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Conserved domains on  [gi|446193733|ref|WP_000271588|]
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MULTISPECIES: MBL fold metallo-hydrolase [Leptospira]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

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];
30-262 5.80e-23

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 94.49  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  30 SLMFDIG--AQ--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEPMQKILDLYseI 98
Cdd:COG1234   30 RLLIDCGegTQrqllraglDPRDI--DAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKAS--G 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  99 ENFTYAYELNAVSPGDKIDLDSNHfFSPHQTFHRVPSQGYTLYQKRKKlkkefqsisqnelnqalkekievselseipvI 178
Cdd:COG1234  106 TDLDFPLEFHEIEPGEVFEIGGFT-VTAFPLDHPVPAYGYRFEEPGRS-------------------------------L 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 179 SFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHTHLDEILNNLSSFKNEKIVLIHFSKRYS-----VS 252
Cdd:COG1234  154 VYSGDTRpCEALVEL--AKGADLLIHEATFLDEEA--ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdpeelLA 229

                        250
                 ....*....|
gi 446193733 253 YIREVLDKRI 262
Cdd:COG1234  230 EARAVFPGPV 239
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
30-262 5.80e-23

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 94.49  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  30 SLMFDIG--AQ--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEPMQKILDLYseI 98
Cdd:COG1234   30 RLLIDCGegTQrqllraglDPRDI--DAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKAS--G 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  99 ENFTYAYELNAVSPGDKIDLDSNHfFSPHQTFHRVPSQGYTLYQKRKKlkkefqsisqnelnqalkekievselseipvI 178
Cdd:COG1234  106 TDLDFPLEFHEIEPGEVFEIGGFT-VTAFPLDHPVPAYGYRFEEPGRS-------------------------------L 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 179 SFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHTHLDEILNNLSSFKNEKIVLIHFSKRYS-----VS 252
Cdd:COG1234  154 VYSGDTRpCEALVEL--AKGADLLIHEATFLDEEA--ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdpeelLA 229

                        250
                 ....*....|
gi 446193733 253 YIREVLDKRI 262
Cdd:COG1234  230 EARAVFPGPV 239
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-147 1.51e-16

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: 75.38  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  14 GISEGGIRTSLYL---PSLSLMFDIGAQNPNRI--------HLDNLLLTHSHLDHSCGLPYYISQRSL-RKLKSPKIFVP 81
Cdd:cd16272    9 AVPSLTRNTSSYLletGGTRILLDCGEGTVYRLlkagvdpdKLDAIFLSHFHLDHIGGLPTLLFARRYgGRKKPLTIYGP 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446193733  82 APLKEPMQKILDLYSEIENFTYAYELNAVSPGDKIDLDSNHFFSPHQTFHRVPSQGYTLYQKRKKL 147
Cdd:cd16272   89 KGIKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSI 154
PRK00055 PRK00055
ribonuclease Z; Reviewed
 31-253 6.48e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 49.41  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  31 LMFDIGA--Q--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEpmqkildlysEIE 99
Cdd:PRK00055  32 FLFDCGEgtQrqllktgiKPRKI--DKIFITHLHGDHIFGLPGLLSTRSLSGRTEPlTIYGPKGIKE----------FVE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 100 NFTYAYELNavspgdkidldsnhffsphqtfhrvpsqGYTLYQKRK--KL---KKEFQSISQNELNQALKEKIEV----- 169
Cdd:PRK00055 100 TLLRASGSL----------------------------GYRIAEKDKpgKLdaeKLKALGVPPGPLFGKLKRGEDVtledg 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 170 -----SELSEIP----VISFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHthldeilnnlSSFKN-- 237
Cdd:PRK00055 152 riinpADVLGPPrkgrKVAYCGDTRpCEALVEL--AKGADLLVHEATFGDEDE--ELAKEYGH----------STARQaa 217

                        250       260
                 ....*....|....*....|....
gi 446193733 238 --------EKIVLIHFSKRYSVSY 253
Cdd:PRK00055 218 eiakeagvKRLILTHFSPRYTGDP 241
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-123 3.77e-06

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: 46.39  E-value: 3.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733    31 LMFDIGAQNPNRIhlDNLLLTHSHLDHSCGLPYyisqrsLRKLKSPKIFVPAPLKEPMQKILDLYSEIENFTYAYELN-A 109
Cdd:smart00849  24 LLAELKKLGPKKI--DAIILTHGHPDHIGGLPE------LLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDrT 95

                           90
                   ....*....|....
gi 446193733   110 VSPGDKIDLDSNHF 123
Cdd:smart00849  96 LKDGDELDLGGGEL 109
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-245 2.22e-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: 44.22  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733   33 FDIGAQNPNRIH--------LDNLLLTHSHLDHSCGLPyyisqrSLRKLKSPKIFVPAPLKEPMQKILDLYSEIENftYA 104
Cdd:pfam12706   9 PDLRQQALPALQpgrlrddpIDAVLLTHDHYDHLAGLL------DLREGRPRPLYAPLGVLAHLRRNFPYLFLLEH--YG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  105 YELNAVSPGDKIDLDS----------NHFFSPHQTFHRVPSQGYTLYQKRKKlkkefqsisqnelnqalkekievselse 174
Cdd:pfam12706  81 VRVHEIDWGESFTVGDggltvtatpaRHGSPRGLDPNPGDTLGFRIEGPGKR---------------------------- 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446193733  175 ipvISFSGDTKieYVLEH--EDVANSSILFIECTYIDNERNVaqarEWGHTHLDEILNNLSSFKNEKIVLIHF 245
Cdd:pfam12706 133 ---VYYAGDTG--YFPDEigERLGGADLLLLDGGAWRDDEMI----HMGHMTPEEAVEAAADLGARRKVLIHI 196
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
30-262 5.80e-23

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 94.49  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  30 SLMFDIG--AQ--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEPMQKILDLYseI 98
Cdd:COG1234   30 RLLIDCGegTQrqllraglDPRDI--DAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKAS--G 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  99 ENFTYAYELNAVSPGDKIDLDSNHfFSPHQTFHRVPSQGYTLYQKRKKlkkefqsisqnelnqalkekievselseipvI 178
Cdd:COG1234  106 TDLDFPLEFHEIEPGEVFEIGGFT-VTAFPLDHPVPAYGYRFEEPGRS-------------------------------L 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 179 SFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHTHLDEILNNLSSFKNEKIVLIHFSKRYS-----VS 252
Cdd:COG1234  154 VYSGDTRpCEALVEL--AKGADLLIHEATFLDEEA--ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdpeelLA 229

                        250
                 ....*....|
gi 446193733 253 YIREVLDKRI 262
Cdd:COG1234  230 EARAVFPGPV 239
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-147 1.51e-16

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: 75.38  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  14 GISEGGIRTSLYL---PSLSLMFDIGAQNPNRI--------HLDNLLLTHSHLDHSCGLPYYISQRSL-RKLKSPKIFVP 81
Cdd:cd16272    9 AVPSLTRNTSSYLletGGTRILLDCGEGTVYRLlkagvdpdKLDAIFLSHFHLDHIGGLPTLLFARRYgGRKKPLTIYGP 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446193733  82 APLKEPMQKILDLYSEIENFTYAYELNAVSPGDKIDLDSNHFFSPHQTFHRVPSQGYTLYQKRKKL 147
Cdd:cd16272   89 KGIKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSI 154
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 31-250 3.48e-16

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: 75.95  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  31 LMFDIG--AQ--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEPMQKILDLYSeiE 99
Cdd:cd07717   29 WLFDCGegTQrqllraglSPSKI--DRIFITHLHGDHILGLPGLLSTMSLLGRTEPlTIYGPKGLKEFLETLLRLSA--S 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 100 NFTYAYELNAVSPGDKIDLDSNHFF-SPHQTFHRVPSQGYTLYQKRKklkkefqsisqnelnqalkekievselseipvI 178
Cdd:cd07717  105 RLPYPIEVHELEPDPGLVFEDDGFTvTAFPLDHRVPCFGYRFEEGRK--------------------------------I 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 179 SFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHthldeilnnlSSFKN----------EKIVLIHFSK 247
Cdd:cd07717  153 AYLGDTRpCEGLVEL--AKGADLLIHEATFLDDDA--EKAKETGH----------STAKQaaeiakkagvKKLVLTHFSA 218


                 ...
gi 446193733 248 RYS 250
Cdd:cd07717  219 RYK 221
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 18-250 1.11e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 60.29  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  18 GGIRTSLYL--PSLSLMFDIG--------AQNPNRIHLDNLLLTHSHLDHSCGLPyyisqrSLRKlkspkIFVPAPL--- 84
Cdd:COG1235   32 GRTRSSILVeaDGTRLLIDAGpdlreqllRLGLDPSKIDAILLTHEHADHIAGLD------DLRP-----RYGPNPIpvy 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  85 --KEPMQKILDLYSEIENFTYAY-ELNAVSPGDKIDLDsNHFFSPHQTFH-RVPSQGYTLYQKRKKlkkefqsisqneln 160
Cdd:COG1235  101 atPGTLEALERRFPYLFAPYPGKlEFHEIEPGEPFEIG-GLTVTPFPVPHdAGDPVGYRIEDGGKK-------------- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 161 qalkekievselseipvISFSGDTkiEYVLEH--EDVANSSILFIECTYidnernvaQAREWGHTHLDEILNNLSSFKNE 238
Cdd:COG1235  166 -----------------LAYATDT--GYIPEEvlELLRGADLLILDATY--------DDPEPGHLSNEEALELLARLGPK 218

                        250
                 ....*....|..
gi 446193733 239 KIVLIHFSKRYS 250
Cdd:COG1235  219 RLVLTHLSPDNN 230
PRK00055 PRK00055
ribonuclease Z; Reviewed
 31-253 6.48e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 49.41  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  31 LMFDIGA--Q--------NPNRIhlDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEpmqkildlysEIE 99
Cdd:PRK00055  32 FLFDCGEgtQrqllktgiKPRKI--DKIFITHLHGDHIFGLPGLLSTRSLSGRTEPlTIYGPKGIKE----------FVE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 100 NFTYAYELNavspgdkidldsnhffsphqtfhrvpsqGYTLYQKRK--KL---KKEFQSISQNELNQALKEKIEV----- 169
Cdd:PRK00055 100 TLLRASGSL----------------------------GYRIAEKDKpgKLdaeKLKALGVPPGPLFGKLKRGEDVtledg 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733 170 -----SELSEIP----VISFSGDTK-IEYVLEHedVANSSILFIECTYIDNERnvAQAREWGHthldeilnnlSSFKN-- 237
Cdd:PRK00055 152 riinpADVLGPPrkgrKVAYCGDTRpCEALVEL--AKGADLLVHEATFGDEDE--ELAKEYGH----------STARQaa 217

                        250       260
                 ....*....|....*....|....
gi 446193733 238 --------EKIVLIHFSKRYSVSY 253
Cdd:PRK00055 218 eiakeagvKRLILTHFSPRYTGDP 241
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-123 3.77e-06

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: 46.39  E-value: 3.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733    31 LMFDIGAQNPNRIhlDNLLLTHSHLDHSCGLPYyisqrsLRKLKSPKIFVPAPLKEPMQKILDLYSEIENFTYAYELN-A 109
Cdd:smart00849  24 LLAELKKLGPKKI--DAIILTHGHPDHIGGLPE------LLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDrT 95

                           90
                   ....*....|....
gi 446193733   110 VSPGDKIDLDSNHF 123
Cdd:smart00849  96 LKDGDELDLGGGEL 109
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-141 7.15e-06

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) 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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 45.71  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  39 NPNRIhlDNLLLTHSHLDHSCGLPYYI--SQRSLRKLKSPKIFVPAPLKEPMQKILDLY---SEIENFTYAYELNAVSPG 113
Cdd:cd07740   46 DPNAI--DAIFITHLHGDHFGGLPFFLldAQFVAKRTRPLTIAGPPGLRERLRRAMEALfpgSSKVPRRFDLEVIELEPG 123

                         90       100
                 ....*....|....*....|....*...
gi 446193733 114 DKIDLDSNHfFSPHQTFHRVPSQGYTLY 141
Cdd:cd07740  124 EPTTLGGVT-VTAFPVVHPSGALPLALR 150
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-245 2.22e-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: 44.22  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733   33 FDIGAQNPNRIH--------LDNLLLTHSHLDHSCGLPyyisqrSLRKLKSPKIFVPAPLKEPMQKILDLYSEIENftYA 104
Cdd:pfam12706   9 PDLRQQALPALQpgrlrddpIDAVLLTHDHYDHLAGLL------DLREGRPRPLYAPLGVLAHLRRNFPYLFLLEH--YG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  105 YELNAVSPGDKIDLDS----------NHFFSPHQTFHRVPSQGYTLYQKRKKlkkefqsisqnelnqalkekievselse 174
Cdd:pfam12706  81 VRVHEIDWGESFTVGDggltvtatpaRHGSPRGLDPNPGDTLGFRIEGPGKR---------------------------- 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446193733  175 ipvISFSGDTKieYVLEH--EDVANSSILFIECTYIDNERNVaqarEWGHTHLDEILNNLSSFKNEKIVLIHF 245
Cdd:pfam12706 133 ---VYYAGDTG--YFPDEigERLGGADLLLLDGGAWRDDEMI----HMGHMTPEEAVEAAADLGARRKVLIHI 196
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 22-135 4.66e-05

uncharacterized bacterial subgroup of Ribonuclease Z, short form; 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. Members of this bacterial 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: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 42.81  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  22 TSLYL---PSLSLMFDIG----AQNPNRI---HLDNLLLTHSHLDHS---CGLPYYI-SQRSLRKLKSPKIFVPAplkEP 87
Cdd:cd07716   18 CSGYLleaDGFRILLDCGsgvlSRLQRYIdpeDLDAVVLSHLHPDHCadlGVLQYARrYHPRGARKPPLPLYGPA---GP 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446193733  88 mqkiLDLYSEIENFTYAYELNAVSPGDKIDLDSnhF-FSPHQTFHRVPS 135
Cdd:cd07716   95 ----AERLAALYGLEDVFDFHPIEPGEPLEIGP--FtITFFRTVHPVPC 137
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 38-93 1.06e-04

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: 42.48  E-value: 1.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  38 QNPNRIHLdnlLLTHSHLDHSCGLPY----YISQRSLRklkspkIFVPAPLKEPMQKILD 93
Cdd:cd07715   54 GPPGEAHL---LLSHTHWDHIQGFPFfapaYDPGNRIH------IYGPHKDGGSLEEVLR 104
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 31-117 9.33e-04

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 39.42  E-value: 9.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  31 LMFDIGAQNPNRIH--------LDNLLLTHSHLDHSCGLPYYISQRSLRKLKSP-KIFVPAPLKEPMQKILDLYSE-IEN 100
Cdd:cd07719   30 YLVDAGSGVVRRLAqaglplgdLDAVFLTHLHSDHVADLPALLLTAWLAGRKTPlPVYGPPGTRALVDGLLAAYALdIDY 109

                         90
                 ....*....|....*..
gi 446193733 101 FTYAYELNAVSPGDKID 117
Cdd:cd07719  110 RARIGDEGRPDPGALVE 126
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 49-118 1.66e-03

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 38.29  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446193733  49 LLTHSHLDHSCGLPYyisqrsLRKLKSPKIFvpaplkepMQKIldlysEIENFTYAYE-LNAVSPGDKIDL 118
Cdd:cd16275   52 LLTHSHFDHVNLVEP------LLAKYDAPVY--------MSKE-----EIDYYGFRCPnLIPLEDGDTIKI 103
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
27-134 1.93e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.50  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733   27 PSLSLMFDIGAQNPNRIHLDNLLLTHSHLDHSCGLPYYISQRSLRKLKSPKIfvpapLKEPMQKILDLYSEIENFTYAYE 106
Cdd:pfam00753  26 AEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE-----ARELLDEELGLAASRLGLPGPPV 100

                          90       100
                  ....*....|....*....|....*...
gi 446193733  107 LNAVSPGDKIDLDSNHFFSPHQTFHRVP 134
Cdd:pfam00753 101 VPLPPDVVLEEGDGILGGGLGLLVTHGP 128
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 45-118 2.93e-03

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN 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: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 37.97  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193733  45 LDNLLLTHSHLDHSCGLPY---------YISQRSLRKLKSPKIFVPAPLKEPMQKILDLYSEIENFTyayeLNAVSPGDK 115
Cdd:cd07721   50 IRRILLTHGHIDHIGSLAAlkeapgapvYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPV----DRTLEDGDT 125


                 ...
gi 446193733 116 IDL 118
Cdd:cd07721  126 LDL 128
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 19-67 5.43e-03

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 37.05  E-value: 5.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446193733  19 GIRTSLYLPSLSLMFDIGaqnpnriHLDNLLLTHSHLDHSCGLPYYISQ 67
Cdd:cd16295   33 GGKELEELNNEPFPFDPK-------EIDAVILTHAHLDHSGRLPLLVKE 74
 
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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