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Conserved domains on  [gi|15834329|ref|NP_313102|]
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5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase [Escherichia coli O157:H7 str. Sakai]

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 6.50e-156

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: 432.61  E-value: 6.50e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    13 AQGVPAWGCECAACARARRSPHYRRQPCSGVVKFNEAITLIDAGRHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    93 GDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15834329   173 LKFLRNNQPQVMVIDCSHPPREDAPRNHCDLNTVLALNQVIRSPRVVLTHISHQFDAWLMENA-LPSGFEAGFDGMEI 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 6.50e-156

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: 432.61  E-value: 6.50e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    13 AQGVPAWGCECAACARARRSPHYRRQPCSGVVKFNEAITLIDAGRHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    93 GDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15834329   173 LKFLRNNQPQVMVIDCSHPPREDAPRNHCDLNTVLALNQVIRSPRVVLTHISHQFDAWLMENA-LPSGFEAGFDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 3.40e-117

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: 332.66  E-value: 3.40e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   3 LTLTLTGSGGAQGVPAWGCECAACARARRSPHYRRQPCSGVVKFNEAITLIDAGRHDLADRWSPGSFQQFLLTHYHMDHV 82
Cdd:cd07736   1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  83 QGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWL 162
Cdd:cd07736  81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                       170       180
                ....*....|....*....|....*.
gi 15834329 163 SDTAGLPEKTLKFLRNNQPQVMVIDC 188
Cdd:cd07736 161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-249 6.66e-64

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 200.12  E-value: 6.66e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   3 LTLTLTGSGGAQGVPAWGCECAACARARrsPHYRRQPCSGVVKFNEAITLIDAG----RHDLADRWSPGSFQQFLLTHYH 78
Cdd:COG1235   1 MKVTFLGSGSSGGVPQIGCDCPVCASTD--PRYGRTRSSILVEADGTRLLIDAGpdlrEQLLRLGLDPSKIDAILLTHEH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  79 MDHVQGLFPLRWG-VGDPIPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFGY 150
Cdd:COG1235  79 ADHIAGLDDLRPRyGPNPIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVGY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 151 LLETAHSRVAWLSDTAGLPEKTLKFLRNnqPQVMVIDCSHPPREDaprNHCDLNTVLALNQVIRSPRVVLTHIS-----H 225
Cdd:COG1235 158 RIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdnndH 232

                       250       260
                ....*....|....*....|....*
gi 15834329 226 QFDAWLMENAL-PSGFEAGFDGMEI 249
Cdd:COG1235 233 ELDYDELEAALlPAGVEVAYDGMEI 257
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-249 1.93e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 92.54  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    3 LTLTLTGSGGAQGVPAWGCECAACARArrSPHYRRQPCSGVVKFNEAITLIDAGRhDLadRWSP-----GSFQQFLLTHY 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDCGP-DF--REQMlrlpfGKIDAVLITHE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   78 HMDHVQGLFPLR-WGVGDPIPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHS 144
Cdd:PRK02113  76 HYDHVGGLDDLRpFCRFGEVPIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  145 KLT-FGYLLetahSRVAWLSDTAGLPEKTLKFLRNnqPQVMVIDCSHPpredAPRN-HCDLNTVLALNQVIRSPRVVLTH 222
Cdd:PRK02113 153 KLPiLGYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNALRI----APHPtHQSLEEALENIKRIGAKETYLIH 222

                        250       260       270
                 ....*....|....*....|....*....|
gi 15834329  223 ISHqfDAWL---MENALPSGFEAGFDGMEI 249
Cdd:PRK02113 223 MSH--HIGLhadVEKELPPHVHFAYDGLEI 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 8.15e-12

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: 62.33  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    73 LLTHYHMDHVQGLFPLRwgVGDPIPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLR--EGRPRPLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   146 ---------LTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNnqPQVMVID-CSHPPREDAPRNHCDLNTVLALNQVIRS 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 15834329   216 PRVVLTHI 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 1.47e-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: 38.30  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329     41 SGVVKFNEAITLIDAGRHD------LADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGdpIPVYGPPDEQG--CDDLFK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEaedllaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 15834329    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 6.50e-156

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: 432.61  E-value: 6.50e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    13 AQGVPAWGCECAACARARRSPHYRRQPCSGVVKFNEAITLIDAGRHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    93 GDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15834329   173 LKFLRNNQPQVMVIDCSHPPREDAPRNHCDLNTVLALNQVIRSPRVVLTHISHQFDAWLMENA-LPSGFEAGFDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 3.40e-117

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: 332.66  E-value: 3.40e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   3 LTLTLTGSGGAQGVPAWGCECAACARARRSPHYRRQPCSGVVKFNEAITLIDAGRHDLADRWSPGSFQQFLLTHYHMDHV 82
Cdd:cd07736   1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  83 QGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWL 162
Cdd:cd07736  81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                       170       180
                ....*....|....*....|....*.
gi 15834329 163 SDTAGLPEKTLKFLRNNQPQVMVIDC 188
Cdd:cd07736 161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-249 6.66e-64

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 200.12  E-value: 6.66e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   3 LTLTLTGSGGAQGVPAWGCECAACARARrsPHYRRQPCSGVVKFNEAITLIDAG----RHDLADRWSPGSFQQFLLTHYH 78
Cdd:COG1235   1 MKVTFLGSGSSGGVPQIGCDCPVCASTD--PRYGRTRSSILVEADGTRLLIDAGpdlrEQLLRLGLDPSKIDAILLTHEH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  79 MDHVQGLFPLRWG-VGDPIPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFGY 150
Cdd:COG1235  79 ADHIAGLDDLRPRyGPNPIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVGY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 151 LLETAHSRVAWLSDTAGLPEKTLKFLRNnqPQVMVIDCSHPPREDaprNHCDLNTVLALNQVIRSPRVVLTHIS-----H 225
Cdd:COG1235 158 RIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdnndH 232

                       250       260
                ....*....|....*....|....*
gi 15834329 226 QFDAWLMENAL-PSGFEAGFDGMEI 249
Cdd:COG1235 233 ELDYDELEAALlPAGVEVAYDGMEI 257
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-188 9.64e-32

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: 115.26  E-value: 9.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   3 LTLTLTGSGGAQGVPAWGCECAACARArrSPHYRRQPCSGVVKFNEAITLIDAG---RHDLAdRWSPGSFQQFLLTHYHM 79
Cdd:cd16279   1 MKLTFLGTGTSSGVPVIGCDCGVCDSS--DPKNRRLRSSILIETGGKNILIDTGpdfRQQAL-RAGIRKLDAVLLTHAHA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  80 DHVQG---LFPLRWGVGDPIPVYGPPD-----EQGCDDLFK-----HPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL 146
Cdd:cd16279  78 DHIHGlddLRPFNRLQQRPIPVYASEEtlddlKRRFPYFFAatgggGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHGKL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15834329 147 -TFGYLLEtahsRVAWLSDTAGLPEKTLKFLRNnqPQVMVIDC 188
Cdd:cd16279 157 pSLGFRFG----DFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-249 6.96e-25

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 98.73  E-value: 6.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   5 LTLTGSGGAQGVPawgcecaacararrsphYRRQPCSgVVKFNEAITLIDAGrhdladrwsPGSFQQFL----------- 73
Cdd:COG1234   3 LTFLGTGGAVPTP-----------------GRATSSY-LLEAGGERLLIDCG---------EGTQRQLLragldprdida 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  74 --LTHYHMDHVQGLFPL---RW--GVGDPIPVYGPPD-EQGCDDLFK-HPGLLDFS---HTVEPFVVFDLQGLQVTPLPL 141
Cdd:COG1234  56 ifITHLHGDHIAGLPGLlstRSlaGREKPLTIYGPPGtKEFLEALLKaSGTDLDFPlefHEIEPGEVFEIGGFTVTAFPL 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 142 NHSKLTFGYLLETAHSRVAWLSDTaGLPEKTLKFLRNnqPQVMVIDCSHPPREDA---PRNHCdlnTVLALNQVIRS--- 215
Cdd:COG1234 136 DHPVPAYGYRFEEPGRSLVYSGDT-RPCEALVELAKG--ADLLIHEATFLDEEAElakETGHS---TAKEAAELAAEagv 209

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15834329 216 PRVVLTHISHQFD---AWLME--NALPSGFEAGFDGMEI 249
Cdd:COG1234 210 KRLVLTHFSPRYDdpeELLAEarAVFPGPVELAEDGMVI 248
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-249 1.93e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 92.54  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    3 LTLTLTGSGGAQGVPAWGCECAACARArrSPHYRRQPCSGVVKFNEAITLIDAGRhDLadRWSP-----GSFQQFLLTHY 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSK--DPRDNRLRTSALVETEGARILIDCGP-DF--REQMlrlpfGKIDAVLITHE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   78 HMDHVQGLFPLR-WGVGDPIPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHS 144
Cdd:PRK02113  76 HYDHVGGLDDLRpFCRFGEVPIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  145 KLT-FGYLLetahSRVAWLSDTAGLPEKTLKFLRNnqPQVMVIDCSHPpredAPRN-HCDLNTVLALNQVIRSPRVVLTH 222
Cdd:PRK02113 153 KLPiLGYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNALRI----APHPtHQSLEEALENIKRIGAKETYLIH 222

                        250       260       270
                 ....*....|....*....|....*....|
gi 15834329  223 ISHqfDAWL---MENALPSGFEAGFDGMEI 249
Cdd:PRK02113 223 MSH--HIGLhadVEKELPPHVHFAYDGLEI 250
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 33-249 5.34e-14

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: 69.40  E-value: 5.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  33 PHYRRQPCSGVVKFNEAITLIDAG--------RHdladRWSPGSFQQFLLTHYHMDHVQGLFPL-----RWGVGDPIPVY 99
Cdd:cd07717  11 PTPERNLSSIALRLEGELWLFDCGegtqrqllRA----GLSPSKIDRIFITHLHGDHILGLPGLlstmsLLGRTEPLTIY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 100 GPPdeqGCDDLFKHpgLLDFSHTVEPF------------VVFDLQGLQVTPLPLNHSKLTFGYLLETAHSrVAWLSDTAg 167
Cdd:cd07717  87 GPK---GLKEFLET--LLRLSASRLPYpievhelepdpgLVFEDDGFTVTAFPLDHRVPCFGYRFEEGRK-IAYLGDTR- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 168 LPEKTLKFLRNnqPQVMVIDC--SHPPREDAPRN-HCdlnTV-----LALNqvIRSPRVVLTHISHQFDAW--LMENALp 237
Cdd:cd07717 160 PCEGLVELAKG--ADLLIHEAtfLDDDAEKAKETgHS---TAkqaaeIAKK--AGVKKLVLTHFSARYKDPeeLLKEAR- 231

                       250
                ....*....|....*
gi 15834329 238 SGF---EAGFDGMEI 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 1.43e-13

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: 66.90  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  33 PHYRRQPCSGVVKFNEAITLIDAGR---HDLADR-WSPGSFQQFLLTHYHMDHVQGLFPLRW-----GVGDPIPVYGPPD 103
Cdd:cd16272  11 PSLTRNTSSYLLETGGTRILLDCGEgtvYRLLKAgVDPDKLDAIFLSHFHLDHIGGLPTLLFarrygGRKKPLTIYGPKG 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15834329 104 -EQGCDDLFKHPGL-------LDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTA 166
Cdd:cd16272  91 iKEFLEKLLNFPVEilplgfpLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-166 1.74e-13

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: 66.77  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   4 TLTLTGSGGaqgvPAWgcecaacaRARRSphyrrQPCSGVVKFNEAItLIDAGRhdladrwspGSFQQF----------- 72
Cdd:cd07719   1 RVTLLGTGG----PIP--------DPDRA-----GPSTLVVVGGRVY-LVDAGS---------GVVRRLaqaglplgdld 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  73 --LLTHYHMDHVQGLFPL---RWGVG--DPIPVYGPP--------------DEQGCDDLFKHPGLLDFSHTVE------P 125
Cdd:cd07719  54 avFLTHLHSDHVADLPALlltAWLAGrkTPLPVYGPPgtralvdgllaayaLDIDYRARIGDEGRPDPGALVEvheiaaG 133

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15834329 126 FVVFDLQGLQVTPLPLNHS--KLTFGYLLETAHSRVAWLSDTA 166
Cdd:cd07719 134 GVVYEDDGVKVTAFLVDHGpvPPALAYRFDTPGRSVVFSGDTG 176
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 8.15e-12

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: 62.33  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    73 LLTHYHMDHVQGLFPLRwgVGDPIPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLR--EGRPRPLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   146 ---------LTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNnqPQVMVID-CSHPPREDAPRNHCDLNTVLALNQVIRS 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 15834329   216 PRVVLTHI 223
Cdd:pfam12706 189 RRKVLIHI 196
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 52-198 2.97e-11

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: 60.97  E-value: 2.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  52 LIDAGR--HDLADRWSPGSFQQ---FLLTHYHMDHVQGL--F-PLRwgvgDP---IPVYGPPDEQGC-----DDLFKHP- 114
Cdd:cd07715  36 ILDAGTgiRELGNELMKEGPPGeahLLLSHTHWDHIQGFpfFaPAY----DPgnrIHIYGPHKDGGSleevlRRQMSPPy 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329 115 ---GLLDFS-----HTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDT------AGLPEKTLKFLRNnq 180
Cdd:cd07715 112 fpvPLEELLaaiefHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDTehypddGESDEALLEFARG-- 189

                       170
                ....*....|....*...
gi 15834329 181 PQVMVIDCSHPPREDAPR 198
Cdd:cd07715 190 ADLLIHDAQYTDEEYPSK 207
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-153 3.35e-10

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: 59.15  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329     5 LTLTGSGGaqGVPawgcecaacararrSPHyrRQPCSGVVKFNEAITLIDAG----RHDLADRWSPGSFQQFLLTHYHMD 80
Cdd:TIGR02651   2 ITFLGTGG--GVP--------------TKE--RNLPSIALKLNGELWLFDCGegtqRQMLRSGISPMKIDRIFITHLHGD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329    81 HVQGLFPL-----RWGVGDPIPVYGPPdeqGCDDLFKHpgLLDFSHTVEPF-----------VVFDLQGLQVTPLPLNHS 144
Cdd:TIGR02651  64 HILGLPGLlstmsFQGRKEPLTIYGPP---GIKEFIET--SLRVSYTYLNYpikiheieeggLVFEDDGFKVEAFPLDHS 138


                  ....*....
gi 15834329   145 KLTFGYLLE 153
Cdd:TIGR02651 139 IPSLGYRFE 147
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 52-166 3.96e-09

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: 54.37  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  52 LIDAGrhdladrwsPGSF---QQF---------LLTHYHMDHVQGLFPLR--------WGVGDPIPVYGPPDEQGC-DDL 110
Cdd:cd07716  31 LLDCG---------SGVLsrlQRYidpedldavVLSHLHPDHCADLGVLQyarryhprGARKPPLPLYGPAGPAERlAAL 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15834329 111 FKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTA 166
Cdd:cd07716 102 YGLEDVFDF-HPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTG 156
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 48-165 3.80e-07

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 49.90  E-value: 3.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  48 EAITLIDAG------RHDLADRWSPGSFQQ-----------FLLTHYHMDHVQGLfPL-----RWGVGDPIPVYGPPDEq 105
Cdd:cd07735  28 DGDILLDAGtgvgalSLEEMFNDILFPSQKaayelyqrirhYLITHAHLDHIAGL-PLlspndGGQRGSPKTIYGLPET- 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15834329 106 gCDDLFKH-------PGLLDFSHTVEPFVVFD---------LQGLQVTPLPLNHSKL-TFGYLLETAHSRVAWLSDT 165
Cdd:cd07735 106 -IDALKKHifnwviwPDFTSIPSGKYPYLRLEpiepeypiaLTGLSVTAFPVSHGVPvSTAFLIRDGGDSFLFFGDT 181
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 8-141 4.53e-07

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: 49.15  E-value: 4.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329   8 TGSGGaqGVPAWGCECAACARARRSP---HYRRQPCSGVVKFNEAITLIDAgrhdladrwSPGSFQQF------------ 72
Cdd:cd16274   8 SAAGG--GFPQWNCNCPNCALARAGDgraTARTQSSIAVSADGENWVLINA---------SPDIRQQIeatpelqprpgl 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  73 --------LLTHYHMDHVQGLFPLRwgVGDPIPVYGPP-------DEQGCDDLFKHPGLLDFSHTV--EPFVVFDLQGLQ 135
Cdd:cd16274  77 rdtpiaavLLTDAEIDHTTGLLSLR--EGQPLTVYATApvledltTNFPFFVLLHAYGGVRRHRILpgEPFTLAGCPGLT 154


                ....*.
gi 15834329 136 VTPLPL 141
Cdd:cd16274 155 VTPFPV 160
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 43-222 7.69e-07

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 48.34  E-value: 7.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  43 VVKFNEAITLIDAGrhdladrwsPGSFQQ-------------FLLTHYHMDH-----------VQGLFPLRwGVgdpipV 98
Cdd:cd07741  24 WIELNGKNIHIDPG---------PGALVRmcrpkldptkldaIILSHRHLDHsndanvlieamTEGGFKKR-GT-----L 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  99 YGPPD---EQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHS-KLTFGYLLETAHSRVAWLSDTAGLPEKTLK 174
Cdd:cd07741  89 LAPEDalnGEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSdPTTYGFIFRTSDKKIGYISDTRYFEELIEY 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15834329 175 FlRNnqPQVMVIDCSHpPREDAPRNHCDLNTVLALNQVIRSPRVVLTH 222
Cdd:cd07741 169 Y-SN--CDVLIINVTR-PRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-165 1.58e-06

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 46.49  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  52 LIDAG--------RHDLADRwSPGSFQQFLLTHYHMDHVQGLFPL--RWGVgdpiPVYGPPDEqgCDDLFKHPGLLDFS- 120
Cdd:cd07733  22 LIDAGlsgrkitgRLAEIGR-DPEDIDAILVTHEHADHIKGLGVLarKYNV----PIYATAGT--LRAMERKVGLIDVDq 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15834329 121 -HTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLLETAHSRVAWLSDT 165
Cdd:cd07733  95 kQIFEPGETFSIGDFDVESFGVSHDAAdPVGYRFEEGGRRFGMLTDL 141
PRK00055 PRK00055
ribonuclease Z; Reviewed
 33-102 2.94e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 44.02  E-value: 2.94e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15834329   33 PHYRRQPCSGVVKFNEAITLIDAG----RHDLADRWSPGSFQQFLLTHYHMDHVQGLFPL-----RWGVGDPIPVYGPP 102
Cdd:PRK00055  14 PTPTRNVSSILLRLGGELFLFDCGegtqRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLlstrsLSGRTEPLTIYGPK 92
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 73-170 5.92e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.98  E-value: 5.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  73 LLTHYHMDHV--QGLFPLRwgvGDPIPVYGPPdeqGCDDLFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHS------ 144
Cdd:COG2220  53 LVTHDHYDHLddATLRALK---RTGATVVAPL---GVAAWLRAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpdr 125

                        90       100
                ....*....|....*....|....*...
gi 15834329 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 3.32e-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: 3.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15834329  73 LLTHYHMDHVQGLFPLRWGVGdpIPVYGPPDEQgcdDLFKHPGLLDFSHTVEPFVVFD 130
Cdd:cd06262  50 LLTHGHFDHIGGLAELKEAPG--APVYIHEADA---ELLEDPELNLAFFGGGPLPPPE 102
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 73-195 5.41e-04

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: 40.08  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  73 LLTHYHMDHVQGLfPLRWGVGDPiPVYGPP----------DEqgcddlFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLN 142
Cdd:cd07714  60 FITHGHEDHIGAL-PYLLPELNV-PIYATPltlalikkklEE------FKLIKKVKL-NEIKPGERIKLGDFEVEFFRVT 130

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15834329 143 HSKL-TFGYLLETAHSRVAWLSD-------TAGLP--EKTLKFLRNNQPQVMVIDC----SHPPRED 195
Cdd:cd07714 131 HSIPdSVGLAIKTPEGTIVHTGDfkfdqtpVDGKPtdLEKLAELGKEGVLLLLSDSvhvsGHASQED 197
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-166 9.06e-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: 39.16  E-value: 9.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  52 LIDAGRHDLAdRW-----SPGSFQQFLLTHYHMDHVQGLfP-------LRWGVGDPIPVYGPPD-----EQGCDDLFKHP 114
Cdd:cd07740  29 LIDCGASSLI-ALkragiDPNAIDAIFITHLHGDHFGGL-PfflldaqFVAKRTRPLTIAGPPGlrerlRRAMEALFPGS 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15834329 115 GLLD--FSHTV---EPFVVFDLQGLQVTPLPLNHSK--LTFGYLLETAHSRVAWLSDTA 166
Cdd:cd07740 107 SKVPrrFDLEVielEPGEPTTLGGVTVTAFPVVHPSgaLPLALRLEAAGRVLAYSGDTE 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 1.47e-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: 38.30  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329     41 SGVVKFNEAITLIDAGRHD------LADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGdpIPVYGPPDEQG--CDDLFK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEaedllaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 15834329    113 HPGLLDFSHTVEPFVVFD 130
Cdd:smart00849  80 LGELGAEAEPAPPDRTLK 97
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 41-144 6.16e-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: 36.98  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834329  41 SGVVKFNEAITLIDAGRHDLADRWSPGSFQQF-------LLTHYHMDHVQGLFPLRWGVGdpIPVYGPPDE------QGC 107
Cdd:COG0491  17 SYLIVGGDGAVLIDTGLGPADAEALLAALAALgldikavLLTHLHPDHVGGLAALAEAFG--APVYAHAAEaealeaPAA 94

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15834329 108 DDLFKHPGlLDFSHTVEPFVVFDLQGLQVTPLPLN-HS 144
Cdd:COG0491  95 GALFGREP-VPPDRTLEDGDTLELGGPGLEVIHTPgHT 131
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 73-113 6.23e-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: 36.28  E-value: 6.23e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15834329  73 LLTHYHMDHVQGLFPL--RWGvgdPIPVYGPPDEQ--GCDDLFKH 113
Cdd:cd07723  48 LTTHHHWDHTGGNAELkaLFP---DAPVYGPAEDRipGLDHPVKD 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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