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Conserved domains on  [gi|625197818|ref|XP_007640996|]
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cytidine monophosphate-N-acetylneuraminic acid hydroxylase isoform X2 [Cricetulus griseus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11454817)

MBL fold metallo-hydrolase similar to as Sus scrofa cytidine monophosphate-N-acetylneuraminic acid hydroxylase and Bacillus subtilis UPF0173 protein YddR; may be inactive as a hydrolase such as human inactive cytidine monophosphate-N-acetylneuraminic CMAHP

CATH:  3.60.15.30
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  11471246|17597585
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 31-149 1.69e-15

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


:

Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 75.34  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  31 GEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFargwwlLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLsqRRP 110
Cdd:COG2220    2 GGMKITWLGHATFLIETGGKRILIDPVFSGRAS------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL--KRT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 625197818 111 DIPIYV--GDTERpvfwnLDQSGVQltniNVVPFGVWQQVD 149
Cdd:COG2220   74 GATVVAplGVAAW-----LRAWGFP----RVTELDWGESVE 105
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 31-149 1.69e-15

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 75.34  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  31 GEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFargwwlLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLsqRRP 110
Cdd:COG2220    2 GGMKITWLGHATFLIETGGKRILIDPVFSGRAS------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL--KRT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 625197818 111 DIPIYV--GDTERpvfwnLDQSGVQltniNVVPFGVWQQVD 149
Cdd:COG2220   74 GATVVAplGVAAW-----LRAWGFP----RVTELDWGESVE 105
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-104 9.69e-07

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 48.36  E-value: 9.69e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 625197818   34 QITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWwllheppsdwlerlCKADLIYISHMHSDHLSYPTLKQ 104
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPP--------------VTADLVLISHGHDDHGHPETLPG 57
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 33-97 2.08e-06

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 48.65  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625197818  33 VQITYLTHACMDLKLGDKRMVFDPWLIG-PAFARgwwllhePPSDWlerlcKADLIYISHMHSDHL 97
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGnPLADL-------KPEDV-----KVDYILLTHGHGDHL 54
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 58-154 5.08e-06

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293841  Cd Length: 181  Bit Score: 46.89  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  58 LIGPAFARGWWLLH-------EPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDI-PIYVGDterpvfWnLDQ 129
Cdd:cd16283   17 LTDPVFSERASPVSfggpkrlTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLvPLGLKK------W-FLK 89

                         90       100
                 ....*....|....*....|....*.
gi 625197818 130 SGVQltniNVVPFGVWQQVD-KNLRF 154
Cdd:cd16283   90 KGIT----NVVELDWWQSTEiGGVRI 111
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 31-149 1.69e-15

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 75.34  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  31 GEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFargwwlLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLsqRRP 110
Cdd:COG2220    2 GGMKITWLGHATFLIETGGKRILIDPVFSGRAS------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL--KRT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 625197818 111 DIPIYV--GDTERpvfwnLDQSGVQltniNVVPFGVWQQVD 149
Cdd:COG2220   74 GATVVAplGVAAW-----LRAWGFP----RVTELDWGESVE 105
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-104 9.69e-07

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 48.36  E-value: 9.69e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 625197818   34 QITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWwllheppsdwlerlCKADLIYISHMHSDHLSYPTLKQ 104
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPP--------------VTADLVLISHGHDDHGHPETLPG 57
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 33-97 2.08e-06

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 48.65  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625197818  33 VQITYLTHACMDLKLGDKRMVFDPWLIG-PAFARgwwllhePPSDWlerlcKADLIYISHMHSDHL 97
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGnPLADL-------KPEDV-----KVDYILLTHGHGDHL 54
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 58-154 5.08e-06

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293841  Cd Length: 181  Bit Score: 46.89  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  58 LIGPAFARGWWLLH-------EPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDI-PIYVGDterpvfWnLDQ 129
Cdd:cd16283   17 LTDPVFSERASPVSfggpkrlTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLvPLGLKK------W-FLK 89

                         90       100
                 ....*....|....*....|....*.
gi 625197818 130 SGVQltniNVVPFGVWQQVD-KNLRF 154
Cdd:cd16283   90 KGIT----NVVELDWWQSTEiGGVRI 111
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-183 1.22e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 39.90  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625197818  73 PPSDWLERLCKADLIYISHMHSDHLSYptlkqLSQRRPDIPIYVGDT-------ERPVFWNLDQSGVqltNINVVPFGVW 145
Cdd:cd07732   65 LGGLRSEEDPSVDAVLLSHAHLDHYGL-----LNYLRPDIPVYMGEAtkrilkaLLPFFGEGDPVPR---NIRVFESGKS 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 625197818 146 QQVDkNLRFM-ILMDgvHPEMDTC-IIVEYKGHKILNTVD 183
Cdd:cd07732  137 FTIG-DFTVTpYLVD--HSAPGAYaFLIEAPGKRIFYTGD 173
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
45-115 6.75e-03

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.25  E-value: 6.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 625197818  45 LKLGDKRMVFDPwliGPAFARGWWLLHEPPSDwlerlckADLIYISHMHSDH-LSYPTLKQ---LSQRRPDIPIY 115
Cdd:COG1234   24 LEAGGERLLIDC---GEGTQRQLLRAGLDPRD-------IDAIFITHLHGDHiAGLPGLLStrsLAGREKPLTIY 88
 
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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