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Conserved domains on  [gi|1610115503|gb|QBY85580|]
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hypothetical protein E5D16_06125 [Listeria monocytogenes]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 191-284 3.51e-03

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd00381:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 325  Bit Score: 38.65  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610115503 191 KQDAKEVIKQLIDAGAD--VIDlpapgSRHGISVRMIqELVQFIHLYKPGTlamTFLNSSVEGADQdtirliALMMKETG 268
Cdd:cd00381    92 REDDKERAEALVEAGVDviVID-----SAHGHSVYVI-EMIKFIKKKYPNV---DVIAGNVVTAEA------ARDLIDAG 156

                          90
                  ....*....|....*.
gi 1610115503 269 ADIHAIGDGGFSGCTT 284
Cdd:cd00381   157 ADGVKVGIGPGSICTT 172
 
Name Accession Description Interval E-value
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 191-284 3.51e-03

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 38.65  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610115503 191 KQDAKEVIKQLIDAGAD--VIDlpapgSRHGISVRMIqELVQFIHLYKPGTlamTFLNSSVEGADQdtirliALMMKETG 268
Cdd:cd00381    92 REDDKERAEALVEAGVDviVID-----SAHGHSVYVI-EMIKFIKKKYPNV---DVIAGNVVTAEA------ARDLIDAG 156

                          90
                  ....*....|....*.
gi 1610115503 269 ADIHAIGDGGFSGCTT 284
Cdd:cd00381   157 ADGVKVGIGPGSICTT 172
 
Name Accession Description Interval E-value
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 191-284 3.51e-03

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 38.65  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610115503 191 KQDAKEVIKQLIDAGAD--VIDlpapgSRHGISVRMIqELVQFIHLYKPGTlamTFLNSSVEGADQdtirliALMMKETG 268
Cdd:cd00381    92 REDDKERAEALVEAGVDviVID-----SAHGHSVYVI-EMIKFIKKKYPNV---DVIAGNVVTAEA------ARDLIDAG 156

                          90
                  ....*....|....*.
gi 1610115503 269 ADIHAIGDGGFSGCTT 284
Cdd:cd00381   157 ADGVKVGIGPGSICTT 172
 
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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