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Conserved domains on  [gi|515634100|ref|WP_017066700|]
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MULTISPECIES: phosphonate metabolism protein PhnP [Vibrio]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870211)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-186 2.79e-103

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: 297.61  E-value: 2.79e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAALEDPNLRREKSSAYLEHNGKFLLLDANAPDLMCRFPAGSIDKILLTHYHMDHV 80
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  81 HSLFDLRWGAGDKISVMSPDDPLGCDDLYKHPGILDFSQRAQAFKSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYL 160
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 515634100 161 TDTVGLPKQTERWLKEFPVDWLITDC 186
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
 
Name Accession Description Interval E-value
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-186 2.79e-103

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: 297.61  E-value: 2.79e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAALEDPNLRREKSSAYLEHNGKFLLLDANAPDLMCRFPAGSIDKILLTHYHMDHV 80
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  81 HSLFDLRWGAGDKISVMSPDDPLGCDDLYKHPGILDFSQRAQAFKSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYL 160
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 515634100 161 TDTVGLPKQTERWLKEFPVDWLITDC 186
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 14-238 4.73e-98

phosphonate metabolism protein PhnP; This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in E. coli and is a member of the metallo-beta-lactamase superfamily (pfam00753). As defined by this model, all instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP.


Pssm-ID: 163212  Cd Length: 238  Bit Score: 286.23  E-value: 4.73e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   14 VPVYGCDCSVCGAALEDPNLRREKSSAYLEHNGKFLLLDANAPDLMCRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDK 93
Cdd:TIGR03307   4 VPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGVGEP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   94 ISVMSPDDPLGCDDLYKHPGILDFSQRAQAFKSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYLTDTVGLPKQTERW 173
Cdd:TIGR03307  84 IPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDTEAF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634100  174 LKEFPVDWLITDCNYPPIEDPQArtslNHNDFHHILDIDETCRPTNLGLIHVSHHMLGWAEQHPQ 238
Cdd:TIGR03307 164 LKNHPLDVLILDCSHPPQSDAPR----NHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPD 224
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-255 1.35e-46

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 155.82  E-value: 1.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCgaALEDPNLRREKSSAYLEHNGKFLLLDAnAPDL---MCRFPAG--SIDKILLTHY 75
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDA-GPDLreqLLRLGLDpsKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  76 HMDHVHSLFDLRWGAGDK-ISVMSPDDPLgcDDL--------YKHPGILDFsQRAQAFKSFDWQGITITPLPLNHSKL-C 145
Cdd:COG1235   78 HADHIAGLDDLRPRYGPNpIPVYATPGTL--EALerrfpylfAPYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 146 LGYCLEFDGKRLAYLTDTVGLPKQTERWLKEfpVDWLITDCNYPPiEDPqartslNHNDFHHILDIDETCRPTNLGLIHV 225
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDD-PEP------GHLSNEEALELLARLGPKRLVLTHL 225

                        250       260       270
                 ....*....|....*....|....*....|....
gi 515634100 226 SH----HMLGWAEQHPQAFSERLRILSDGEEITL 255
Cdd:COG1235  226 SPdnndHELDYDELEAALLPAGVEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-255 3.25e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 91.77  E-value: 3.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAAleDPNLRREKSSAYLEHNGKFLLLDAnAPDL---MCRFPAGSIDKILLTHYHM 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDC-GPDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  78 DHVHSLFDLR-WGAGDKISVMSPDDPLG--------CDDLYKHPGILDFS-QRAQAFKSFDWQGITITPLPLNHSKL-CL 146
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLpIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 147 GYCLefdgKRLAYLTDTVGLPKQTERWLKEfpVDWLITDCnYPPIEDPqartslNHNDFHHILDIDETCRPTNLGLIHVS 226
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNA-LRIAPHP------THQSLEEALENIKRIGAKETYLIHMS 224

                        250       260
                 ....*....|....*....|....*....
gi 515634100 227 HHMlGWAEQHPQAFSERLRILSDGEEITL 255
Cdd:PRK02113 225 HHI-GLHADVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 60-188 2.83e-13

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: 66.56  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   60 CRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDKISVmspddPLGCDDLYKHPGILDFSQRAQAFKS--FDWQ------- 130
Cdd:pfam12706  22 GRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYA-----PLGVLAHLRRNFPYLFLLEHYGVRVheIDWGesftvgd 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634100  131 -GITITPLPLNHSK---------LCLGYCLEFDGKRLAYLTDTVGLPKQTERWLKefPVDWLITDCNY 188
Cdd:pfam12706  97 gGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLG--GADLLLLDGGA 162
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 38-165 1.83e-04

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: 41.00  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100    38 SSAYLEHNGKFLLLDANAPD------LMCRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDKISVMSPDDPLGCDDLYKH 111
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaedllaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515634100   112 PGILDFSQRAQAFK------SFDWQGITITPLPL-NHSKLCLgyCLEFDGKRLAYLTDTVG 165
Cdd:smart00849  81 GELGAEAEPAPPDRtlkdgdELDLGGGELEVIHTpGHTPGSI--VLYLPEGKILFTGDLLF 139
 
Name Accession Description Interval E-value
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-186 2.79e-103

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: 297.61  E-value: 2.79e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAALEDPNLRREKSSAYLEHNGKFLLLDANAPDLMCRFPAGSIDKILLTHYHMDHV 80
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  81 HSLFDLRWGAGDKISVMSPDDPLGCDDLYKHPGILDFSQRAQAFKSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYL 160
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 515634100 161 TDTVGLPKQTERWLKEFPVDWLITDC 186
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 14-238 4.73e-98

phosphonate metabolism protein PhnP; This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in E. coli and is a member of the metallo-beta-lactamase superfamily (pfam00753). As defined by this model, all instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP.


Pssm-ID: 163212  Cd Length: 238  Bit Score: 286.23  E-value: 4.73e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   14 VPVYGCDCSVCGAALEDPNLRREKSSAYLEHNGKFLLLDANAPDLMCRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDK 93
Cdd:TIGR03307   4 VPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGVGEP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   94 ISVMSPDDPLGCDDLYKHPGILDFSQRAQAFKSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYLTDTVGLPKQTERW 173
Cdd:TIGR03307  84 IPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDTEAF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634100  174 LKEFPVDWLITDCNYPPIEDPQArtslNHNDFHHILDIDETCRPTNLGLIHVSHHMLGWAEQHPQ 238
Cdd:TIGR03307 164 LKNHPLDVLILDCSHPPQSDAPR----NHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPD 224
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-255 1.35e-46

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 155.82  E-value: 1.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCgaALEDPNLRREKSSAYLEHNGKFLLLDAnAPDL---MCRFPAG--SIDKILLTHY 75
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDA-GPDLreqLLRLGLDpsKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  76 HMDHVHSLFDLRWGAGDK-ISVMSPDDPLgcDDL--------YKHPGILDFsQRAQAFKSFDWQGITITPLPLNHSKL-C 145
Cdd:COG1235   78 HADHIAGLDDLRPRYGPNpIPVYATPGTL--EALerrfpylfAPYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 146 LGYCLEFDGKRLAYLTDTVGLPKQTERWLKEfpVDWLITDCNYPPiEDPqartslNHNDFHHILDIDETCRPTNLGLIHV 225
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDD-PEP------GHLSNEEALELLARLGPKRLVLTHL 225

                        250       260       270
                 ....*....|....*....|....*....|....
gi 515634100 226 SH----HMLGWAEQHPQAFSERLRILSDGEEITL 255
Cdd:COG1235  226 SPdnndHELDYDELEAALLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-186 1.37e-34

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: 122.97  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCgaALEDPNLRREKSSAYLEHNGKFLLLDAnAPDL---MCRFPAGSIDKILLTHYHM 77
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVC--DSSDPKNRRLRSSILIETGGKNILIDT-GPDFrqqALRAGIRKLDAVLLTHAHA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  78 DHVHSLFDLR---WGAGDKISV-MSPD---------DPLGCDDLYKHPGILDFsQRAQAFKSFDWQGITITPLPLNHSKL 144
Cdd:cd16279   78 DHIHGLDDLRpfnRLQQRPIPVyASEEtlddlkrrfPYFFAATGGGGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHGKL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515634100 145 -CLGYCLEfdgkRLAYLTDTVGLPKQTERWLKEfpVDWLITDC 186
Cdd:cd16279  157 pSLGFRFG----DFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-255 1.47e-26

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 103.35  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAmvpvygcdcsvcgaaledPNLRREKSSAYLEHNGKFLLLDA--NAPDLMCRF--PAGSIDKILLTHYH 76
Cdd:COG1234    1 MKLTFLGTGGAV------------------PTPGRATSSYLLEAGGERLLIDCgeGTQRQLLRAglDPRDIDAIFITHLH 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  77 MDHV---HSLFDLRWGAGDKisvmspdDPLgcdDLYKHPGILDFSQRAQAF-----------------KSFDWQGITITP 136
Cdd:COG1234   63 GDHIaglPGLLSTRSLAGRE-------KPL---TIYGPPGTKEFLEALLKAsgtdldfplefheiepgEVFEIGGFTVTA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 137 LPLNHSKLCLGYCLEFDGKRLAYLTDTvGLPKQTERWLKEfpVDWLITDCNYPPIEDPQARTSLnHNDFHHILDIDETCR 216
Cdd:COG1234  133 FPLDHPVPAYGYRFEEPGRSLVYSGDT-RPCEALVELAKG--ADLLIHEATFLDEEAELAKETG-HSTAKEAAELAAEAG 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 515634100 217 PTNLGLIHVSHHMLGWAEQHPQA---FSERLRILSDGEEITL 255
Cdd:COG1234  209 VKRLVLTHFSPRYDDPEELLAEAravFPGPVELAEDGMVIEL 250
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-255 3.25e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 91.77  E-value: 3.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAAleDPNLRREKSSAYLEHNGKFLLLDAnAPDL---MCRFPAGSIDKILLTHYHM 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDC-GPDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  78 DHVHSLFDLR-WGAGDKISVMSPDDPLG--------CDDLYKHPGILDFS-QRAQAFKSFDWQGITITPLPLNHSKL-CL 146
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLpIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 147 GYCLefdgKRLAYLTDTVGLPKQTERWLKEfpVDWLITDCnYPPIEDPqartslNHNDFHHILDIDETCRPTNLGLIHVS 226
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNA-LRIAPHP------THQSLEEALENIKRIGAKETYLIHMS 224

                        250       260
                 ....*....|....*....|....*....
gi 515634100 227 HHMlGWAEQHPQAFSERLRILSDGEEITL 255
Cdd:PRK02113 225 HHI-GLHADVEKELPPHVHFAYDGLEIIF 252
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 31-186 1.68e-16

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 74.99  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  31 PNLRREKSSAYLEHNGKFLLLDA--NAPD--LMCRFPAGSIDKILLTHYHMDHV---HSLFDLRWGAGdkisvmsPDDPL 103
Cdd:cd16272   11 PSLTRNTSSYLLETGGTRILLDCgeGTVYrlLKAGVDPDKLDAIFLSHFHLDHIgglPTLLFARRYGG-------RKKPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 104 gcdDLYKHPGILDFSQRAQAFKSFDWQ--------------------GITITPLPLNHSKLCLGYCLEFDGKRLAYLTDT 163
Cdd:cd16272   84 ---TIYGPKGIKEFLEKLLNFPVEILPlgfpleieeleeggevlelgDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDT 160

                        170       180
                 ....*....|....*....|...
gi 515634100 164 vGLPKQTERWLKEfpVDWLITDC 186
Cdd:cd16272  161 -GPCENLVELAKG--ADLLIHEC 180
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 42-195 4.84e-15

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: 71.76  E-value: 4.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  42 LEHNGKFLLLDA--------NApdLMCRFPAGSIDkILLTHYHMDHVH------SLFDlrwgAGDKISVMSPDDPLGC-- 105
Cdd:cd07715   28 VRAGGELLILDAgtgirelgNE--LMKEGPPGEAH-LLLSHTHWDHIQgfpffaPAYD----PGNRIHIYGPHKDGGSle 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 106 ---DDLYKHP----GILDFSQRAQAF-----KSFDWQGITITPLPLNHSKLCLGYCLEFDGKRLAYLTDT---VGLPKQT 170
Cdd:cd07715  101 evlRRQMSPPyfpvPLEELLAAIEFHdlepgEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDTehyPDDGESD 180

                        170       180
                 ....*....|....*....|....*..
gi 515634100 171 ERWLkEF--PVDWLITDCNYPPIEDPQ 195
Cdd:cd07715  181 EALL-EFarGADLLIHDAQYTDEEYPS 206
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 60-188 2.83e-13

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: 66.56  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   60 CRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDKISVmspddPLGCDDLYKHPGILDFSQRAQAFKS--FDWQ------- 130
Cdd:pfam12706  22 GRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYA-----PLGVLAHLRRNFPYLFLLEHYGVRVheIDWGesftvgd 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634100  131 -GITITPLPLNHSK---------LCLGYCLEFDGKRLAYLTDTVGLPKQTERWLKefPVDWLITDCNY 188
Cdd:pfam12706  97 gGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLG--GADLLLLDGGA 162
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-163 3.98e-13

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: 66.70  E-value: 3.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   3 LTMLGTanSAMVPvygcdcsvcgaaledpNLRREKSSAYLEHNGKFLLLDanapdlmC-----------RFPAGSIDKIL 71
Cdd:cd07717    1 LTFLGT--GSAVP----------------TPERNLSSIALRLEGELWLFD-------CgegtqrqllraGLSPSKIDRIF 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  72 LTHYHMDHVHSLFDLrwgagdkISVMS---PDDPLgcdDLYKHPGILDFSQRAQAF-------------------KSFDW 129
Cdd:cd07717   56 ITHLHGDHILGLPGL-------LSTMSllgRTEPL---TIYGPKGLKEFLETLLRLsasrlpypievhelepdpgLVFED 125

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515634100 130 QGITITPLPLNHSKLCLGYCLEFdGKRLAYLTDT 163
Cdd:cd07717  126 DGFTVTAFPLDHRVPCFGYRFEE-GRKIAYLGDT 158
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-164 3.94e-08

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: 51.75  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   2 KLTMLGTAnsamVPVygcdcsvcgaaledPNLRREKSSAYLEHNGKFLLLDA---------NApdlmcRFPAGSIDKILL 72
Cdd:cd07719    1 RVTLLGTG----GPI--------------PDPDRAGPSTLVVVGGRVYLVDAgsgvvrrlaQA-----GLPLGDLDAVFL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  73 THYHMDHVHSLFDL---RWGAGDK------------------ISVMSPDDPLGC---DDLYKHPGIL----DFSQRAQAF 124
Cdd:cd07719   58 THLHSDHVADLPALlltAWLAGRKtplpvygppgtralvdglLAAYALDIDYRArigDEGRPDPGALvevhEIAAGGVVY 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515634100 125 KSfdwQGITITPLPLNHS--KLCLGYCLEFDGKRLAYLTDTV 164
Cdd:cd07719  138 ED---DGVKVTAFLVDHGpvPPALAYRFDTPGRSVVFSGDTG 176
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 38-163 4.76e-08

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 51.29  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  38 SSAYL-EHNGKFLLLDAN---APDLMCRFPAGSIDKILLTHYHMDHVHSLFDL----RWGAGDKisvmsPDDPLgcdDLY 109
Cdd:cd07716   18 CSGYLlEADGFRILLDCGsgvLSRLQRYIDPEDLDAVVLSHLHPDHCADLGVLqyarRYHPRGA-----RKPPL---PLY 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515634100 110 KHPGILDFSQRAQAFK-SFDWQ-----------GITITPLPLNHSKLCLGYCLEFDGKRLAYLTDT 163
Cdd:cd07716   90 GPAGPAERLAALYGLEdVFDFHpiepgepleigPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDT 155
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 38-191 1.63e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 50.69  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  38 SSAYLEHNGKFLLLD--------ANAPDLMCRFPAGSIDKILLTHYHMDHVHSLFDLRWgAGDKISVMSpddPLGCDDLY 109
Cdd:COG2220   12 ATFLIETGGKRILIDpvfsgrasPVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAL-KRTGATVVA---PLGVAAWL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 110 KHPGILDFsQRAQAFKSFDWQGITITPLPLNHS--------KLCLGYCLEFDGKRLAYLTDTvGLPKQTERWLKEFPVDW 181
Cdd:COG2220   88 RAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpdrngGLWVGFVIETDGKTIYHAGDT-GYFPEMKEIGERFPIDV 165

                        170
                 ....*....|
gi 515634100 182 LITDCNYPPI 191
Cdd:COG2220  166 ALLPIGAYPF 175
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 24-156 1.99e-06

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: 47.98  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   24 CGAALedPNLRREKSSAYLEHNGKFLLLDA--NAPDLMCRFPAG--SIDKILLTHYHMDHVHSLFDLrwgagdkISVMSP 99
Cdd:TIGR02651   7 TGGGV--PTKERNLPSIALKLNGELWLFDCgeGTQRQMLRSGISpmKIDRIFITHLHGDHILGLPGL-------LSTMSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634100  100 D---DPLgcdDLYKHPGILDFSQRA-QAFKS-----------------FDWQGITITPLPLNHSKLCLGYCLEFDGKR 156
Cdd:TIGR02651  78 QgrkEPL---TIYGPPGIKEFIETSlRVSYTylnypikiheieegglvFEDDGFKVEAFPLDHSIPSLGYRFEEKDRP 152
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-224 5.09e-06

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 46.03  E-value: 5.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  41 YLEHNGKFLLLDANAPDL--MCRFP--AGSIDKILLTHYHMDH---VHSLFDLRWGAGDKI--SVMSPDDPLGCDD---L 108
Cdd:cd07741   24 WIELNGKNIHIDPGPGALvrMCRPKldPTKLDAIILSHRHLDHsndANVLIEAMTEGGFKKrgTLLAPEDALNGEPvvlL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100 109 YKHPGILDFSQRAQAFKSFDWQGITITPLPLNHS-KLCLGYCLEFDGKRLAYLTDTvglpKQTERWLKEFP-VDWLITDC 186
Cdd:cd07741  104 YYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSdPTTYGFIFRTSDKKIGYISDT----RYFEELIEYYSnCDVLIINV 179

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515634100 187 NYppiedPQARTSLNHNDFHHILDIDETCRPTNLGLIH 224
Cdd:cd07741  180 TR-----PRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
38-165 2.46e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 43.90  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   38 SSAYL-EHNGKFLLLDA-NAPDLMC-------RFPAGSIDKILLTHYHMDHVHSLFDLR------WGAGDKISVMSPDDP 102
Cdd:pfam00753   6 VNSYLiEGGGGAVLIDTgGSAEAALllllaalGLGPKDIDAVILTHGHFDHIGGLGELAeatdvpVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  103 LGCDDLYK-------HPGILDFSQRAQAFKSFDWQGITITPLPLNHSklcLGYCLEFDGKRLAYLTDTVG 165
Cdd:pfam00753  86 LGLAASRLglpgppvVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGP---GHVVVYYGGGKVLFTGDLLF 152
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
39-79 3.06e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 44.10  E-value: 3.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 515634100  39 SAYLEHNGKFLLLDANAPDLMCR------FPAGSIDKILLTHYHMDH 79
Cdd:COG1237   24 SALIETEGKRILFDTGQSDVLLKnaeklgIDLSDIDAVVLSHGHYDH 70
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 39-80 5.26e-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: 5.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515634100  39 SAYL-EHNGKFLLLDA------------NAPDLMcrFPAGSIDKILLTHYHMDHV 80
Cdd:cd16295   13 SCYLlETGGKRILLDCglfqggkeleelNNEPFP--FDPKEIDAVILTHAHLDHS 65
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 38-165 1.83e-04

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: 41.00  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100    38 SSAYLEHNGKFLLLDANAPD------LMCRFPAGSIDKILLTHYHMDHVHSLFDLRWGAGDKISVMSPDDPLGCDDLYKH 111
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaedllaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515634100   112 PGILDFSQRAQAFK------SFDWQGITITPLPL-NHSKLCLgyCLEFDGKRLAYLTDTVG 165
Cdd:smart00849  81 GELGAEAEPAPPDRtlkdgdELDLGGGELEVIHTpGHTPGSI--VLYLPEGKILFTGDLLF 139
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-121 2.19e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 41.70  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTanSAMVPvygcdcsvcgaaleDPNlrREKSSAYLEHNGKFLLLDanapdlmC-----------RFPAGSIDK 69
Cdd:PRK00055   2 MELTFLGT--GSGVP--------------TPT--RNVSSILLRLGGELFLFD-------CgegtqrqllktGIKPRKIDK 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515634100  70 ILLTHYHMDHVHSLFDL---RWGAGDKisvmspdDPLgcdDLYKHPGILDFSQRA 121
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLlstRSLSGRT-------EPL---TIYGPKGIKEFVETL 101
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-184 3.09e-04

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 40.67  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  66 SIDKILLTHYHMDHvhslfdlrWGAgdkISVMSPDDPL----GCDDLYK------------HPGILDFSQRaqafKSFDW 129
Cdd:cd07732   75 SVDAVLLSHAHLDH--------YGL---LNYLRPDIPVymgeATKRILKallpffgegdpvPRNIRVFESG----KSFTI 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515634100 130 QGITITPLPLNHSKL--ClGYCLEFDGKRLAYLTD--TVGL-PKQTERWLKEFP--VDWLIT 184
Cdd:cd07732  140 GDFTVTPYLVDHSAPgaY-AFLIEAPGKRIFYTGDfrFHGRkPELTEAFVEKAPknIDVLLM 200
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 38-197 3.13e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 41.33  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  38 SSAYLEHNGKFLLLDA---------NAPDLmcRFPAGSIDKILLTHYHMDH---VHSLF------------------DLR 87
Cdd:COG1236   15 SCYLLETGGTRILIDCglfqggkerNWPPF--PFRPSDVDAVVLTHAHLDHsgaLPLLVkegfrgpiyatpatadlaRIL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  88 WGAGDKISVMSPDDPLgcddLYKHPGILDFSQRAQAF---KSFDWQGITITPLPLNHsklCLG---YCLEFDGKRLAYLT 161
Cdd:COG1236   93 LGDSAKIQEEEAEAEP----LYTEEDAERALELFQTVdygEPFEIGGVRVTFHPAGH---ILGsaqVELEVGGKRIVFSG 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515634100 162 DtVGLPKQteRWLKEF----PVDWLIT-----DCNYPPIEDPQAR 197
Cdd:COG1236  166 D-YGREDD--PLLAPPepvpPADVLITestygDRLHPPREEVEAE 207
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 1-139 4.02e-04

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. 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: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 40.68  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100   1 MKLTMLGTANSAMVPVYGCDCSVCGAALE--DPNLRREKSSAYLEHNGK-FLLLDAnAPDL---MCRFPAGS-------- 66
Cdd:cd16274    1 MRIKVLGSAAGGGFPQWNCNCPNCALARAgdGRATARTQSSIAVSADGEnWVLINA-SPDIrqqIEATPELQprpglrdt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  67 -IDKILLTHYHMDHVHSLFDLRWGAGDKISVMSP-----DDPLGCDDLYKHPGILdfsQR-----AQAFKSFDWQGITIT 135
Cdd:cd16274   80 pIAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPvledlTTNFPFFVLLHAYGGV---RRhrilpGEPFTLAGCPGLTVT 156


                 ....
gi 515634100 136 PLPL 139
Cdd:cd16274  157 PFPV 160
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-163 5.48e-04

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: 39.93  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  66 SIDKILLTHYHMDH----VHSLFDLRWGAG--DKISVMSPddplgcddlykhPGILDFSQRA--QAF-------KSFDWQ 130
Cdd:cd07740   49 AIDAIFITHLHGDHfgglPFFLLDAQFVAKrtRPLTIAGP------------PGLRERLRRAmeALFpgsskvpRRFDLE 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515634100 131 -------------GITITPLPLNHSKLCLGYCLEFD--GKRLAYLTDT 163
Cdd:cd07740  117 vielepgepttlgGVTVTAFPVVHPSGALPLALRLEaaGRVLAYSGDT 164
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 40-90 1.33e-03

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 38.74  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515634100  40 AYL-EHNGKFLLLDANAP---DLMCR------FPAGSIDKILLTHYHMDHVHSLFDLR--WGA 90
Cdd:cd07721   13 AYLiEDDDGLTLIDTGLPgsaKRILKalrelgLSPKDIRRILLTHGHIDHIGSLAALKeaPGA 75
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 67-101 2.76e-03

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: 37.65  E-value: 2.76e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515634100  67 IDKILLTHYHMDHVHSLFDLRWGAGDKIsVMSPDD 101
Cdd:cd06262   46 IKAILLTHGHFDHIGGLAELKEAPGAPV-YIHEAD 79
PRK04286 PRK04286
hypothetical protein; Provisional
 68-185 3.10e-03

hypothetical protein; Provisional


Pssm-ID: 235270  Cd Length: 298  Bit Score: 38.03  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  68 DKILLTHYHMDHvHSLFDlrwgaGDKISVMSPDDPlgcDDLY-------KHPG-ILDFSQ--RAQAF------------- 124
Cdd:PRK04286  67 DVITISHYHYDH-HTPFY-----EDPYELSDEEIP---KEIYkgkivliKDPTeNINWSQrrRAPRFlkavkdiakkiey 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515634100 125 ---KSFDWQGITIT---PLPlnH----SKlcLGYCLEF---DGK-RLAYLTDTVGLPK-QTERWLKEFPVDWLITD 185
Cdd:PRK04286 138 adgKTFRFGGTTIEfspPVP--HgadgSK--LGYVIMVrisDGDeSFVFASDVQGPLNdEAVEFILEKKPDVVIIG 209
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 41-112 4.79e-03

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: 37.13  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  41 YLEHNGK-FLLLDA---------NAPDLMCRFPAGSIDKILLTHYHMDHV---HSLFDLRWGAGDKISVMSPDDPLGCDD 107
Cdd:cd07722   21 YLVGTGKrRILIDTgegrpsyipLLKSVLDSEGNATISDILLTHWHHDHVgglPDVLDLLRGPSPRVYKFPRPEEDEDPD 100


                 ....*
gi 515634100 108 LYKHP 112
Cdd:cd07722  101 EDGGD 105
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 64-162 7.16e-03

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: 36.54  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634100  64 AGSIDKILLTHYHMDHV--HSLF-------------------------DLRWGAGDKISVMSPDDPLGCDDLYKHPGILD 116
Cdd:cd07734   47 PPEIDAILISHFHLDHCgaLPYLfrgfifrgpiyathptvalgrllleDYVKSAERIGQDQSLYTPEDIEEALKHIVPLG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515634100 117 FSQRAQAFKsfdwqGITITPLPLNHsklCLG---YCLEFDGKRLAYLTD 162
Cdd:cd07734  127 YGQSIDLFP-----ALSLTAYNAGH---VLGaamWEIQIYGEKLVYTGD 167
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 39-80 8.98e-03

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: 36.83  E-value: 8.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515634100  39 SAYLEHNGKFLLLDANAPDLMCR------FPAGSIDKILLTHYHMDHV 80
Cdd:cd07713   22 SLLIETEGKKILFDTGQSGVLLHnakklgIDLSDIDAVVLSHGHYDHT 69
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 39-80 9.99e-03

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: 36.37  E-value: 9.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515634100  39 SAYL-EHNGKFLLLDANAPDLMC----RFPA---------GSIDKILLTHYHMDHV 80
Cdd:cd07720   50 NAFLvRTGGRLILVDTGAGGLFGptagKLLAnlaaagidpEDIDDVLLTHLHPDHI 105
 
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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