrKHPEADGVYIQGGGWQTARVVELLENDLQIPVVHATICEAWRIHKQLSVRTTTPGFGRLLAE 238
Cdd:COG3473   168 SPEELRDLAREV--DAPDADAIFISCTNLRTLDVIAELEAELGKPVLSSNQATAWHALRLAGLDDRVPGWGRLLRE 241
Amdase pfam17645
Arylmalonate decarboxylase; This entry contains members such as the arylmalonate ...
62-236 8.21e-17

Arylmalonate decarboxylase; This entry contains members such as the arylmalonate decarboxylases (AMDase; EC 4.1.1.76), which belong to the family of carboxy-lyases (EC 4.1). Amdases are capable of decarboxylating a range of alpha-disubstituted malonic acid derivates to enantiopure products without the need for any cofactor. AMDases are members of the widespread Asp/Glu racemase family pfam01177 together with aspartate (EC 5.1.1.13) and glutamate racemases (EC 5.1.1.3), hydantoin racemases (EC 5.1.99.5) and maleate isomerases (EC 5.2.1.1).


Pssm-ID: 375226  Cd Length: 217  Bit Score: 76.22  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005  62 AELAEQAVDLIILSGAPPFMLLGPEKEAALTRRLEDKFGIPVVTDPQLQVAGLHAMKIKKF-IGASYSALQNKIVLDYMT 140
Cdd:pfam17645  41 RRLAARGAQAVSLMGTSLSFYRGAAFNDELVARMADATGLPCTTMSHAVVEALRALGARRIaVATAYIDDVNDRLRAYLE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005 141 QAGFTALSMEPIDVP-FDQVAQISVETLYAHVKGLYRKHPEADGVYIQGGGWQTARVVELLENDLQIPVVHATICEAWRI 219
Cdd:pfam17645 121 QSGIEVAALRSLGITdVEAVAKVTAQTLIELGLRAVAAAPQADALLISCGGLRTLDAVRPLEDRLGLPVVSSAPAGFWGA 200
                         170
                  ....*....|....*..
gi 1056595005 220 HKQLSVRTTTPGFGRLL 236
Cdd:pfam17645 201 VRLAGLDPRAPGYGRLF 217
 
Name Accession Description Interval E-value
COG3473 COG3473
Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];
6-238 1.25e-54

Maleate cis-trans isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442696  Cd Length: 242  Bit Score: 175.39  E-value: 1.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005   6 WRGVVGLVRPTRRPGTLEELIRILPEGIGVIPLLLNFKAGSNEEFLNSI-PLYEQYVAELAEQAVDLIILSGAPPFMLLG 84
Cdd:COG3473     8 WRARIGLIVPSSNTTVEPEFPRMLPEGVTLHFSRIPVPEIVTPEELAAMaDDLDAAARLLADARVDVIAYACTSGSFLIG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005  85 PEKEAALTRRLEDKFGIPVVTDPQLQVAGLHAMKIKKF-IGASYSALQNKIVLDYMTQAGFTALSMEPIDVPFD-QVAQI 162
Cdd:COG3473    88 PDGDRELCARITEATGVPVTTSAGALVAALRALGARRIaLVTPYTDEVNERVVAYLEAAGFEVVAVRGLGLPDNaEIARV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056595005 163 SVETLYAHVKGLyrKHPEADGVYIQGGGWQTARVVELLENDLQIPVVHATICEAWRIHKQLSVRTTTPGFGRLLAE 238
Cdd:COG3473   168 SPEELRDLAREV--DAPDADAIFISCTNLRTLDVIAELEAELGKPVLSSNQATAWHALRLAGLDDRVPGWGRLLRE 241
Amdase pfam17645
Arylmalonate decarboxylase; This entry contains members such as the arylmalonate ...
62-236 8.21e-17

Arylmalonate decarboxylase; This entry contains members such as the arylmalonate decarboxylases (AMDase; EC 4.1.1.76), which belong to the family of carboxy-lyases (EC 4.1). Amdases are capable of decarboxylating a range of alpha-disubstituted malonic acid derivates to enantiopure products without the need for any cofactor. AMDases are members of the widespread Asp/Glu racemase family pfam01177 together with aspartate (EC 5.1.1.13) and glutamate racemases (EC 5.1.1.3), hydantoin racemases (EC 5.1.99.5) and maleate isomerases (EC 5.2.1.1).


Pssm-ID: 375226  Cd Length: 217  Bit Score: 76.22  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005  62 AELAEQAVDLIILSGAPPFMLLGPEKEAALTRRLEDKFGIPVVTDPQLQVAGLHAMKIKKF-IGASYSALQNKIVLDYMT 140
Cdd:pfam17645  41 RRLAARGAQAVSLMGTSLSFYRGAAFNDELVARMADATGLPCTTMSHAVVEALRALGARRIaVATAYIDDVNDRLRAYLE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056595005 141 QAGFTALSMEPIDVP-FDQVAQISVETLYAHVKGLYRKHPEADGVYIQGGGWQTARVVELLENDLQIPVVHATICEAWRI 219
Cdd:pfam17645 121 QSGIEVAALRSLGITdVEAVAKVTAQTLIELGLRAVAAAPQADALLISCGGLRTLDAVRPLEDRLGLPVVSSAPAGFWGA 200
                         170
                  ....*....|....*..
gi 1056595005 220 HKQLSVRTTTPGFGRLL 236
Cdd:pfam17645 201 VRLAGLDPRAPGYGRLF 217
 
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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