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Conserved domains on  [gi|1224115052|ref|WP_092144072|]
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MBL fold metallo-hydrolase [Cupriavidus sp. YR651]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869928)

MBL fold metallo-hydrolase may have substrate towards phosphotriesters, esters, and/or lactones; similar to Pseudomonas pseudoalcaligenes phosphotriesterase opch2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 30-285 2.27e-79

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: 241.30  E-value: 2.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  30 VRVGDVDVVLISDGILPLPTSTMSTNvSEADRNKWFDGRFLQRDMFDWALNIALVRSGERLILIDSGVGDGFeyFTRAGQ 109
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGG-AAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLF--GPTAGK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 110 SVMRLESAGIDLAAITDIVITHMHMDHVGGLnVDGVKAKLHPDVRIHVSATEVAFWENPDFSKTVMPETVPPAlrKAAAK 189
Cdd:cd07720    78 LLANLAAAGIDPEDIDDVLLTHLHPDHIGGL-VDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFF--DAARD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 190 FVELYsENIVQFDREVEVAAGVSARVTGGHTPGHCVVDVASNGEKLTFVGDAIF--EVGFDKPEWQNGFEHDPEVAVDVR 267
Cdd:cd07720   155 RLRPY-AAAGRFEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHhpALQFAHPDWTIAFDVDPEQAAATR 233

                         250
                  ....*....|....*...
gi 1224115052 268 IALLNEAAETGALLAAAH 285
Cdd:cd07720   234 RRLLDRAAAEGLLVAGAH 251
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 30-285 2.27e-79

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: 241.30  E-value: 2.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  30 VRVGDVDVVLISDGILPLPTSTMSTNvSEADRNKWFDGRFLQRDMFDWALNIALVRSGERLILIDSGVGDGFeyFTRAGQ 109
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGG-AAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLF--GPTAGK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 110 SVMRLESAGIDLAAITDIVITHMHMDHVGGLnVDGVKAKLHPDVRIHVSATEVAFWENPDFSKTVMPETVPPAlrKAAAK 189
Cdd:cd07720    78 LLANLAAAGIDPEDIDDVLLTHLHPDHIGGL-VDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFF--DAARD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 190 FVELYsENIVQFDREVEVAAGVSARVTGGHTPGHCVVDVASNGEKLTFVGDAIF--EVGFDKPEWQNGFEHDPEVAVDVR 267
Cdd:cd07720   155 RLRPY-AAAGRFEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHhpALQFAHPDWTIAFDVDPEQAAATR 233

                         250
                  ....*....|....*...
gi 1224115052 268 IALLNEAAETGALLAAAH 285
Cdd:cd07720   234 RRLLDRAAAEGLLVAGAH 251
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 74-277 3.66e-21

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: 89.36  E-value: 3.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  74 MFDWALNIALVRSGERLILIDSGVGDGFEYFTRAgqsvmRLESAGIDlaaITDIVITHMHMDHVGGLnvDGVKAKLhpDV 153
Cdd:COG0491    10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLA-----ALAALGLD---IKAVLLTHLHPDHVGGL--AALAEAF--GA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 154 RIHVSATEVAFWENPDFSKTVMPETVPPalrkaaakfvelysENIVQFDREVEVAA-GVSARVTGGHTPGHCVVDVAsnG 232
Cdd:COG0491    78 PVYAHAAEAEALEAPAAGALFGREPVPP--------------DRTLEDGDTLELGGpGLEVIHTPGHTPGHVSFYVP--D 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1224115052 233 EKLTFVGDAIFEVGFDKPewqNGFEHDPEVAVDVRIALLNEAAET 277
Cdd:COG0491   142 EKVLFTGDALFSGGVGRP---DLPDGDLAQWLASLERLLALPPDL 183
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
80-285 7.37e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 7.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGERLILIDSGVGDGFEYFtragqsvMRLESAGIDLAAITDIVITHMHMDHVGGLNvdgvKAKLHPDVRIHVSA 159
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALL-------LLLAALGLGPKDIDAVILTHGHFDHIGGLG----ELAEATDVPVIVVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 160 TEVAFWENPDFSKTVMPETVPPALRKAAAKFVelyseniVQFDREVEVAAGVSARVTGGHTPGHCVVDVASNGEKLTFVG 239
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLPPDV-------VLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1224115052 240 DAIF--EVGFDKPEWQNGFEHDPEVAVDVRIALLNEAAETGALLAAAH 285
Cdd:pfam00753 149 DLLFagEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-285 5.03e-18

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: 79.90  E-value: 5.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052   80 NIALVRSGERLILIDSGVGDGFEYFTRAGQsvmrlesagIDLAAITDIVITHMHMDHVGGLnvDGVKAklHPDVRIHVSA 159
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKK---------LGPKKIDAIILTHGHPDHIGGL--PELLE--APGAPVYAPE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  160 TEVAFWENPDFSKTVMPETVPPALRkaaakFVELYSENIVQFDREvevaaGVSARVTGGHTPGHCVVDVasNGEKLTFVG 239
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPAPP-----DRTLKDGDELDLGGG-----ELEVIHTPGHTPGSIVLYL--PEGKILFTG 135

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1224115052  240 DAIFEvGFDKPEWQNGFEHDPEVAVDvriALLNEAAETGALLAAAH 285
Cdd:smart00849 136 DLLFA-GGDGRTLVDGGDAAASDALE---SLLKLLKLLPKLVVPGH 177
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-240 6.58e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 46.71  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGL-------NVDGVKAKLH----P 151
Cdd:PRK00055   24 LLRLGGELFLFDCGEG-----------TQRQLLKTGIKPRKIDKIFITHLHGDHIFGLpgllstrSLSGRTEPLTiygpK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 152 DVRIHVSATEVAFwenPDFSKTVMPETVPPALRKAAAKfvELYSENIVQFDReveVAAGVSARVTGGHT-PGHCVVDVAS 230
Cdd:PRK00055   93 GIKEFVETLLRAS---GSLGYRIAEKDKPGKLDAEKLK--ALGVPPGPLFGK---LKRGEDVTLEDGRIiNPADVLGPPR 164

                         170
                  ....*....|
gi 1224115052 231 NGEKLTFVGD 240
Cdd:PRK00055  165 KGRKVAYCGD 174
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
91-140 1.08e-04

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 43.46  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1224115052  91 ILIDSGVGDGFEYFTRAGQ-SVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:NF041257   34 ILVELGNGERDKFFFDIGSgSVANIIALQIPYNLLNKVFITHLHVDHYGDL 84
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 81-140 1.94e-03

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 39.12  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  81 IALVRSGErLILIDSGVGdgfeyfTRagqsvMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:TIGR02651  21 IALKLNGE-LWLFDCGEG------TQ-----RQMLRSGISPMKIDRIFITHLHGDHILGL 68
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 30-285 2.27e-79

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: 241.30  E-value: 2.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  30 VRVGDVDVVLISDGILPLPTSTMSTNvSEADRNKWFDGRFLQRDMFDWALNIALVRSGERLILIDSGVGDGFeyFTRAGQ 109
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGG-AAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLF--GPTAGK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 110 SVMRLESAGIDLAAITDIVITHMHMDHVGGLnVDGVKAKLHPDVRIHVSATEVAFWENPDFSKTVMPETVPPAlrKAAAK 189
Cdd:cd07720    78 LLANLAAAGIDPEDIDDVLLTHLHPDHIGGL-VDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFF--DAARD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 190 FVELYsENIVQFDREVEVAAGVSARVTGGHTPGHCVVDVASNGEKLTFVGDAIF--EVGFDKPEWQNGFEHDPEVAVDVR 267
Cdd:cd07720   155 RLRPY-AAAGRFEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHhpALQFAHPDWTIAFDVDPEQAAATR 233

                         250
                  ....*....|....*...
gi 1224115052 268 IALLNEAAETGALLAAAH 285
Cdd:cd07720   234 RRLLDRAAAEGLLVAGAH 251
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-285 6.34e-39

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: 136.50  E-value: 6.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDG-----FEYFTRAGQSVM-RLESAGIDLAAITDIVITHMHMDHVGGL--NVDGVKAKLHPDVR 154
Cdd:cd16277    17 LVRTPGRTILVDTGIGNDkprpgPPAFHNLNTPYLeRLAAAGVRPEDVDYVLCTHLHVDHVGWNtrLVDGRWVPTFPNAR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 155 IHVSATEVAFWENPD----FSKTVMPETVPPALRKAAAKFVelysenivqfDREVEVAAGVSARVTGGHTPGHCVVDVAS 230
Cdd:cd16277    97 YLFSRAEYDHWSSPDaggpPNRGVFEDSVLPVIEAGLADLV----------DDDHEILDGIRLEPTPGHTPGHVSVELES 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1224115052 231 NGEKLTFVGDAIFE-VGFDKPEWQNGFEHDPEVAVDVRIALLNEAAETGALLAAAH 285
Cdd:cd16277   167 GGERALFTGDVMHHpIQVARPDWSSVFDEDPAQAAATRRRLLERAADTDTLLFPAH 222
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 83-257 6.62e-26

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: 102.68  E-value: 6.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGD-------GFEYFTRAGQS-----VMRLESAGIDLAAITDIVITHMHMDHVGGLnvdgvkaKLH 150
Cdd:cd07729    36 LIEHPEGTILVDTGFHPdaaddpgGLELAFPPGVTeeqtlEEQLARLGLDPEDIDYVILSHLHFDHAGGL-------DLF 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 151 PDVRIHVSATEVAFWENPDfsktvmpETVPPALRKAAAKFVELYSENIVQFDREVEVAAGVSARVTGGHTPGHCVVDVAS 230
Cdd:cd07729   109 PNATIIVQRAELEYATGPD-------PLAAGYYEDVLALDDDLPGGRVRLVDGDYDLFPGVTLIPTPGHTPGHQSVLVRL 181

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1224115052 231 NGEKLTFVGDAI-----------FEVGFDKPEWQNGFE 257
Cdd:cd07729   182 PEGTVLLAGDAAytyenleegrpPGINYDPEAALASLE 219
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 76-285 7.88e-25

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: 100.26  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  76 DWALNIALVRSGERLILIDSGVGDGF-----EYFTRAGQSVMR--LESAGIDLAAITDIVITHMHMDHVGGL---NVDGV 145
Cdd:cd16281    40 TLAMRCLLIETGGRNILIDTGIGDKQdpkfrSIYVQHSEHSLLksLARLGLSPEDITDVILTHLHFDHCGGAtraDDDGL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 146 KAKLHPDVRIHVSATEvafWENpdfsktvmpeTVPPALRKAAAKFvelySENIVQF----------DREVEVAAGVSARV 215
Cdd:cd16281   120 VELLFPNATYWVQKRH---WEW----------ALNPNPRERASFL----PENIEPLeesgrlklidGSDAELGPGIRFHL 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 216 TGGHTPGHCVVDVASNGEKLTFVGDAIFEVGFDKPEWQNGFEHDPEVAVDVRIALLNEAAETGALLAAAH 285
Cdd:cd16281   183 SDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLLDEAVEEGGRLFFEH 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 74-277 3.66e-21

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: 89.36  E-value: 3.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  74 MFDWALNIALVRSGERLILIDSGVGDGFEYFTRAgqsvmRLESAGIDlaaITDIVITHMHMDHVGGLnvDGVKAKLhpDV 153
Cdd:COG0491    10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLA-----ALAALGLD---IKAVLLTHLHPDHVGGL--AALAEAF--GA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 154 RIHVSATEVAFWENPDFSKTVMPETVPPalrkaaakfvelysENIVQFDREVEVAA-GVSARVTGGHTPGHCVVDVAsnG 232
Cdd:COG0491    78 PVYAHAAEAEALEAPAAGALFGREPVPP--------------DRTLEDGDTLELGGpGLEVIHTPGHTPGHVSFYVP--D 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1224115052 233 EKLTFVGDAIFEVGFDKPewqNGFEHDPEVAVDVRIALLNEAAET 277
Cdd:COG0491   142 EKVLFTGDALFSGGVGRP---DLPDGDLAQWLASLERLLALPPDL 183
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 75-265 5.94e-20

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: 85.74  E-value: 5.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  75 FDWALNIALVRSGERLILIDSGVGDGFEYFTRAgqsvmrLESAGIDLAAITDIVITHMHMDHVGGLnvdgvkAKL--HPD 152
Cdd:cd07721     7 LLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKA------LRELGLSPKDIRRILLTHGHIDHIGSL------AALkeAPG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 153 VRIHVSATEVAFWENPDFSKtvmpetvPPALRKAAAKFVELYSENIVQFDREVE----VAAGVSARV--TGGHTPGHCVV 226
Cdd:cd07721    75 APVYAHEREAPYLEGEKPYP-------PPVRLGLLGLLSPLLPVKPVPVDRTLEdgdtLDLAGGLRVihTPGHTPGHISL 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1224115052 227 DVASNGekLTFVGDAIFEVGFDKPEWQNGFEHDPEVAVD 265
Cdd:cd07721   148 YLEEDG--VLIAGDALVTVGGELVPPPPPFTWDMEEALE 184
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
80-285 7.37e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 7.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGERLILIDSGVGDGFEYFtragqsvMRLESAGIDLAAITDIVITHMHMDHVGGLNvdgvKAKLHPDVRIHVSA 159
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALL-------LLLAALGLGPKDIDAVILTHGHFDHIGGLG----ELAEATDVPVIVVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 160 TEVAFWENPDFSKTVMPETVPPALRKAAAKFVelyseniVQFDREVEVAAGVSARVTGGHTPGHCVVDVASNGEKLTFVG 239
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLPPDV-------VLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1224115052 240 DAIF--EVGFDKPEWQNGFEHDPEVAVDVRIALLNEAAETGALLAAAH 285
Cdd:pfam00753 149 DLLFagEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 83-240 5.86e-19

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: 84.23  E-value: 5.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDG------FEYF--TRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGLN--VDGVKAKLHPD 152
Cdd:cd07728    47 LIQYQGKNYLIDAGIGNGkltekqKRNFgvTEESSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTkvKGEQLVSVFPN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 153 VRIHVSATEvafWE---NPDF-SK-TVMPETVPPalrkaaakfvelYSENIVQFDREVEVAAGVSARVTGGHTPGHCVVD 227
Cdd:cd07728   127 ATIYVSEIE---WEemrNPNIrSKnTYWKENWEP------------IEDQVKTFSDEIEIVPGITMIHTGGHSDGHSIIE 191

                         170
                  ....*....|...
gi 1224115052 228 VASNGEKLTFVGD 240
Cdd:cd07728   192 IEQGGETAIHMAD 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-285 5.03e-18

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: 79.90  E-value: 5.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052   80 NIALVRSGERLILIDSGVGDGFEYFTRAGQsvmrlesagIDLAAITDIVITHMHMDHVGGLnvDGVKAklHPDVRIHVSA 159
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKK---------LGPKKIDAIILTHGHPDHIGGL--PELLE--APGAPVYAPE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  160 TEVAFWENPDFSKTVMPETVPPALRkaaakFVELYSENIVQFDREvevaaGVSARVTGGHTPGHCVVDVasNGEKLTFVG 239
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPAPP-----DRTLKDGDELDLGGG-----ELEVIHTPGHTPGSIVLYL--PEGKILFTG 135

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1224115052  240 DAIFEvGFDKPEWQNGFEHDPEVAVDvriALLNEAAETGALLAAAH 285
Cdd:smart00849 136 DLLFA-GGDGRTLVDGGDAAASDALE---SLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 80-243 1.30e-14

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: 70.78  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGER-LILIDSGvGDGFEYFTRAgqsvmrLESAGIDLAAItdiVITHMHMDHVGGLNvdgvKAKLHPDVRIHVS 158
Cdd:cd06262    11 NCYLVSDEEGeAILIDPG-AGALEKILEA------IEELGLKIKAI---LLTHGHFDHIGGLA----ELKEAPGAPVYIH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 159 ATEVAFWENPDFSKTVMPETVPPALRKaaakfvelysENIVQFDREVEVAA-GVSARVTGGHTPGHCVVDVASngEKLTF 237
Cdd:cd06262    77 EADAELLEDPELNLAFFGGGPLPPPEP----------DILLEDGDTIELGGlELEVIHTPGHTPGSVCFYIEE--EGVLF 144


                  ....*.
gi 1224115052 238 VGDAIF 243
Cdd:cd06262   145 TGDTLF 150
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 79-260 7.51e-13

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 65.78  E-value: 7.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  79 LNIALVRSGERLILIDSGVGDgfeyfTRAGQSVM-RLESAGIDLAAITDIVITHMHMDHVGGLNVdgVKAKLHPDVRIhv 157
Cdd:cd07725    15 VNVYLLRDGDETTLIDTGLAT-----EEDAEALWeGLKELGLKPSDIDRVLLTHHHPDHIGLAGK--LQEKSGATVYI-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 158 satevafwenpdfsktVMPETVPpalrkaaakfvelysenivqfDREVEVAAGVSARV--TGGHTPGH-CVVDVasnGEK 234
Cdd:cd07725    86 ----------------LDVTPVK---------------------DGDKIDLGGLRLKVieTPGHTPGHiVLYDE---DRR 125

                         170       180
                  ....*....|....*....|....*...
gi 1224115052 235 LTFVGDAIFEvgFDKPE--WQNGFEHDP 260
Cdd:cd07725   126 ELFVGDAVLP--KITPNvsLWAVRVEDP 151
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 80-244 7.66e-13

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 66.02  E-value: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGERLILIDSGvgDGFEYFTRAGQSVMRLESAgidlAAITDIVITHMHMDHVGGLnvdgvkaklhPDVRIHVSA 159
Cdd:cd07722    19 NTYLVGTGKRRILIDTG--EGRPSYIPLLKSVLDSEGN----ATISDILLTHWHHDHVGGL----------PDVLDLLRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 160 TEVAFWENPdfsktvmPETVPPALRKAAAKFVELYSENIVQfdrevevAAGVSARVTggHTPGHCvVDVAS---NGEKLT 236
Cdd:cd07722    83 PSPRVYKFP-------RPEEDEDPDEDGGDIHDLQDGQVFK-------VEGATLRVI--HTPGHT-TDHVCfllEEENAL 145

                         170
                  ....*....|....*
gi 1224115052 237 FVGD-------AIFE 244
Cdd:cd07722   146 FTGDcvlghgtAVFE 160
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 80-274 4.61e-11

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: 60.68  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGERLILIDSG-VGDGFEYftragqsVMRLESAGIDLAAITDIVITHMHMDHVGGLNvdgvkakLHPDVRIHVS 158
Cdd:cd07711    23 TVTLIKDGGKNILVDTGtPWDRDLL-------LKALAEHGLSPEDIDYVVLTHGHPDHIGNLN-------LFPNATVIVG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 159 -ATEVAFWENPDFSKtvmpetvppalrkaaakfvelysenivqfDREVEVAAGVSARVTGGHTPGHC--VVDVASNGeKL 235
Cdd:cd07711    89 wDICGDSYDDHSLEE-----------------------------GDGYEIDENVEVIPTPGHTPEDVsvLVETEKKG-TV 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1224115052 236 TFVGDAI-FEVGFDKPEWQNGFEHDPEVAVDVRIALLNEA 274
Cdd:cd07711   139 AVAGDLFeREEDLEDPILWDPLSEDPELQEESRKRILALA 178
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-243 3.76e-10

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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 59.18  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGF-----EYFTRAGQSVMR------------LESAGIDLAAITDIVITHMHMDHVGGLnVDgv 145
Cdd:cd07742    23 LVETDDGLVLVDTGFGLADvadpkRRLGGPFRRLLRprldedetavrqIEALGFDPSDVRHIVLTHLDLDHAGGL-AD-- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 146 kaklHPDVRIHVSATEVAFWENPdfsKTVMPETVPPALRKAAAKFVELYS---ENIVQFDrEVEVAAGVSARVT----GG 218
Cdd:cd07742   100 ----FPHATVHVHAAELDAATSP---RTRYERRRYRPQQLAHGPWWVTYAaggERWFGFE-AVRPLDGLPPEILlvplPG 171

                         170       180
                  ....*....|....*....|....*
gi 1224115052 219 HTPGHCVVDVASNGEKLTFVGDAIF 243
Cdd:cd07742   172 HTRGHCGVAVRTGDRWLLHAGDAYF 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-243 1.28e-09

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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 56.77  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRSGER-LILIDSGVGDgfeyftRAGQSVMR-LESAGIDLAAItdiVITHMHMDHVGGlNVDGVKaklHPDVRIHV 157
Cdd:cd07743     9 NIGVYVFGDKeALLIDSGLDE------DAGRKIRKiLEELGWKLKAI---INTHSHADHIGG-NAYLQK---KTGCKVYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 158 SATEVAFWENPD-FSKTVMPETVPPALRKAAAKFVELYSENIVQFDREVEVAAGVSARVTGGHTPGHCVVdvaSNGEKLT 236
Cdd:cd07743    76 PKIEKAFIENPLlEPSYLGGAYPPKELRNKFLMAKPSKVDDIIEEGELELGGVGLEIIPLPGHSFGQIGI---LTPDGVL 152


                  ....*..
gi 1224115052 237 FVGDAIF 243
Cdd:cd07743   153 FAGDALF 159
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
83-141 2.67e-09

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 56.74  E-value: 2.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGLN 141
Cdd:COG1234    23 LLEAGGERLLIDCGEG-----------TQRQLLRAGLDPRDIDAIFITHLHGDHIAGLP 70
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 83-140 3.07e-09

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: 55.60  E-value: 3.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:cd07719    22 LVVVGGRVYLVDAGSG-----------VVRRLAQAGLPLGDLDAVFLTHLHSDHVADL 68
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 83-241 4.89e-09

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: 55.58  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGFEYFTRAgqsvmrLESAGIDLAAITDIVITHMHMDHVGGLnvdGVKAKLHPDVRIHV----- 157
Cdd:cd07726    20 LLDGEGRPALIDTGPSSSVPRLLAA------LEALGIAPEDVDYIILTHIHLDHAGGA---GLLAEALPNAKVYVhprga 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 158 -----------SATEVAFWENPDFSKTVMPetVPpalrkaAAKFVELYSENIVQF-DREVEVAagvsarvtggHTPGH-- 223
Cdd:cd07726    91 rhlidpsklwaSARAVYGDEADRLGGEILP--VP------EERVIVLEDGETLDLgGRTLEVI----------DTPGHap 152

                         170       180
                  ....*....|....*....|.
gi 1224115052 224 ---CVVDVASNGeklTFVGDA 241
Cdd:cd07726   153 hhlSFLDEESDG---LFTGDA 170
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 83-140 5.69e-09

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: 54.58  E-value: 5.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:cd16272    21 LLETGGTRILLDCGEG-----------TVYRLLKAGVDPDKLDAIFLSHFHLDHIGGL 67
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
82-192 9.07e-09

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 55.27  E-value: 9.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  82 ALVRSGERLILIDSGVGDGFEYftragqsvmRLESAGIDLAAITDIVITHMHMDHVGGLnvDGV-KAKLHPDVRIHVSAT 160
Cdd:COG1237    25 ALIETEGKRILFDTGQSDVLLK---------NAEKLGIDLSDIDAVVLSHGHYDHTGGL--PALlELNPKAPVYAHPDAF 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1224115052 161 EVAFWENPDFSKTVMPETvPPALRKAAAKFVE 192
Cdd:COG1237    94 EKRYSKRPGGKYIGIPFS-REELEKLGARLIL 124
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-236 5.50e-08

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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 52.97  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGFEYFTRAGqsvmrLESAGIDLAAITDIVITHMHMDHVGGLNVdgVKAKLHPdvRIHVSATEV 162
Cdd:cd16280    26 AIDTGDGLILIDALNNNEAADLIVDG-----LEKLGLDPADIKYILITHGHGDHYGGAAY--LKDLYGA--KVVMSEADW 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224115052 163 AFWENPDFSKTVMPETVPPalrkaaAKFVELYSENIVQF-DREVEVaagvsaRVTGGHTPG--HCVVDVASNGEKLT 236
Cdd:cd16280    97 DMMEEPPEEGDNPRWGPPP------ERDIVIKDGDTLTLgDTTITV------YLTPGHTPGtlSLIFPVKDGGKTHR 161
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 80-243 5.62e-08

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 52.35  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  80 NIALVRS--GERLILIDSGvgdgfeyfTRAGQSVMRLESAGIDLAAItdiVITHMHMDHVGGLNVdgvkAKLHPDVRIHV 157
Cdd:cd16322    12 NTYLVADegGGEAVLVDPG--------DESEKLLARFGTTGLTLLYI---LLTHAHFDHVGGVAD----LRRHPGAPVYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 158 SATEVAFWENPD-FSKT--VMPETVPPALRKAAakfvelysenivqfDREVEVAAGVSARV--TGGHTPGHCVVDVASng 232
Cdd:cd16322    77 HPDDLPLYEAADlGAKAfgLGIEPLPPPDRLLE--------------DGQTLTLGGLEFKVlhTPGHSPGHVCFYVEE-- 140

                         170
                  ....*....|.
gi 1224115052 233 EKLTFVGDAIF 243
Cdd:cd16322   141 EGLLFSGDLLF 151
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 83-240 1.21e-07

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 51.18  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGFEYFTRAgqsvmrLESAGIDLAAITDIVITHMHMDHVGGL-------NVDGVKAKLHPDVRI 155
Cdd:cd07734    15 LVEFKGRTVLLDCGMNPGKEDPEAC------LPQFELLPPEIDAILISHFHLDHCGALpylfrgfIFRGPIYATHPTVAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 156 --------HVSATEVAFWENpdfskTVMPETVppalRKAAAKFVEL-YSEnIVQFDREVEVAAGVSarvtgGHTPGHCVV 226
Cdd:cd07734    89 grllledyVKSAERIGQDQS-----LYTPEDI----EEALKHIVPLgYGQ-SIDLFPALSLTAYNA-----GHVLGAAMW 153

                         170
                  ....*....|....
gi 1224115052 227 DVASNGEKLTFVGD 240
Cdd:cd07734   154 EIQIYGEKLVYTGD 167
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-244 3.45e-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.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 49.87  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  69 FLQRDMFDWALNIALVRSGERLILIDSGvgdgfeYFTRAGQSVMRLesagidLAAITD-----IVITHMHMDHVGGLNV- 142
Cdd:cd16282     5 LIGPDGGGFISNIGFIVGDDGVVVIDTG------ASPRLARALLAA------IRKVTDkpvryVVNTHYHGDHTLGNAAf 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 143 DGVKAKL--HPDVRIHVSATEVAFWEN-PDFSKTVMPET--VPPALRKAAAKFVELYsenivqfDREVEVAAgvsarVTG 217
Cdd:cd16282    73 ADAGAPIiaHENTREELAARGEAYLELmRRLGGDAMAGTelVLPDRTFDDGLTLDLG-------GRTVELIH-----LGP 140

                         170       180
                  ....*....|....*....|....*..
gi 1224115052 218 GHTPGHCVVDVASngEKLTFVGDAIFE 244
Cdd:cd16282   141 AHTPGDLVVWLPE--EGVLFAGDLVFN 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 114-243 3.53e-07

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: 49.46  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 114 LESAGIDLAAITDIVITHMHMDHVGglnvdGVKAKLH-PDVRIHVSATEVAFWENPdfsktvmpetvppalrkaaakfve 192
Cdd:cd16275    38 LAKLNELGLTLTGILLTHSHFDHVN-----LVEPLLAkYDAPVYMSKEEIDYYGFR------------------------ 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1224115052 193 lySENIVQFDREVEVAAG---VSARVTGGHTPG-HC--VvdvasnGEKLtFVGDAIF 243
Cdd:cd16275    89 --CPNLIPLEDGDTIKIGdteITCLLTPGHTPGsMCylL------GDSL-FTGDTLF 136
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 67-140 3.62e-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) 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: 49.56  E-value: 3.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224115052  67 GRFlqRDMFdwalniaLVRSGERLILIDSGvgdgfeyftraGQSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:cd07740    13 GRL--NTCF-------HVASEAGRFLIDCG-----------ASSLIALKRAGIDPNAIDAIFITHLHGDHFGGL 66
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-241 7.31e-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: 49.57  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  82 ALVR-SGERLILIDSGVG-DGFEYfTRAGQSVMR---------------LESAGIDLAAITDIVITHMHMDHVGGLnvdg 144
Cdd:cd07730    26 FLIEhPTGGKILFDLGYRkDFEEY-TPRVPERLYrtpvpleveedvaeqLAAGGIDPEDIDAVILSHLHWDHIGGL---- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 145 vkaKLHPDVRIHVSATEVAFWENPDFSKTVMPETVPPALRKAAAKFVELysenivqFDREVEVAAGVSAR---------- 214
Cdd:cd07730   101 ---SDFPNARLIVGPGAKEALRPPGYPSGFLPELLPSDFEGRLVRWEED-------DFLWVPLGPFPRALdlfgdgslyl 170

                         170       180
                  ....*....|....*....|....*....
gi 1224115052 215 V-TGGHTPGH-CVVDVASNGEKLTFVGDA 241
Cdd:cd07730   171 VdLPGHAPGHlGLLARTTSGTWVFLAGDA 199
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 82-153 1.74e-06

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 48.39  E-value: 1.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224115052  82 ALVRSGERLILIDSGVGDGFEYftragqsvmRLESAGIDLAAITDIVITHMHMDHVGGL-----NVDGVKAKLHPDV 153
Cdd:cd07713    23 LLIETEGKKILFDTGQSGVLLH---------NAKKLGIDLSDIDAVVLSHGHYDHTGGLkalleLNPKAPVYAHPDA 90
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 80-142 3.02e-06

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 46.10  E-value: 3.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224115052  80 NIALVRSGERLILIDSGVGdgfeyfTRAGQSvmRLESAGIDLAAITDIVITHMHMDHVGGLNV 142
Cdd:cd07733    10 NCTYLETEDGKLLIDAGLS------GRKITG--RLAEIGRDPEDIDAILVTHEHADHIKGLGV 64
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 76-242 3.34e-06

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 46.47  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  76 DWALNIALVRSGERLILIDSGVGDG--FEYftragqsVMRLEsagiDLAAItdIVITHMHMDHVGGLNvDGVKAKLHPDv 153
Cdd:cd07712     6 DDRVNIYLLRGRDRALLIDTGLGIGdlKEY-------VRTLT----DLPLL--VVATHGHFDHIGGLH-EFEEVYVHPA- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 154 rihvsatEVAFWENPDFSKTVMPETVPPALRKAAAKFVELYSENIVQFDREVEVAAgvsarvTGGHTPGH-CVVDVASng 232
Cdd:cd07712    71 -------DAEILAAPDNFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIH------TPGHTPGSiALLDRAN-- 135

                         170
                  ....*....|
gi 1224115052 233 eKLTFVGDAI 242
Cdd:cd07712   136 -RLLFSGDVV 144
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-240 6.58e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 46.71  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGL-------NVDGVKAKLH----P 151
Cdd:PRK00055   24 LLRLGGELFLFDCGEG-----------TQRQLLKTGIKPRKIDKIFITHLHGDHIFGLpgllstrSLSGRTEPLTiygpK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 152 DVRIHVSATEVAFwenPDFSKTVMPETVPPALRKAAAKfvELYSENIVQFDReveVAAGVSARVTGGHT-PGHCVVDVAS 230
Cdd:PRK00055   93 GIKEFVETLLRAS---GSLGYRIAEKDKPGKLDAEKLK--ALGVPPGPLFGK---LKRGEDVTLEDGRIiNPADVLGPPR 164

                         170
                  ....*....|
gi 1224115052 231 NGEKLTFVGD 240
Cdd:PRK00055  165 KGRKVAYCGD 174
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 82-161 1.63e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 45.27  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  82 ALVRSGERLILIDSGVGdgfeyftragqsvMR--LESAGIDLAAITDIVITHMHMDHVGGLnvdGVKAKLHPDVRIHVSA 159
Cdd:COG1235    38 ILVEADGTRLLIDAGPD-------------LReqLLRLGLDPSKIDAILLTHEHADHIAGL---DDLRPRYGPNPIPVYA 101


                  ..
gi 1224115052 160 TE 161
Cdd:COG1235   102 TP 103
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 83-222 2.25e-05

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 45.03  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGfeyftrAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGLnvdgvkAKLHPDVRIHVSATEV 162
Cdd:cd16315    26 LITGDDGHVLIDSGTEEA------APLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGL------AALQRATGARVAASAA 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224115052 163 AfwenpdfsKTVMpETVPPALRKAAAKFVELYSEniVQFDREVE----VAAG---VSARVTGGHTPG 222
Cdd:cd16315    94 A--------APVL-ESGKPAPDDPQAGLHEPFPP--VRVDRIVEdgdtVALGslrLTAHATPGHTPG 149
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 83-140 2.60e-05

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 45.50  E-value: 2.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052  83 LVRSGERLILIDSGVGDGfeyftRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:COG1782    18 LLETGESRILLDCGLFQG-----GREERERNNDAFPFDPEELDAVVLTHAHLDHSGLL 70
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 83-140 4.35e-05

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: 43.98  E-value: 4.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052  83 LVRSGERLILIDSGVGdgfeyftragqSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:cd07717    21 ALRLEGELWLFDCGEG-----------TQRQLLRAGLSPSKIDRIFITHLHGDHILGL 67
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 83-240 5.38e-05

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 44.41  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGFEYFTRagqsvmrlESAGIDLAAITDIVITHMHMDHVGGLNvdgVKAKLHPDVRIHvsATEV 162
Cdd:COG1236    18 LLETGGTRILIDCGLFQGGKERNW--------PPFPFRPSDVDAVVLTHAHLDHSGALP---LLVKEGFRGPIY--ATPA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 163 AFwenpDFSKTVMP----------ETVPPALRKAAAKFVELYSEniVQFDREVEVaAGVSARVTG-GHTPGHCVVDVASN 231
Cdd:COG1236    85 TA----DLARILLGdsakiqeeeaEAEPLYTEEDAERALELFQT--VDYGEPFEI-GGVRVTFHPaGHILGSAQVELEVG 157


                  ....*....
gi 1224115052 232 GEKLTFVGD 240
Cdd:COG1236   158 GKRIVFSGD 166
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 91-156 5.61e-05

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: 43.74  E-value: 5.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  91 ILID--SGVGDGFEYFTRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGL--NVDGVKAKLHPDVRIH 156
Cdd:cd07735    31 ILLDagTGVGALSLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLplLSPNDGGQRGSPKTIY 100
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 83-140 7.90e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.51  E-value: 7.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224115052  83 LVRSGERLILIDSGvgdgfEYFTRAGQSVMR-LESAGIDlaAITDIVITHMHMDHVGGL 140
Cdd:cd07731    14 LIQTPGKTILIDTG-----PRDSFGEDVVVPyLKARGIK--KLDYLILTHPDADHIGGL 65
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 83-240 8.68e-05

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: 42.83  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVgdgfeYFTRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGLnvdgvkAKLH---PDVRIHvsA 159
Cdd:cd16295    16 LLETGGKRILLDCGL-----FQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRL------PLLVkegFRGPIY--A 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 160 TEVAFwenpDFSKTVMPETVPPALRKAAAKFVE-LYSEN----------IVQFDREVEVAAGVSARVT-GGHTPG--HCV 225
Cdd:cd16295    83 TPATK----DLAELLLLDSAKIQEEEAEHPPAEpLYTEEdvekalkhfrPVEYGEPFEIGPGVKVTFYdAGHILGsaSVE 158

                         170
                  ....*....|....*
gi 1224115052 226 VDVaSNGEKLTFVGD 240
Cdd:cd16295   159 LEI-GGGKRILFSGD 172
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
91-140 1.08e-04

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 43.46  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1224115052  91 ILIDSGVGDGFEYFTRAGQ-SVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:NF041257   34 ILVELGNGERDKFFFDIGSgSVANIIALQIPYNLLNKVFITHLHVDHYGDL 84
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 83-238 1.22e-04

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 42.82  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGVGDGFEYFTRAGQSVmrlesaGIDLAAITDIVITHMHMDHVGGLnvdgvkAKLHPDV--RIHVSAT 160
Cdd:cd16310    26 LITSNHGAILLDGGLEENAALIEQNIKAL------GFKLSDIKIIINTHAHYDHAGGL------AQLKADTgaKLWASRG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 161 EVAFWEN--PDFSKTVMPETVPPAlrkaaakfvelYSENIVQfDREVEVAAGVS--ARVTGGHTPGhCV---VDVASNGE 233
Cdd:cd16310    94 DRPALEAgkHIGDNITQPAPFPAV-----------KVDRILG-DGEKIKLGDITltATLTPGHTKG-CTtwsTTVKENGR 160


                  ....*
gi 1224115052 234 KLTFV 238
Cdd:cd16310   161 PLRVV 165
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 82-266 1.39e-04

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 42.54  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  82 ALVRSGE-RLILIDSGVGDGFEyftrAGQSVMR--LESAGIDlaAITDIVITHMHMDHVGGLnvDGVKAKLHPDvrihvs 158
Cdd:COG2333    14 ILIRTPDgKTILIDTGPRPSFD----AGERVVLpyLRALGIR--RLDLLVLTHPDADHIGGL--AAVLEAFPVG------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 159 atevAFWENPDFSKTVMPETVPPALRKAAAKFVELYSENIVQFDrevevaaGVSARV------TGGHTPGH---CVVDVA 229
Cdd:COG2333    80 ----RVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLG-------GVRFEVlwppedLLEGSDENnnsLVLRLT 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1224115052 230 SNGEKLTFVGDAifevgfDKPEWQNGFEHDPEVAVDV 266
Cdd:COG2333   149 YGGFSFLLTGDA------EAEAEAALLARGPDLKADV 179
NorV COG0426
Flavorubredoxin [Energy production and conversion];
83-159 2.64e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.13  E-value: 2.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224115052  83 LVRsGERLILIDSgVGDGF--EYFtragqsvMRLESAgIDLAAITDIVITHMHMDHVGGLNvdgVKAKLHPDVRIHVSA 159
Cdd:COG0426    38 LIV-DEKTALIDT-VGESFfeEFL-------ENLSKV-IDPKKIDYIIVNHQEPDHSGSLP---ELLELAPNAKIVCSK 103
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 114-243 3.25e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 40.52  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 114 LESAGIDLAAItdiVITHMHMDHVGGlnVDGVKAKlHPDVRIHVSAtevafwenpdfsktvmpETVPPALrkaaakfvel 193
Cdd:cd07723    37 LEKNGLTLTAI---LTTHHHWDHTGG--NAELKAL-FPDAPVYGPA-----------------EDRIPGL---------- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1224115052 194 ysENIVQFDREVEVaAGVSARV--TGGHTPGHcvvdVA--SNGEKLTFVGDAIF 243
Cdd:cd07723    84 --DHPVKDGDEIKL-GGLEVKVlhTPGHTLGH----ICyyVPDEPALFTGDTLF 130
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 87-177 3.31e-04

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 41.32  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  87 GERLILIDSgVGDGFeyftrAGQSVMRLESAgIDLAAITDIVITHMHMDHVGGLNvdgVKAKLHPDVRIHVSATEV---- 162
Cdd:cd07709    39 DEKTALIDT-VKEPF-----FDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLP---ELLELAPNAKIVCSKKAArflk 108

                          90
                  ....*....|....*
gi 1224115052 163 AFWENPDFSKTVMPE 177
Cdd:cd07709   109 HFYPGIDERFVVVKD 123
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 79-222 1.17e-03

Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293869  Cd Length: 257  Bit Score: 39.97  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  79 LNIALVRSGERLILIDSGVGDGfeyftrAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGL----NVDGVKAKLHPDVR 154
Cdd:cd16311    22 LSSVLVTSPQGHVLVDGGLPES------APKIIANIEALGFRIEDVKLILNSHGHIDHAGGLaelqRRSGALVAASPSAA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052 155 IHVSATEVAfwenPDFSKTVMPETVPPALRKAAAKFVELYSENIVQfdrevevaagVSARVTGGHTPG 222
Cdd:cd16311    96 LDLASGEVG----PDDPQYHALPKYPPVKDMRLARDGGQFNVGPVS----------LTAHATPGHTPG 149
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 79-222 1.33e-03

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 39.64  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  79 LNIALVRSGERLILIDSGVGdgfeyftragQSVMRLES----AGIDLAAITDIVITHMHMDHVGGLnvdgvkAKLHPDVR 154
Cdd:cd16290    22 LSAVLITSPQGLILIDGALP----------QSAPQIEAniraLGFRLEDVKLILNSHAHFDHAGGI------AALQRDSG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224115052 155 IHVSATEVAfwenpdfSKTVMPETVPPALRKAAakFVELYSEniVQFDREVE----VAAG---VSARVTGGHTPG 222
Cdd:cd16290    86 ATVAASPAG-------AAALRSGGVDPDDPQAG--AADPFPP--VAKVRVVAdgevVKLGplaVTAHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 82-140 1.60e-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: 38.99  E-value: 1.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224115052  82 ALVRSGERLILIDSGvGDgfeyftragqsvMR--LESAGIDlaAITDIVITHMHMDHVGGL 140
Cdd:cd16279    38 ILIETGGKNILIDTG-PD------------FRqqALRAGIR--KLDAVLLTHAHADHIHGL 83
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 82-140 1.77e-03

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: 38.76  E-value: 1.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224115052  82 ALVRSGERLILIDSGVGDGFEYFtRAGQsvmrlesagidlaaITDIVITHMHMDHVGGL 140
Cdd:cd07736    40 ALIEVDGERILLDAGLTDLAERF-PPGS--------------IDAILLTHFHMDHVQGL 83
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 81-140 1.94e-03

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 39.12  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  81 IALVRSGErLILIDSGVGdgfeyfTRagqsvMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:TIGR02651  21 IALKLNGE-LWLFDCGEG------TQ-----RQMLRSGISPMKIDRIFITHLHGDHILGL 68
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
91-140 3.34e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 38.40  E-value: 3.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1224115052  91 ILIDSG-VGDGFEyftRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGL 140
Cdd:COG5212    42 VLLDAGtVVSGLE---LAEQKGAFKGRQGYVLEHIKGYLISHAHLDHIAGL 89
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 84-140 4.22e-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: 37.86  E-value: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1224115052  84 VRSGERLILIDSGVGdgfeyFTRAGQSVMRlESAGIDLaaitDIVITHMHMDHVGGL 140
Cdd:cd07715    28 VRAGGELLILDAGTG-----IRELGNELMK-EGPPGEA----HLLLSHTHWDHIQGF 74
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 83-140 5.39e-03

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849  Cd Length: 199  Bit Score: 37.24  E-value: 5.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224115052  83 LVRSGERLILIDSGVGDG---------FEYFTRAGQsvmrlesagidLAAITD-IVITHMHMDHVGGL 140
Cdd:cd16291    16 LVTIGGKNIMFDCGMHMGynderrfpdFSYISQNGP-----------FTEHIDcVIISHFHLDHCGAL 72
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 83-238 7.16e-03

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 37.30  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  83 LVRSGERLILIDSGvgdgfeYFTRAGQSVMRLESAGIDLAAITDIVITHMHMDHVGGLnvdgVKAKLHPDVRIHVSATEV 162
Cdd:cd16288    26 LITTPQGLILIDTG------LESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGL----AALKKLTGAKLMASAEDA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 163 AFWE---NPDFSKTVMPETVPPalrkaaakfvelyseniVQFDREV----EVAAG---VSARVTGGHTPGHC--VVDVAS 230
Cdd:cd16288    96 ALLAsggKSDFHYGDDSLAFPP-----------------VKVDRVLkdgdRVTLGgttLTAHLTPGHTRGCTtwTMTVKD 158


                  ....*...
gi 1224115052 231 NGEKLTFV 238
Cdd:cd16288   159 DGKVYQVV 166
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 91-264 8.63e-03

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: 36.90  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052  91 ILIDSGVgDGFEYFTRAGQSVMRLESaGIDLaaitdIVITHMHMDHVGGLNV--DGVKAKL--HPDVRIHVSATEVAFWE 166
Cdd:pfam12706   3 ILIDPGP-DLRQQALPALQPGRLRDD-PIDA-----VLLTHDHYDHLAGLLDlrEGRPRPLyaPLGVLAHLRRNFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224115052 167 NPDFSKTVMP----ETVPPALRKAAAKFVELYSENIVQFDREVEVAAGVsaRVTGG-----HTPGHCVVDvasnGEKLTF 237
Cdd:pfam12706  76 LEHYGVRVHEidwgESFTVGDGGLTVTATPARHGSPRGLDPNPGDTLGF--RIEGPgkrvyYAGDTGYFP----DEIGER 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1224115052 238 VGDA---IFEVGFDKPEWQNGFEH-DPEVAV 264
Cdd:pfam12706 150 LGGAdllLLDGGAWRDDEMIHMGHmTPEEAV 180
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 80-140 8.77e-03

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 37.00  E-value: 8.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224115052  80 NIALVRSGERLILIDSGVGdgFEyftragqsvmRLESAGIDLAaITD-------------IVITHMHMDHVGGL 140
Cdd:cd07714    12 NMYVVEYDDDIIIIDCGLK--FP----------DEDMPGVDYI-IPDfsyleenkdkikgIFITHGHEDHIGAL 72
 
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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