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Conserved domains on  [gi|445982071|ref|WP_000059926|]
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MULTISPECIES: phosphonate metabolism protein PhnP [Enterobacteriaceae]

Protein Classification

phosphoribosyl 1,2-cyclic phosphate phosphodiesterase( domain architecture ID 17621284)

phosphoribosyl 1,2-cyclic phosphate phosphodiesterase catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 4.63e-155

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: 430.68  E-value: 4.63e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   13 AQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGRHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   93 GDVIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445982071  173 LKFLLNNHPQVMVIDCSHPPRADAPRNHCDLNTVLALNQVIRSPQVILTHISHQFDAWLMENA-LPSGFEVGFDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 4.63e-155

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: 430.68  E-value: 4.63e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   13 AQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGRHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   93 GDVIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445982071  173 LKFLLNNHPQVMVIDCSHPPRADAPRNHCDLNTVLALNQVIRSPQVILTHISHQFDAWLMENA-LPSGFEVGFDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 13-188 6.28e-112

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: 319.18  E-value: 6.28e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  13 AQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGRHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:cd07736   11 AGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHVQGLFHLRWGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  93 GDVIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:cd07736   91 GDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYLTDTLGLPEET 170

                        170
                 ....*....|....*.
gi 445982071 173 LKFLLNNHPQVMVIDC 188
Cdd:cd07736  171 LEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-249 3.09e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.48  E-value: 3.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  13 AQGVPAWGCECAACARARrsPQYRRQPCSGVVKFNDAITLIDAG----RHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPL 88
Cdd:COG1235   11 SGGVPQIGCDCPVCASTD--PRYGRTRSSILVEADGTRLLIDAGpdlrEQLLRLGLDPSKIDAILLTHEHADHIAGLDDL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  89 RWGVGDV-IPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLLETAHSRVA 160
Cdd:COG1235   89 RPRYGPNpIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVGYRIEDGGKKLA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 161 WLSDTAGLPEKTLKFLLNnhPQVMVIDCSHPPraDAPrNHCDLNTVLALNQVIRSPQVILTHIS-----HQFDAWLMENA 235
Cdd:COG1235  168 YATDTGYIPEEVLELLRG--ADLLILDATYDD--PEP-GHLSNEEALELLARLGPKRLVLTHLSpdnndHELDYDELEAA 242

                        250
                 ....*....|....*
gi 445982071 236 L-PSGFEVGFDGMEI 249
Cdd:COG1235  243 LlPAGVEVAYDGMEI 257
PRK02113 PRK02113
MBL fold metallo-hydrolase;
15-249 2.50e-19

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 84.06  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  15 GVPAWGCECAACARArrSPQYRRQPCSGVVKFNDAITLIDAG---RHDLTdRWSPGSFQQFLLTHYHMDHVQGLFPLR-- 89
Cdd:PRK02113  13 GVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDCGpdfREQML-RLPFGKIDAVLITHEHYDHVGGLDDLRpf 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  90 -WgVGDViPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHSKLT-FGYLLeta 155
Cdd:PRK02113  90 cR-FGEV-PIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiLGYRI--- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 156 hSRVAWLSDTAGLPEKTLKFLLNnhPQVMVIDCSHPpradAPRN-HCDLNTVLALNQVIRSPQVILTHISHqfDAWL--- 231
Cdd:PRK02113 162 -GKMAYITDMLTMPEEEYEQLQG--IDVLVMNALRI----APHPtHQSLEEALENIKRIGAKETYLIHMSH--HIGLhad 232

                        250
                 ....*....|....*...
gi 445982071 232 MENALPSGFEVGFDGMEI 249
Cdd:PRK02113 233 VEKELPPHVHFAYDGLEI 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 6.23e-09

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: 54.24  E-value: 6.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   73 LLTHYHMDHVQGLFPLRWGVGdvIPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLREGRP--RPLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  146 ---------LTFGYLLETAHSRVAWLSDTAGLPEKTLKFLLNnhPQVMVID-CSHPPRADAPRNHCDLNTVLALNQVIRS 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 445982071  216 PQVILTHI 223
Cdd:pfam12706 189 RRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 1.08e-03

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 38.69  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071    41 SGVVKFNDAITLIDAGRHDLTD------RWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGdvIPVYGPPDEQG--CDDLFK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDllaelkKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 445982071   113 HPGLLDFSHTVEPFVVFD 130
Cdd:smart00849  80 LGELGAEAEPAPPDRTLK 97
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 4.63e-155

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: 430.68  E-value: 4.63e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   13 AQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGRHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   93 GDVIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445982071  173 LKFLLNNHPQVMVIDCSHPPRADAPRNHCDLNTVLALNQVIRSPQVILTHISHQFDAWLMENA-LPSGFEVGFDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 13-188 6.28e-112

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: 319.18  E-value: 6.28e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  13 AQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGRHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:cd07736   11 AGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHVQGLFHLRWGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  93 GDVIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:cd07736   91 GDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYLTDTLGLPEET 170

                        170
                 ....*....|....*.
gi 445982071 173 LKFLLNNHPQVMVIDC 188
Cdd:cd07736  171 LEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-249 3.09e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.48  E-value: 3.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  13 AQGVPAWGCECAACARARrsPQYRRQPCSGVVKFNDAITLIDAG----RHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPL 88
Cdd:COG1235   11 SGGVPQIGCDCPVCASTD--PRYGRTRSSILVEADGTRLLIDAGpdlrEQLLRLGLDPSKIDAILLTHEHADHIAGLDDL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  89 RWGVGDV-IPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLLETAHSRVA 160
Cdd:COG1235   89 RPRYGPNpIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVGYRIEDGGKKLA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 161 WLSDTAGLPEKTLKFLLNnhPQVMVIDCSHPPraDAPrNHCDLNTVLALNQVIRSPQVILTHIS-----HQFDAWLMENA 235
Cdd:COG1235  168 YATDTGYIPEEVLELLRG--ADLLILDATYDD--PEP-GHLSNEEALELLARLGPKRLVLTHLSpdnndHELDYDELEAA 242

                        250
                 ....*....|....*
gi 445982071 236 L-PSGFEVGFDGMEI 249
Cdd:COG1235  243 LlPAGVEVAYDGMEI 257
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 13-188 8.43e-25

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: 97.16  E-value: 8.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  13 AQGVPAWGCECAACARArrSPQYRRQPCSGVVKFNDAITLIDAG---RHDLTdRWSPGSFQQFLLTHYHMDHVQG---LF 86
Cdd:cd16279   11 SSGVPVIGCDCGVCDSS--DPKNRRLRSSILIETGGKNILIDTGpdfRQQAL-RAGIRKLDAVLLTHAHADHIHGlddLR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  87 PLRWGVGDVIPVYGPPD-----EQGCDDLFK-----HPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLLEta 155
Cdd:cd16279   88 PFNRLQQRPIPVYASEEtlddlKRRFPYFFAatgggGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHGKLpSLGFRFG-- 164

                        170       180       190
                 ....*....|....*....|....*....|...
gi 445982071 156 hsRVAWLSDTAGLPEKTLKFLLNnhPQVMVIDC 188
Cdd:cd16279  165 --DFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
34-249 1.44e-21

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 89.87  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  34 QYRRQPCSgVVKFNDAITLIDAGrhdltdrwsPGSFQQFL-------------LTHYHMDHVQGLFPL---RW--GVGDV 95
Cdd:COG1234   15 PGRATSSY-LLEAGGERLLIDCG---------EGTQRQLLragldprdidaifITHLHGDHIAGLPGLlstRSlaGREKP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  96 IPVYGPPD-EQGCDDLFK-HPGLLDFS---HTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTaGLPE 170
Cdd:COG1234   85 LTIYGPPGtKEFLEALLKaSGTDLDFPlefHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDT-RPCE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 171 KTLKFLLNnhPQVMVIDCSHPPRADA---PRNHCdlnTVLALNQVIRS---PQVILTHISHQFD---AWLME--NALPSG 239
Cdd:COG1234  164 ALVELAKG--ADLLIHEATFLDEEAElakETGHS---TAKEAAELAAEagvKRLVLTHFSPRYDdpeELLAEarAVFPGP 238

                        250
                 ....*....|
gi 445982071 240 FEVGFDGMEI 249
Cdd:COG1234  239 VELAEDGMVI 248
PRK02113 PRK02113
MBL fold metallo-hydrolase;
15-249 2.50e-19

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 84.06  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  15 GVPAWGCECAACARArrSPQYRRQPCSGVVKFNDAITLIDAG---RHDLTdRWSPGSFQQFLLTHYHMDHVQGLFPLR-- 89
Cdd:PRK02113  13 GVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDCGpdfREQML-RLPFGKIDAVLITHEHYDHVGGLDDLRpf 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  90 -WgVGDViPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHSKLT-FGYLLeta 155
Cdd:PRK02113  90 cR-FGEV-PIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiLGYRI--- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 156 hSRVAWLSDTAGLPEKTLKFLLNnhPQVMVIDCSHPpradAPRN-HCDLNTVLALNQVIRSPQVILTHISHqfDAWL--- 231
Cdd:PRK02113 162 -GKMAYITDMLTMPEEEYEQLQG--IDVLVMNALRI----APHPtHQSLEEALENIKRIGAKETYLIHMSH--HIGLhad 232

                        250
                 ....*....|....*...
gi 445982071 232 MENALPSGFEVGFDGMEI 249
Cdd:PRK02113 233 VEKELPPHVHFAYDGLEI 250
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 33-249 2.03e-12

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: 64.78  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  33 PQYRRQPCSGVVKFNDAITLIDAG--------RHdltdRWSPGSFQQFLLTHYHMDHVQGLFPL-----RWGVGDVIPVY 99
Cdd:cd07717   11 PTPERNLSSIALRLEGELWLFDCGegtqrqllRA----GLSPSKIDRIFITHLHGDHILGLPGLlstmsLLGRTEPLTIY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 100 GPPdeqGCDDLFKHpgLLDFSHTVEPF------------VVFDLQGLQVTPLPLNHSKLTFGYLLETAHSrVAWLSDTAg 167
Cdd:cd07717   87 GPK---GLKEFLET--LLRLSASRLPYpievhelepdpgLVFEDDGFTVTAFPLDHRVPCFGYRFEEGRK-IAYLGDTR- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071 168 LPEKTLKFLLNnhPQVMVIDC----SHPPRAdAPRNHCdlnTV-----LALNqvIRSPQVILTHISHQFDAW--LMENAL 236
Cdd:cd07717  160 PCEGLVELAKG--ADLLIHEAtfldDDAEKA-KETGHS---TAkqaaeIAKK--AGVKKLVLTHFSARYKDPeeLLKEAR 231

                        250
                 ....*....|....*.
gi 445982071 237 pSGF---EVGFDGMEI 249
Cdd:cd07717  232 -AVFpntILAEDFMTI 246
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 33-166 1.51e-11

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: 61.13  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  33 PQYRRQPCSGVVKFNDAITLIDAGRHDLTDRW----SPGSFQQFLLTHYHMDHVQGLFPLRW-----GVGDVIPVYGPPD 103
Cdd:cd16272   11 PSLTRNTSSYLLETGGTRILLDCGEGTVYRLLkagvDPDKLDAIFLSHFHLDHIGGLPTLLFarrygGRKKPLTIYGPKG 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445982071 104 -EQGCDDLFKHPGL-------LDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTA 166
Cdd:cd16272   91 iKEFLEKLLNFPVEilplgfpLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 36-166 2.55e-11

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: 60.99  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  36 RRQPCSGVVkFNDAITLIDAGRhdltdrwspGSFQQF-------------LLTHYHMDHVQGLFPL---RWGVG--DVIP 97
Cdd:cd07719   16 RAGPSTLVV-VGGRVYLVDAGS---------GVVRRLaqaglplgdldavFLTHLHSDHVADLPALlltAWLAGrkTPLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  98 VYGPP--------------DEQGCDDLFKHPGLLDFSHTVE------PFVVFDLQGLQVTPLPLNHS--KLTFGYLLETA 155
Cdd:cd07719   86 VYGPPgtralvdgllaayaLDIDYRARIGDEGRPDPGALVEvheiaaGGVVYEDDGVKVTAFLVDHGpvPPALAYRFDTP 165

                        170
                 ....*....|.
gi 445982071 156 HSRVAWLSDTA 166
Cdd:cd07719  166 GRSVVFSGDTG 176
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 52-165 1.48e-09

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: 56.35  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  52 LIDAGR--HDLTDRWSPGSFQQ---FLLTHYHMDHVQGL--F-PLrWGVGDVIPVYGPPDEQGC-----DDLFKHP---- 114
Cdd:cd07715   36 ILDAGTgiRELGNELMKEGPPGeahLLLSHTHWDHIQGFpfFaPA-YDPGNRIHIYGPHKDGGSleevlRRQMSPPyfpv 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445982071 115 GLLDFS-----HTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDT 165
Cdd:cd07715  115 PLEELLaaiefHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDT 170
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 6.23e-09

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: 54.24  E-value: 6.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   73 LLTHYHMDHVQGLFPLRWGVGdvIPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLREGRP--RPLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  146 ---------LTFGYLLETAHSRVAWLSDTAGLPEKTLKFLLNnhPQVMVID-CSHPPRADAPRNHCDLNTVLALNQVIRS 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 445982071  216 PQVILTHI 223
Cdd:pfam12706 189 RRKVLIHI 196
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 33-153 1.66e-08

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: 54.15  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071   33 PQYRRQPCSGVVKFNDAITLIDAG----RHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPL-----RWGVGDVIPVYGPPd 103
Cdd:TIGR02651  12 PTKERNLPSIALKLNGELWLFDCGegtqRQMLRSGISPMKIDRIFITHLHGDHILGLPGLlstmsFQGRKEPLTIYGPP- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445982071  104 eqGCDDLFKHpgLLDFSHTVEPF-----------VVFDLQGLQVTPLPLNHSKLTFGYLLE 153
Cdd:TIGR02651  91 --GIKEFIET--SLRVSYTYLNYpikiheieeggLVFEDDGFKVEAFPLDHSIPSLGYRFE 147
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 38-166 4.28e-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: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  38 QPCSG-VVKFNDAITLIDAGrhdltdrwsPGSF---QQF---------LLTHYHMDHVQGLFPLR--------WGVGDVI 96
Cdd:cd07716   16 GACSGyLLEADGFRILLDCG---------SGVLsrlQRYidpedldavVLSHLHPDHCADLGVLQyarryhprGARKPPL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445982071  97 PVYGPPDEQGC-DDLFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTA 166
Cdd:cd07716   87 PLYGPAGPAERlAALYGLEDVFDF-HPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTG 156
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-222 1.97e-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: 47.18  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  34 QYRRqpcSG--VVKFNDAITLIDAGrhdltdrwsPGSFQQ-------------FLLTHYHMDH-----------VQGLFP 87
Cdd:cd07741   16 QLRA---SGgiWIELNGKNIHIDPG---------PGALVRmcrpkldptkldaIILSHRHLDHsndanvlieamTEGGFK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  88 LRwGVgdvipVYGPPD---EQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHS-KLTFGYLLETAHSRVAWLS 163
Cdd:cd07741   84 KR-GT-----LLAPEDalnGEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSdPTTYGFIFRTSDKKIGYIS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445982071 164 DTAGLPEKTLKFllnNHPQVMVIDCSHpPRADAPRNHCDLNTVLALNQVIRSPQVILTH 222
Cdd:cd07741  158 DTRYFEELIEYY---SNCDVLIINVTR-PRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-165 2.81e-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: 45.72  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  52 LIDAG--------RHDLTDRwSPGSFQQFLLTHYHMDHVQGLFPL--RWGVgdviPVYGPPDEqgCDDLFKHPGLLDFS- 120
Cdd:cd07733   22 LIDAGlsgrkitgRLAEIGR-DPEDIDAILVTHEHADHIKGLGVLarKYNV----PIYATAGT--LRAMERKVGLIDVDq 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445982071 121 -HTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLLETAHSRVAWLSDT 165
Cdd:cd07733   95 kQIFEPGETFSIGDFDVESFGVSHDAAdPVGYRFEEGGRRFGMLTDL 141
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 48-165 9.52e-06

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: 45.67  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  48 DAITLIDAG------RHDLTDRWSPGSFQQ-----------FLLTHYHMDHVQGLfPLrwGVGDV-------IPVYGPPD 103
Cdd:cd07735   28 DGDILLDAGtgvgalSLEEMFNDILFPSQKaayelyqrirhYLITHAHLDHIAGL-PL--LSPNDggqrgspKTIYGLPE 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445982071 104 EqgCDDLFKH-------PGLLDFSHTVEPFVVFD---------LQGLQVTPLPLNHSKL-TFGYLLETAHSRVAWLSDT 165
Cdd:cd07735  105 T--IDALKKHifnwviwPDFTSIPSGKYPYLRLEpiepeypiaLTGLSVTAFPVSHGVPvSTAFLIRDGGDSFLFFGDT 181
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 15-141 3.10e-05

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: 43.76  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  15 GVPAWGCECAACARARRSP---QYRRQPCSGVVKFNDAITLIDAgrhdltdrwSPGSFQQF------------------- 72
Cdd:cd16274   13 GFPQWNCNCPNCALARAGDgraTARTQSSIAVSADGENWVLINA---------SPDIRQQIeatpelqprpglrdtpiaa 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445982071  73 -LLTHYHMDHVQGLFPLRWGVGdvIPVYGPP-------DEQGCDDLFKHPGLLDFSHTV--EPFVVFDLQGLQVTPLPL 141
Cdd:cd16274   84 vLLTDAEIDHTTGLLSLREGQP--LTVYATApvledltTNFPFFVLLHAYGGVRRHRILpgEPFTLAGCPGLTVTPFPV 160
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 73-170 8.20e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.60  E-value: 8.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  73 LLTHYHMDHV--QGLFPLRwgvGDVIPVYGPPdeqGCDDLFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHS------ 144
Cdd:COG2220   53 LVTHDHYDHLddATLRALK---RTGATVVAPL---GVAAWLRAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpdr 125

                         90       100
                 ....*....|....*....|....*...
gi 445982071 145 --KLTFGYLLETAHSRVAWLSDTAGLPE 170
Cdd:COG2220  126 ngGLWVGFVIETDGKTIYHAGDTGYFPE 153
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 73-130 4.01e-04

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 40.35  E-value: 4.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445982071  73 LLTHYHMDHVQGLFPLRWGVGdvIPVYGPPDEQgcdDLFKHPGLLDFSHTVEPFVVFD 130
Cdd:cd06262   50 LLTHGHFDHIGGLAELKEAPG--APVYIHEADA---ELLEDPELNLAFFGGGPLPPPE 102
PRK00055 PRK00055
ribonuclease Z; Reviewed
 33-102 5.74e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 5.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445982071  33 PQYRRQPCSGVVKFNDAITLIDAG----RHDLTDRWSPGSFQQFLLTHYHMDHVQGLFPL-----RWGVGDVIPVYGPP 102
Cdd:PRK00055  14 PTPTRNVSSILLRLGGELFLFDCGegtqRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLlstrsLSGRTEPLTIYGPK 92
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 1.08e-03

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 38.69  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071    41 SGVVKFNDAITLIDAGRHDLTD------RWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGdvIPVYGPPDEQG--CDDLFK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDllaelkKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 445982071   113 HPGLLDFSHTVEPFVVFD 130
Cdd:smart00849  80 LGELGAEAEPAPPDRTLK 97
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 41-144 3.64e-03

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: 37.75  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  41 SGVVKFNDAITLIDAGRHDLTDRWSPGSFQQF-------LLTHYHMDHVQGLFPLRWGVGdvIPVYGPPDE------QGC 107
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPADAEALLAALAALgldikavLLTHLHPDHVGGLAALAEAFG--APVYAHAAEaealeaPAA 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 445982071 108 DDLFKHPGlLDFSHTVEPFVVFDLQGLQVTPLPLN-HS 144
Cdd:COG0491   95 GALFGREP-VPPDRTLEDGDTLELGGPGLEVIHTPgHT 131
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 73-164 5.64e-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: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445982071  73 LLTHYHMDHVQGLfPLRWGVGDViPVYGPP----------DEqgcddlFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLN 142
Cdd:cd07714   60 FITHGHEDHIGAL-PYLLPELNV-PIYATPltlalikkklEE------FKLIKKVKL-NEIKPGERIKLGDFEVEFFRVT 130

                         90       100
                 ....*....|....*....|...
gi 445982071 143 HSKL-TFGYLLETAHSRVAWLSD 164
Cdd:cd07714  131 HSIPdSVGLAIKTPEGTIVHTGD 153
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 73-113 8.11e-03

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: 35.90  E-value: 8.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 445982071  73 LLTHYHMDHVQGLFPLRWGVGDvIPVYGPPDEQ--GCDDLFKH 113
Cdd:cd07723   48 LTTHHHWDHTGGNAELKALFPD-APVYGPAEDRipGLDHPVKD 89
 
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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