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Conserved domains on  [gi|492175241|ref|WP_005770491|]
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MBL fold metallo-hydrolase [Coxiella burnetii]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-231 8.20e-19

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 82.17  E-value: 8.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGeiepSAPY-HSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPDHAFFV------- 61
Cdd:COG1234    1 MKLTFLGTGG----AVPTpGRATSSYLLeagGERLLIDCGEgtqRQLLRAgldprDIDAIFITHLHGDHIAGLpgllstr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  62 ----REPkkdytiDAPLFAPESFKGnlWVKAL-------------------TQPKSFGSYEITPIPTHHShkVNSQAYLI 118
Cdd:COG1234   77 slagREK------PLTIYGPPGTKE--FLEALlkasgtdldfplefheiepGEVFEIGGFTVTAFPLDHP--VPAYGYRF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 119 KKGKEKMLYTGDMIWiNKEYHHLLENLDLVITEGSFIQkggrirRHEESKKIYGHT---GIPNLLNFFKPytRHLIFVHF 195
Cdd:COG1234  147 EEPGRSLVYSGDTRP-CEALVELAKGADLLIHEATFLD------EEAELAKETGHStakEAAELAAEAGV--KRLVLTHF 217

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492175241 196 GSWFyqnmpSARKKLITLGKEH-GINVYVGHDGMTLD 231
Cdd:COG1234  218 SPRY-----DDPEELLAEARAVfPGPVELAEDGMVIE 249
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-231 8.20e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 82.17  E-value: 8.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGeiepSAPY-HSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPDHAFFV------- 61
Cdd:COG1234    1 MKLTFLGTGG----AVPTpGRATSSYLLeagGERLLIDCGEgtqRQLLRAgldprDIDAIFITHLHGDHIAGLpgllstr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  62 ----REPkkdytiDAPLFAPESFKGnlWVKAL-------------------TQPKSFGSYEITPIPTHHShkVNSQAYLI 118
Cdd:COG1234   77 slagREK------PLTIYGPPGTKE--FLEALlkasgtdldfplefheiepGEVFEIGGFTVTAFPLDHP--VPAYGYRF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 119 KKGKEKMLYTGDMIWiNKEYHHLLENLDLVITEGSFIQkggrirRHEESKKIYGHT---GIPNLLNFFKPytRHLIFVHF 195
Cdd:COG1234  147 EEPGRSLVYSGDTRP-CEALVELAKGADLLIHEATFLD------EEAELAKETGHStakEAAELAAEAGV--KRLVLTHF 217

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492175241 196 GSWFyqnmpSARKKLITLGKEH-GINVYVGHDGMTLD 231
Cdd:COG1234  218 SPRY-----DDPEELLAEARAVfPGPVELAEDGMVIE 249
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-231 1.06e-08

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 53.99  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   3 IKILGTRGEIePSApyHSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPDHAF----FV-----R 62
Cdd:cd07717    1 LTFLGTGSAV-PTP--ERNLSSIALrleGELWLFDCGEgtqRQLLRAglspsKIDRIFITHLHGDHILglpgLLstmslL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  63 EPKKDYTIdaplFAPESFKgnLWVKALTQPKSF---------------------GSYEITPIPTHHShkVNSQAYLIKKG 121
Cdd:cd07717   78 GRTEPLTI----YGPKGLK--EFLETLLRLSASrlpypievhelepdpglvfedDGFTVTAFPLDHR--VPCFGYRFEEG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 122 KeKMLYTGDMIWInKEYHHLLENLDLVITEGSFIQKggrirrHEESKKIYGHTgipnllnffkpyT-------------R 188
Cdd:cd07717  150 R-KIAYLGDTRPC-EGLVELAKGADLLIHEATFLDD------DAEKAKETGHS------------TakqaaeiakkagvK 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 492175241 189 HLIFVHFgswfyqnmpSAR----KKLITLGKEHGINVYVGHDGMTLD 231
Cdd:cd07717  210 KLVLTHF---------SARykdpEELLKEARAVFPNTILAEDFMTIE 247
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-195 5.72e-05

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 42.68  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   33 FDLGEEAFLTYQPK--------YILITHLHPDH---AFFVRE--------PKKDYTIDAPLFAPESFKGNLWVK----AL 89
Cdd:pfam12706   9 PDLRQQALPALQPGrlrddpidAVLLTHDHYDHlagLLDLREgrprplyaPLGVLAHLRRNFPYLFLLEHYGVRvheiDW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   90 TQPKSFGS--YEITPIPTHHSHKVNSQA-------YLIKKGKEKMLYTGDMIWINKEYHHLLENLDLVITEGSFiqkggr 160
Cdd:pfam12706  89 GESFTVGDggLTVTATPARHGSPRGLDPnpgdtlgFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGGA------ 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492175241  161 irRHEESKKIYGHTGIPNLLNFFKPY-TRHLIFVHF 195
Cdd:pfam12706 163 --WRDDEMIHMGHMTPEEAVEAAADLgARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 44-135 1.01e-03

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: 38.69  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241    44 QPKYILITHLHPDHAFFVREPKKDYtiDAPLFAPESFKGNLWVKALTQPKS--------------------FGSYEITPI 103
Cdd:smart00849  35 KIDAIILTHGHPDHIGGLPELLEAP--GAPVYAPEGTAELLKDLLALLGELgaeaepappdrtlkdgdeldLGGGELEVI 112

                           90       100       110
                   ....*....|....*....|....*....|..
gi 492175241   104 PTHHsHKVNSQAYLIKKGkeKMLYTGDMIWIN 135
Cdd:smart00849 113 HTPG-HTPGSIVLYLPEG--KILFTGDLLFAG 141
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-59 1.84e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 1.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGEIePSApyHSHHSGVLV---DDIFLFDLGEE-----AFLTYQPK---YILITHLHPDHAF 59
Cdd:PRK00055   2 MELTFLGTGSGV-PTP--TRNVSSILLrlgGELFLFDCGEGtqrqlLKTGIKPRkidKIFITHLHGDHIF 68
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-231 8.20e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 82.17  E-value: 8.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGeiepSAPY-HSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPDHAFFV------- 61
Cdd:COG1234    1 MKLTFLGTGG----AVPTpGRATSSYLLeagGERLLIDCGEgtqRQLLRAgldprDIDAIFITHLHGDHIAGLpgllstr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  62 ----REPkkdytiDAPLFAPESFKGnlWVKAL-------------------TQPKSFGSYEITPIPTHHShkVNSQAYLI 118
Cdd:COG1234   77 slagREK------PLTIYGPPGTKE--FLEALlkasgtdldfplefheiepGEVFEIGGFTVTAFPLDHP--VPAYGYRF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 119 KKGKEKMLYTGDMIWiNKEYHHLLENLDLVITEGSFIQkggrirRHEESKKIYGHT---GIPNLLNFFKPytRHLIFVHF 195
Cdd:COG1234  147 EEPGRSLVYSGDTRP-CEALVELAKGADLLIHEATFLD------EEAELAKETGHStakEAAELAAEAGV--KRLVLTHF 217

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492175241 196 GSWFyqnmpSARKKLITLGKEH-GINVYVGHDGMTLD 231
Cdd:COG1234  218 SPRY-----DDPEELLAEARAVfPGPVELAEDGMVIE 249
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-231 8.27e-13

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 65.69  E-value: 8.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGEIEPSAP-------------YHSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPD 56
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIgcdcpvcastdprYGRTRSSILVeadGTRLLIDAGPdlrEQLLRLgldpsKIDAILLTHEHAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  57 H---AFFVREPKKDYTIdaPLFAPES---------------FKGNLWVKALT--QPKSFGSYEITPIPTHHShKVNSQAY 116
Cdd:COG1235   81 HiagLDDLRPRYGPNPI--PVYATPGtlealerrfpylfapYPGKLEFHEIEpgEPFEIGGLTVTPFPVPHD-AGDPVGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 117 LIKKGKEKMLYTGDMIWINKEYHHLLENLDLVITEGSfiqkggriRRHEEskkiYGHTGIPNLLNFFKPY-TRHLIFVHF 195
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDAT--------YDDPE----PGHLSNEEALELLARLgPKRLVLTHL 225

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492175241 196 GSwfYQNMPS-ARKKLITLGKEHGinVYVGHDGMTLD 231
Cdd:COG1235  226 SP--DNNDHElDYDELEAALLPAG--VEVAYDGMEIE 258
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-231 1.06e-08

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 53.99  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   3 IKILGTRGEIePSApyHSHHSGVLV---DDIFLFDLGE---EAFLTY-----QPKYILITHLHPDHAF----FV-----R 62
Cdd:cd07717    1 LTFLGTGSAV-PTP--ERNLSSIALrleGELWLFDCGEgtqRQLLRAglspsKIDRIFITHLHGDHILglpgLLstmslL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  63 EPKKDYTIdaplFAPESFKgnLWVKALTQPKSF---------------------GSYEITPIPTHHShkVNSQAYLIKKG 121
Cdd:cd07717   78 GRTEPLTI----YGPKGLK--EFLETLLRLSASrlpypievhelepdpglvfedDGFTVTAFPLDHR--VPCFGYRFEEG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241 122 KeKMLYTGDMIWInKEYHHLLENLDLVITEGSFIQKggrirrHEESKKIYGHTgipnllnffkpyT-------------R 188
Cdd:cd07717  150 R-KIAYLGDTRPC-EGLVELAKGADLLIHEATFLDD------DAEKAKETGHS------------TakqaaeiakkagvK 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 492175241 189 HLIFVHFgswfyqnmpSAR----KKLITLGKEHGINVYVGHDGMTLD 231
Cdd:cd07717  210 KLVLTHF---------SARykdpEELLKEARAVFPNTILAEDFMTIE 247
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-154 3.75e-07

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 49.52  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGEIEPS-------APYHSHHSgVLVD--------------DIFLFDLGEEAFLTYQP-KYILITHLHPDH- 57
Cdd:cd07735    1 FELVVLGCSGGPDEGntssfllDPAGSDGD-ILLDagtgvgalsleemfNDILFPSQKAAYELYQRiRHYLITHAHLDHi 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  58 ---------AFFVREPKKD-----YTIDA-----------PLFAPESFKGNLWVK----ALTQPKSFGSYEITPIPTHHS 108
Cdd:cd07735   80 aglpllspnDGGQRGSPKTiyglpETIDAlkkhifnwviwPDFTSIPSGKYPYLRlepiEPEYPIALTGLSVTAFPVSHG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492175241 109 hKVNSQAYLIKKGKEKMLYTGDM-------------IW--INKeyhHLLENLDLVITEGSF 154
Cdd:cd07735  160 -VPVSTAFLIRDGGDSFLFFGDTgpdsvsksprldaLWraLAP---LIPKKLKAIIIECSF 216
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-151 1.07e-06

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 47.26  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   3 IKILGTRGEIePSAPYHShhSGVLV---DDIFLFDLGEEAF--------LTYQPKYILITHLHPDH---------AFFVR 62
Cdd:cd16272    1 LTFLGTGGAV-PSLTRNT--SSYLLetgGTRILLDCGEGTVyrllkagvDPDKLDAIFLSHFHLDHigglptllfARRYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  63 EPKKDYTIdaplFAPESFKGNL--------WVKALTQPKSF------------GSYEITPIPTHHShkVNSQAYLIKKGK 122
Cdd:cd16272   78 GRKKPLTI----YGPKGIKEFLekllnfpvEILPLGFPLEIeeleeggevlelGDLKVEAFPVKHS--VESLGYRIEAEG 151

                        170       180
                 ....*....|....*....|....*....
gi 492175241 123 EKMLYTGDMIwINKEYHHLLENLDLVITE 151
Cdd:cd16272  152 KSIVYSGDTG-PCENLVELAKGADLLIHE 179
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 44-134 2.29e-05

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: 43.91  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  44 QPKYILITHLHPDHAFFVREPKKDYtiDAPLFAPE--------SFKGNLWVKALTQPK---------SFGSYEITPIPTH 106
Cdd:COG0491   51 DIKAVLLTHLHPDHVGGLAALAEAF--GAPVYAHAaeaealeaPAAGALFGREPVPPDrtledgdtlELGGPGLEVIHTP 128

                         90       100
                 ....*....|....*....|....*....
gi 492175241 107 -HSHkvNSQAYLIKkgKEKMLYTGDMIWI 134
Cdd:COG0491  129 gHTP--GHVSFYVP--DEKVLFTGDALFS 153
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-195 5.72e-05

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 42.68  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   33 FDLGEEAFLTYQPK--------YILITHLHPDH---AFFVRE--------PKKDYTIDAPLFAPESFKGNLWVK----AL 89
Cdd:pfam12706   9 PDLRQQALPALQPGrlrddpidAVLLTHDHYDHlagLLDLREgrprplyaPLGVLAHLRRNFPYLFLLEHYGVRvheiDW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   90 TQPKSFGS--YEITPIPTHHSHKVNSQA-------YLIKKGKEKMLYTGDMIWINKEYHHLLENLDLVITEGSFiqkggr 160
Cdd:pfam12706  89 GESFTVGDggLTVTATPARHGSPRGLDPnpgdtlgFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGGA------ 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492175241  161 irRHEESKKIYGHTGIPNLLNFFKPY-TRHLIFVHF 195
Cdd:pfam12706 163 --WRDDEMIHMGHMTPEEAVEAAADLgARRKVLIHI 196
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 43-132 1.17e-04

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: 42.15  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  43 YQPK---YILITHLHPDH-----------AF-----FVREPKKDYTIDAPLF--APESFKGNLW-----VKALTQPKSFG 96
Cdd:cd07720   87 IDPEdidDVLLTHLHPDHigglvdaggkpVFpnaevHVSEAEWDFWLDDANAakAPEGAKRFFDaardrLRPYAAAGRFE 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 492175241  97 SYE-----ITPIPTH-----HShkvnsqAYLIKKGKEKMLYTGDMI 132
Cdd:cd07720  167 DGDevlpgITAVPAPghtpgHT------GYRIESGGERLLIWGDIV 206
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 28-149 4.99e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 39.91  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  28 DDIFLFDLG----EEAFLTYQPKYILITHLHPDHA---FFVREPKKDyTIdaPLFAPES-------FK--GNLWVKALT- 90
Cdd:cd07736   46 GERILLDAGltdlAERFPPGSIDAILLTHFHMDHVqglFHLRWGVGD-PI--PVYGPPDpqgcadlFKhpGILDFQPLVa 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492175241  91 --QPKSFGSYEITPIPTHHSHkvNSQAYLIKKGKEKMLYTGDMIWINKEYHHLL--ENLDLVI 149
Cdd:cd07736  123 pfQSFELGGLKITPLPLNHSK--PTFGYLLESGGKRLAYLTDTLGLPEETLEFLkqQQPDVLV 183
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 18-132 7.08e-04

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase 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 which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, 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 which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 39.19  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  18 YHSHHSGVLVD-----DIFLFDLGEEAFLtyQPKYILITHLHPDHAFFVREPKKDYTI-------DAPLF-APESFKGNL 84
Cdd:cd06262   16 SDEEGEAILIDpgagaLEKILEAIEELGL--KIKAILLTHGHFDHIGGLAELKEAPGApvyiheaDAELLeDPELNLAFF 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  85 WVKALTQPK-----------SFGSYEITPIPT-HHSHkvNSQAYLIKkgKEKMLYTGDMI 132
Cdd:cd06262   94 GGGPLPPPEpdilledgdtiELGGLELEVIHTpGHTP--GSVCFYIE--EEGVLFTGDTL 149
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 44-135 1.01e-03

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: 38.69  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241    44 QPKYILITHLHPDHAFFVREPKKDYtiDAPLFAPESFKGNLWVKALTQPKS--------------------FGSYEITPI 103
Cdd:smart00849  35 KIDAIILTHGHPDHIGGLPELLEAP--GAPVYAPEGTAELLKDLLALLGELgaeaepappdrtlkdgdeldLGGGELEVI 112

                           90       100       110
                   ....*....|....*....|....*....|..
gi 492175241   104 PTHHsHKVNSQAYLIKKGkeKMLYTGDMIWIN 135
Cdd:smart00849 113 HTPG-HTPGSIVLYLPEG--KILFTGDLLFAG 141
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-130 1.12e-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: 38.75  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  48 ILITHLHPDHA------------FFVREPKKDYTIDAPLFAPE-SFKGNLWVKALTQPKSFGSYEITPIPTHHShKVNSQ 114
Cdd:cd07732   79 VLLSHAHLDHYgllnylrpdipvYMGEATKRILKALLPFFGEGdPVPRNIRVFESGKSFTIGDFTVTPYLVDHS-APGAY 157

                         90
                 ....*....|....*.
gi 492175241 115 AYLIKKGKEKMLYTGD 130
Cdd:cd07732  158 AFLIEAPGKRIFYTGD 173
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
25-139 1.18e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.89  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   25 VLVD------DIFLFDLGEEAFLTYQPKYILITHLHPDHAF-------------FVREPKKDYTIDAPLFAPESFKGNLW 85
Cdd:pfam00753  18 VLIDtggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGglgelaeatdvpvIVVAEEARELLDEELGLAASRLGLPG 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492175241   86 VKALTQPK------------SFGSYEITPIPTHHSHKVnsqayLIKKGKEKMLYTGDMIWINKEYH 139
Cdd:pfam00753  98 PPVVPLPPdvvleegdgilgGGLGLLVTHGPGHGPGHV-----VVYYGGGKVLFTGDLLFAGEIGR 158
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 28-157 1.34e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 38.63  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  28 DDIFLFDLG------------EEAFLTYqpkYILITHLHPDH----AFFV--REPKKDYTIDAPLFAPESFKGNLwvKAL 89
Cdd:cd07715   32 GELLILDAGtgirelgnelmkEGPPGEA---HLLLSHTHWDHiqgfPFFApaYDPGNRIHIYGPHKDGGSLEEVL--RRQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  90 TQPKSF------------------------GSYEITPIPTHHSHkvNSQAYLIKKGKEKMLYTGD------MIWINKEYH 139
Cdd:cd07715  107 MSPPYFpvpleellaaiefhdlepgepfsiGGVTVTTIPLNHPG--GALGYRIEEDGKSVVYATDtehypdDGESDEALL 184

                        170       180
                 ....*....|....*....|...
gi 492175241 140 HLLENLDLVI-----TEGSFIQK 157
Cdd:cd07715  185 EFARGADLLIhdaqyTDEEYPSK 207
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-59 1.84e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 1.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241   1 MKIKILGTRGEIePSApyHSHHSGVLV---DDIFLFDLGEE-----AFLTYQPK---YILITHLHPDHAF 59
Cdd:PRK00055   2 MELTFLGTGSGV-PTP--TRNVSSILLrlgGELFLFDCGEGtqrqlLKTGIKPRkidKIFITHLHGDHIF 68
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 48-149 2.05e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 37.84  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  48 ILITHLHPDHAF-------FVREPKK-------DYTIDA-----PLFAPESFKGN-----LWVKALTQPKSFGSYEITPI 103
Cdd:cd16279   70 VLLTHAHADHIHglddlrpFNRLQQRpipvyasEETLDDlkrrfPYFFAATGGGGvpkldLHIIEPDEPFTIGGLEITPL 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 492175241 104 PTHHsHKVNSQAYLIkkgkEKMLYTGDMIWINKEYHHLLENLDLVI 149
Cdd:cd16279  150 PVLH-GKLPSLGFRF----GDFAYLTDVSEIPEESLEKLRGLDVLI 190
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 46-146 6.03e-03

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: 36.81  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492175241  46 KYILITHLHPDHA----------FFVREPKKDYTIDAPLFAPESFKGNLWVKALTQPKSF----GSYEITP----IPTH- 106
Cdd:cd07729   90 DYVILSHLHFDHAggldlfpnatIIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGRVrlvdGDYDLFPgvtlIPTPg 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492175241 107 HSHkvNSQAYLIKKGKEKMLYTGDMIwinkeyhHLLENLD 146
Cdd:cd07729  170 HTP--GHQSVLVRLPEGTVLLAGDAA-------YTYENLE 200
 
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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