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Conserved domains on  [gi|512377728|dbj|BAN49193|]
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hypothetical protein PCA10_34610 [Pseudomonas resinovorans NBRC 106553]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888683)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-256 2.36e-119

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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: 293839  Cd Length: 252  Bit Score: 342.17  E-value: 2.36e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   3 RRLSVLAGRLRKLDGGSMFGSLPRQRWSDCIEPDAENQIGLASRVLLVQEPGRNVLIMAGSEPLLAPVPRTCRCQPQPLG 82
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  83 LLDSLAQRGLDEHDIDVVILTHVHALLPPDVRSAFQAGDpPRLLFPGASYVTGARQWSRALRPHPRDRAWFVPQLLDQLE 162
Cdd:cd16281   81 LLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGL-VELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 163 ESGRLKLVEDSaSGVLGEGWRFHVSDGYTPGQLLPELEMPGGPVVFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLL 242
Cdd:cd16281  160 ESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 512377728 243 DHLVATGGRLLLAR 256
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-256 2.36e-119

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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: 293839  Cd Length: 252  Bit Score: 342.17  E-value: 2.36e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   3 RRLSVLAGRLRKLDGGSMFGSLPRQRWSDCIEPDAENQIGLASRVLLVQEPGRNVLIMAGSEPLLAPVPRTCRCQPQPLG 82
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  83 LLDSLAQRGLDEHDIDVVILTHVHALLPPDVRSAFQAGDpPRLLFPGASYVTGARQWSRALRPHPRDRAWFVPQLLDQLE 162
Cdd:cd16281   81 LLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGL-VELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 163 ESGRLKLVEDSaSGVLGEGWRFHVSDGYTPGQLLPELEMPGGPVVFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLL 242
Cdd:cd16281  160 ESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 512377728 243 DHLVATGGRLLLAR 256
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-249 2.89e-09

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 55.85  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  35 PDAENQIGLASRVLLVQEPGRNVLIMAGSEPLLAPVprtcrcqpqplgLLDSLAQRGLDehdIDVVILTHVHallpPD-- 112
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA------------LLAALAALGLD---IKAVLLTHLH----PDhv 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 113 -----VRSAFqagdpprllfpGASYVTGARQWSRALRPHPRDRAWFVPQLLDQ-LEESGRLKLvedsasgvLGEGWRFHV 186
Cdd:COG0491   66 gglaaLAEAF-----------GAPVYAHAAEAEALEAPAAGALFGREPVPPDRtLEDGDTLEL--------GGPGLEVIH 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512377728 187 SDGYTPGQLLpeLEMPGGPVVFAGDLipgLHWLELDVTTAFDRNPECLIEEKERLL---DHLVATG 249
Cdd:COG0491  127 TPGHTPGHVS--FYVPDEKVLFTGDA---LFSGGVGRPDLPDGDLAQWLASLERLLalpPDLVIPG 187
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-224 6.75e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 48.90  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   47 VLLVQEPGRNVLIMAGSepllapvprtcrcqPQPLGLLDSLAQRGLDEHDIDVVILTHVHallpPDvrsafQAGDPPRLL 126
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGG--------------SAEAALLLLLAALGLGPKDIDAVILTHGH----FD-----HIGGLGELA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  127 FPGASYVTGARQWSRALRPHPRDRAWFVPQLLDQLEESGRLKLVEDSASGVLGEGWRFHVSDGYTPGQLLPELEMPGGPV 206
Cdd:pfam00753  65 EATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKV 144

                         170
                  ....*....|....*...
gi 512377728  207 VFAGDLIPGLHWLELDVT 224
Cdd:pfam00753 145 LFTGDLLFAGEIGRLDLP 162
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 49-243 1.73e-05

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 44.47  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728    49 LVQEPGRNVLIMAGSepllapvprtcrcqPQPLGLLDSLAQRGLDehDIDVVILTHVHallpPDvrsafQAGDPPRLLfp 128
Cdd:smart00849   4 LVRDDGGAILIDTGP--------------GEAEDLLAELKKLGPK--KIDAIILTHGH----PD-----HIGGLPELL-- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   129 gasYVTGARQW-SRALRPHPRDRAWFVPQLLDQLEESGRLKLVEDSAS-GVLGEGWRFHVSDGYTPGQLLpeLEMPGGPV 206
Cdd:smart00849  57 ---EAPGAPVYaPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDElDLGGGELEVIHTPGHTPGSIV--LYLPEGKI 131

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 512377728   207 VFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLLD 243
Cdd:smart00849 132 LFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKL 168
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-256 2.36e-119

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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: 293839  Cd Length: 252  Bit Score: 342.17  E-value: 2.36e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   3 RRLSVLAGRLRKLDGGSMFGSLPRQRWSDCIEPDAENQIGLASRVLLVQEPGRNVLIMAGSEPLLAPVPRTCRCQPQPLG 82
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  83 LLDSLAQRGLDEHDIDVVILTHVHALLPPDVRSAFQAGDpPRLLFPGASYVTGARQWSRALRPHPRDRAWFVPQLLDQLE 162
Cdd:cd16281   81 LLKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGL-VELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 163 ESGRLKLVEDSaSGVLGEGWRFHVSDGYTPGQLLPELEMPGGPVVFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLL 242
Cdd:cd16281  160 ESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 512377728 243 DHLVATGGRLLLAR 256
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 5-244 6.64e-20

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 86.16  E-value: 6.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   5 LSVLAGRLRKLDGGSMFGSLPRQRWSDCIEPDAENQIGLASRVLLVQEPGRNVLIMAG------SEPLLAPVPRTcrcqp 78
Cdd:cd07728    3 LTWLDGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTDPILIQYQGKNYLIDAGigngklTEKQKRNFGVT----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  79 QPLGLLDSLAQRGLDEHDIDVVILTHVHallppdvrsaF--------QAGDPPRLLFPGASYVTGARQWSRALRPHPRDR 150
Cdd:cd07728   78 EESSIEESLAELGLTPEDIDYVLMTHLH----------FdhasgltkVKGEQLVSVFPNATIYVSEIEWEEMRNPNIRSK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 151 AWFVPQLLDQLEesGRLKLVEDSASGVlgEGWRFHVSDGYTPGQLLPELEMPGGPVVFAGDLIPGL-H----WLeldvtT 225
Cdd:cd07728  148 NTYWKENWEPIE--DQVKTFSDEIEIV--PGITMIHTGGHSDGHSIIEIEQGGETAIHMADLMPTHaHqnplWV-----L 218

                        250
                 ....*....|....*....
gi 512377728 226 AFDRNPECLIEEKERLLDH 244
Cdd:cd07728  219 AYDDYPMTSIEAKEKWLKE 237
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-255 1.11e-18

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 82.57  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  48 LLVQEPGRNVLIMAGSEPLLAPvPRTCRCQPQPLGLLDSLAQRGLDEHDIDVVILTHVHA--------LLPPDVRsafqa 119
Cdd:cd16277   16 WLVRTPGRTILVDTGIGNDKPR-PGPPAFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVdhvgwntrLVDGRWV----- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 120 gdpPRllFPGASYVTGARQWSRALRPHPRDRAWFVPqLLDQLE---ESGRLKLVEDsaSGVLGEGWRFHVSDGYTPGQLL 196
Cdd:cd16277   90 ---PT--FPNARYLFSRAEYDHWSSPDAGGPPNRGV-FEDSVLpviEAGLADLVDD--DHEILDGIRLEPTPGHTPGHVS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512377728 197 PELEMPGGPVVFAGDLI--PgLHWLELDVTTAFDRNPECLIEEKERLLDHLVATGGRLLLA 255
Cdd:cd16277  162 VELESGGERALFTGDVMhhP-IQVARPDWSSVFDEDPAQAAATRRRLLERAADTDTLLFPA 221
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 47-255 9.81e-13

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 66.42  E-value: 9.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  47 VLLVQEPGRNVLIMAGSEPLLAPVprtcrcqpqpLG-LLDSLAQRGLDEHDIDVVILTHVHA-----LLPPDVRSAfqag 120
Cdd:cd07720   51 AFLVRTGGRLILVDTGAGGLFGPT----------AGkLLANLAAAGIDPEDIDDVLLTHLHPdhiggLVDAGGKPV---- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 121 dpprllFPGASYVTGARQWSRALRPHPRDRA-WFVPQLLDQLEesGRLKLVEDSASGVLGE----GWRFHVSDGYTPGQL 195
Cdd:cd07720  117 ------FPNAEVHVSEAEWDFWLDDANAAKApEGAKRFFDAAR--DRLRPYAAAGRFEDGDevlpGITAVPAPGHTPGHT 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512377728 196 LPELEMPGGPVVFAGDLI--PGLHWLELDVTTAFDRNPECLIEEKERLLDHLVAtgGRLLLA 255
Cdd:cd07720  189 GYRIESGGERLLIWGDIVhhPALQFAHPDWTIAFDVDPEQAAATRRRLLDRAAA--EGLLVA 248
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 49-258 1.14e-10

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 60.31  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  49 LVQEPGRNVLIMAGSEPLLA-----PVPRTCRCQPQPLGLLDSLAQRGLDEHDIDVVILTHVHallpPD----VRsafqa 119
Cdd:cd07729   36 LIEHPEGTILVDTGFHPDAAddpggLELAFPPGVTEEQTLEEQLARLGLDPEDIDYVILSHLH----FDhaggLD----- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 120 gdpprlLFPGASYVTGARQWSRALRPHPRDRA-WFVPQLLDQLEESGRLKLVEDSASgvLGEGWRFHVSDGYTPGQLLPE 198
Cdd:cd07729  107 ------LFPNATIIVQRAELEYATGPDPLAAGyYEDVLALDDDLPGGRVRLVDGDYD--LFPGVTLIPTPGHTPGHQSVL 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 199 LEMPGGPVVFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLLDHLVATGGRLLLARDP 258
Cdd:cd07729  179 VRLPEGTVLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEREGARVIPGHDP 238
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-249 2.89e-09

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 55.85  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  35 PDAENQIGLASRVLLVQEPGRNVLIMAGSEPLLAPVprtcrcqpqplgLLDSLAQRGLDehdIDVVILTHVHallpPD-- 112
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA------------LLAALAALGLD---IKAVLLTHLH----PDhv 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 113 -----VRSAFqagdpprllfpGASYVTGARQWSRALRPHPRDRAWFVPQLLDQ-LEESGRLKLvedsasgvLGEGWRFHV 186
Cdd:COG0491   66 gglaaLAEAF-----------GAPVYAHAAEAEALEAPAAGALFGREPVPPDRtLEDGDTLEL--------GGPGLEVIH 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512377728 187 SDGYTPGQLLpeLEMPGGPVVFAGDLipgLHWLELDVTTAFDRNPECLIEEKERLL---DHLVATG 249
Cdd:COG0491  127 TPGHTPGHVS--FYVPDEKVLFTGDA---LFSGGVGRPDLPDGDLAQWLASLERLLalpPDLVIPG 187
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-224 6.75e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 48.90  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   47 VLLVQEPGRNVLIMAGSepllapvprtcrcqPQPLGLLDSLAQRGLDEHDIDVVILTHVHallpPDvrsafQAGDPPRLL 126
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGG--------------SAEAALLLLLAALGLGPKDIDAVILTHGH----FD-----HIGGLGELA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  127 FPGASYVTGARQWSRALRPHPRDRAWFVPQLLDQLEESGRLKLVEDSASGVLGEGWRFHVSDGYTPGQLLPELEMPGGPV 206
Cdd:pfam00753  65 EATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKV 144

                         170
                  ....*....|....*...
gi 512377728  207 VFAGDLIPGLHWLELDVT 224
Cdd:pfam00753 145 LFTGDLLFAGEIGRLDLP 162
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-211 8.90e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 48.80  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  83 LLDSLAQRGLDEHDIDVVILTHVHAllppDvrsafQAGDPPRllFPGASYVTGARQWSRALRphPRDRAWFVPQLLD-QL 161
Cdd:cd07730   70 VAEQLAAGGIDPEDIDAVILSHLHW----D-----HIGGLSD--FPNARLIVGPGAKEALRP--PGYPSGFLPELLPsDF 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512377728 162 EESGRLKLVEDSASGVLGEGWRFH----------V-SDGYTPGQ---LLPELemPGGPVVFAGD 211
Cdd:cd07730  137 EGRLVRWEEDDFLWVPLGPFPRALdlfgdgslylVdLPGHAPGHlglLARTT--SGTWVFLAGD 198
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-243 1.04e-06

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. 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.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 47.97  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728  34 EPDAENQIGLASRVLLVQEPGRNVLIMAGSepllaPVPRTcrcqpqplGLLDSLAQRGLDEHDIDVVILTHVHallpPDv 113
Cdd:cd07711   11 RRDSDGGFRASSTVTLIKDGGKNILVDTGT-----PWDRD--------LLLKALAEHGLSPEDIDYVVLTHGH----PD- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728 114 rSAFQAGdpprlLFPGASYVTGARQWSRALRPHPrdrawfvpqlldqleesgrlklvedsasgvLGEGWRFHVSDG---- 189
Cdd:cd07711   73 -HIGNLN-----LFPNATVIVGWDICGDSYDDHS------------------------------LEEGDGYEIDENvevi 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512377728 190 YTPGQ------LLPELEmPGGPVVFAGDLIPGLHWLELDVTT-AFDRNPECLIEEKERLLD 243
Cdd:cd07711  117 PTPGHtpedvsVLVETE-KKGTVAVAGDLFEREEDLEDPILWdPLSEDPELQEESRKRILA 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 49-243 1.73e-05

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 44.47  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728    49 LVQEPGRNVLIMAGSepllapvprtcrcqPQPLGLLDSLAQRGLDehDIDVVILTHVHallpPDvrsafQAGDPPRLLfp 128
Cdd:smart00849   4 LVRDDGGAILIDTGP--------------GEAEDLLAELKKLGPK--KIDAIILTHGH----PD-----HIGGLPELL-- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512377728   129 gasYVTGARQW-SRALRPHPRDRAWFVPQLLDQLEESGRLKLVEDSAS-GVLGEGWRFHVSDGYTPGQLLpeLEMPGGPV 206
Cdd:smart00849  57 ---EAPGAPVYaPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDElDLGGGELEVIHTPGHTPGSIV--LYLPEGKI 131

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 512377728   207 VFAGDLIPGLHWLELDVTTAFDRNPECLIEEKERLLD 243
Cdd:smart00849 132 LFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKL 168
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 49-106 7.97e-03

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 36.70  E-value: 7.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 512377728  49 LVQEPGRNVLIMAGSEPllaPVPRtcrcqpqplgLLDSLAQRGLDEHDIDVVILTHVH 106
Cdd:cd07726   20 LLDGEGRPALIDTGPSS---SVPR----------LLAALEALGIAPEDVDYIILTHIH 64
 
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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