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Conserved domains on  [gi|15598568|ref|NP_252062|]
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carbon-phosphorus lyase complex accessory protein [Pseudomonas aeruginosa PAO1]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
11-254 7.09e-128

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.


The actual alignment was detected with superfamily member TIGR03307:

Pssm-ID: 451500  Cd Length: 238  Bit Score: 362.12  E-value: 7.09e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    11 ARQVPVYGCDCPACRNARADAGLRRRPCSALLECAGQRWLIDSGLVDLCERFPPHSLDGILQTHYHADHAQGLLHLRWGQ 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    91 GLVIPVHGPADPEGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiRRLAYLTDTVG 170
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDG-----QRVAYLTDTAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   171 LPADSASRLLAAPLDLLVLDCSMPPQERPPRNHNDLTRALECIESLRPRRAVLTHVGHAVDAWLLDHPaALPEGVELAHD 250
Cdd:TIGR03307 156 LPPDTEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENP-DLPSGVAVGYD 234

                  ....
gi 15598568   251 GMCL 254
Cdd:TIGR03307 235 GQTL 238
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
11-254 7.09e-128

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: 362.12  E-value: 7.09e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    11 ARQVPVYGCDCPACRNARADAGLRRRPCSALLECAGQRWLIDSGLVDLCERFPPHSLDGILQTHYHADHAQGLLHLRWGQ 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    91 GLVIPVHGPADPEGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiRRLAYLTDTVG 170
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDG-----QRVAYLTDTAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   171 LPADSASRLLAAPLDLLVLDCSMPPQERPPRNHNDLTRALECIESLRPRRAVLTHVGHAVDAWLLDHPaALPEGVELAHD 250
Cdd:TIGR03307 156 LPPDTEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENP-DLPSGVAVGYD 234

                  ....
gi 15598568   251 GMCL 254
Cdd:TIGR03307 235 GQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
1-191 2.26e-104

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: 300.31  E-value: 2.26e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACRNARADAGLRRRPCSALLECAGQRWLIDSGLVDLCERFPPHSLDGILQTHYHADHA 80
Cdd:cd07736   1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  81 QGLLHLRWGQGLVIPVHGPADPEGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiR 160
Cdd:cd07736  81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGG-----K 155
                       170       180       190
                ....*....|....*....|....*....|.
gi 15598568 161 RLAYLTDTVGLPADSASRLLAAPLDLLVLDC 191
Cdd:cd07736 156 RLAYLTDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
1-256 2.86e-58

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 185.87  E-value: 2.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACrnARADAGLRRRPCSALLECAGQRWLIDSG--LVDLCERFP--PHSLDGILQTHYH 76
Cdd:COG1235   1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDAGpdLREQLLRLGldPSKIDAILLTHEH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  77 ADHAQGLLHLRWGQGLV-IPVHGPADP-EGLADLYK-----HPGILDFsQPFGAFERRQWGALAATALPLVHSK-PTFGY 148
Cdd:COG1235  79 ADHIAGLDDLRPRYGPNpIPVYATPGTlEALERRFPylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAgDPVGY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 149 LLEGASeegtiRRLAYLTDTVGLPADSASRLlaAPLDLLVLDCSMPPQErppRNHNDLTRALECIESLRPRRAVLTHVG- 227
Cdd:COG1235 158 RIEDGG-----KKLAYATDTGYIPEEVLELL--RGADLLILDATYDDPE---PGHLSNEEALELLARLGPKRLVLTHLSp 227
                       250       260       270
                ....*....|....*....|....*....|...
gi 15598568 228 ----HAVDAWLLDHpAALPEGVELAHDGMCLPL 256
Cdd:COG1235 228 dnndHELDYDELEA-ALLPAGVEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-252 3.59e-23

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 94.46  E-value: 3.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    1 MRLTLLGTGDARQVPVYGCDCPACRNA-RADAGLRrrpCSALLECAGQRWLIDSGlVDLCE---RFPPHSLDGILQTHYH 76
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKdPRDNRLR---TSALVETEGARILIDCG-PDFREqmlRLPFGKIDAVLITHEH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   77 ADHAQGLLHLR-WGQGLVIPVHGPAD-PEGLADL-------YKHPGILDFS----QPFGAFERRQwgaLAATALPLVHSK 143
Cdd:PRK02113  77 YDHVGGLDDLRpFCRFGEVPIYAEQYvAERLRSRmpycfveHSYPGVPNIPlreiEPDRPFLVNH---TEVTPLRVMHGK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  144 -PTFGYllegaseegTIRRLAYLTDTVGLPADSASRLLAapLDLLVLDcSMPPQERPprNHNDLTRALECIESLRPRRAV 222
Cdd:PRK02113 154 lPILGY---------RIGKMAYITDMLTMPEEEYEQLQG--IDVLVMN-ALRIAPHP--THQSLEEALENIKRIGAKETY 219
                        250       260       270
                 ....*....|....*....|....*....|
gi 15598568  223 LTHVGHAVdAWLLDHPAALPEGVELAHDGM 252
Cdd:PRK02113 220 LIHMSHHI-GLHADVEKELPPHVHFAYDGL 248
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
67-225 2.37e-13

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 66.56  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    67 LDGILQTHYHADHAQGLLHLRWGQGLviPVHGPAdpeGLADLYKHPGILDFSQPFGAFERR--QWG--------ALAATA 136
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLREGRPR--PLYAPL---GVLAHLRRNFPYLFLLEHYGVRVHeiDWGesftvgdgGLTVTA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   137 LPLVHSKP---------TFGYLLEGASeegtiRRLAYLTDTVGLPADSASRLlaAPLDLLVLD-CSMPPQERPPRNHNDL 206
Cdd:pfam12706 104 TPARHGSPrgldpnpgdTLGFRIEGPG-----KRVYYAGDTGYFPDEIGERL--GGADLLLLDgGAWRDDEMIHMGHMTP 176
                         170
                  ....*....|....*....
gi 15598568   207 TRALECIESLRPRRAVLTH 225
Cdd:pfam12706 177 EEAVEAAADLGARRKVLIH 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
39-101 2.79e-05

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: 43.70  E-value: 2.79e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568     39 SALLECAGQRWLIDSG-------LVDLcERFPPHSLDGILQTHYHADHAQGLLHLRWGQGlvIPVHGPAD 101
Cdd:smart00849   2 SYLVRDDGGAILIDTGpgeaedlLAEL-KKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEG 68
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
11-254 7.09e-128

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: 362.12  E-value: 7.09e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    11 ARQVPVYGCDCPACRNARADAGLRRRPCSALLECAGQRWLIDSGLVDLCERFPPHSLDGILQTHYHADHAQGLLHLRWGQ 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    91 GLVIPVHGPADPEGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiRRLAYLTDTVG 170
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDG-----QRVAYLTDTAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   171 LPADSASRLLAAPLDLLVLDCSMPPQERPPRNHNDLTRALECIESLRPRRAVLTHVGHAVDAWLLDHPaALPEGVELAHD 250
Cdd:TIGR03307 156 LPPDTEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENP-DLPSGVAVGYD 234

                  ....
gi 15598568   251 GMCL 254
Cdd:TIGR03307 235 GQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
1-191 2.26e-104

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: 300.31  E-value: 2.26e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACRNARADAGLRRRPCSALLECAGQRWLIDSGLVDLCERFPPHSLDGILQTHYHADHA 80
Cdd:cd07736   1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  81 QGLLHLRWGQGLVIPVHGPADPEGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiR 160
Cdd:cd07736  81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGG-----K 155
                       170       180       190
                ....*....|....*....|....*....|.
gi 15598568 161 RLAYLTDTVGLPADSASRLLAAPLDLLVLDC 191
Cdd:cd07736 156 RLAYLTDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
1-256 2.86e-58

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 185.87  E-value: 2.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACrnARADAGLRRRPCSALLECAGQRWLIDSG--LVDLCERFP--PHSLDGILQTHYH 76
Cdd:COG1235   1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDAGpdLREQLLRLGldPSKIDAILLTHEH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  77 ADHAQGLLHLRWGQGLV-IPVHGPADP-EGLADLYK-----HPGILDFsQPFGAFERRQWGALAATALPLVHSK-PTFGY 148
Cdd:COG1235  79 ADHIAGLDDLRPRYGPNpIPVYATPGTlEALERRFPylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAgDPVGY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 149 LLEGASeegtiRRLAYLTDTVGLPADSASRLlaAPLDLLVLDCSMPPQErppRNHNDLTRALECIESLRPRRAVLTHVG- 227
Cdd:COG1235 158 RIEDGG-----KKLAYATDTGYIPEEVLELL--RGADLLILDATYDDPE---PGHLSNEEALELLARLGPKRLVLTHLSp 227
                       250       260       270
                ....*....|....*....|....*....|...
gi 15598568 228 ----HAVDAWLLDHpAALPEGVELAHDGMCLPL 256
Cdd:COG1235 228 dnndHELDYDELEA-ALLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
1-191 2.73e-34

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 122.20  E-value: 2.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACrnARADAGLRRRPCSALLECAGQRWLIDSGlVDL---CERFPPHSLDGILQTHYHA 77
Cdd:cd16279   1 MKLTFLGTGTSSGVPVIGCDCGVC--DSSDPKNRRLRSSILIETGGKNILIDTG-PDFrqqALRAGIRKLDAVLLTHAHA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  78 DHAQGLLHLR---WGQGLVIPVHgpADPEGLADL------------YKHPGILDFsQPFGAFERRQWGALAATALPLVHS 142
Cdd:cd16279  78 DHIHGLDDLRpfnRLQQRPIPVY--ASEETLDDLkrrfpyffaatgGGGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15598568 143 K-PTFGYLlegaseegtIRRLAYLTDTVGLPADSASRLLAapLDLLVLDC 191
Cdd:cd16279 155 KlPSLGFR---------FGDFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-256 1.17e-29

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 111.44  E-value: 1.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARqvpvygcdcpacrnaradAGLRRRPCSALLECAGQRWLID--SGLVDLCERF--PPHSLDGILQTHYH 76
Cdd:COG1234   1 MKLTFLGTGGAV------------------PTPGRATSSYLLEAGGERLLIDcgEGTQRQLLRAglDPRDIDAIFITHLH 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  77 ADHAQGL---LHLRWGQGLV--IPVHGPADP-EGLADLYK-HPGILDFS---QPFGAFERRQWGALAATALPLVHSKPTF 146
Cdd:COG1234  63 GDHIAGLpglLSTRSLAGREkpLTIYGPPGTkEFLEALLKaSGTDLDFPlefHEIEPGEVFEIGGFTVTAFPLDHPVPAY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 147 GYLLEgasEEGtiRRLAYLTDTVglPADSASRlLAAPLDLLVLDCSMPPQER---PPRNHNDLTRALECIESLRPRRAVL 223
Cdd:COG1234 143 GYRFE---EPG--RSLVYSGDTR--PCEALVE-LAKGADLLIHEATFLDEEAelaKETGHSTAKEAAELAAEAGVKRLVL 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15598568 224 THVGhavdAWLLDHPAAL-------PEGVELAHDGMCLPL 256
Cdd:COG1234 215 THFS----PRYDDPEELLaearavfPGPVELAEDGMVIEL 250
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-252 3.59e-23

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 94.46  E-value: 3.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    1 MRLTLLGTGDARQVPVYGCDCPACRNA-RADAGLRrrpCSALLECAGQRWLIDSGlVDLCE---RFPPHSLDGILQTHYH 76
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKdPRDNRLR---TSALVETEGARILIDCG-PDFREqmlRLPFGKIDAVLITHEH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   77 ADHAQGLLHLR-WGQGLVIPVHGPAD-PEGLADL-------YKHPGILDFS----QPFGAFERRQwgaLAATALPLVHSK 143
Cdd:PRK02113  77 YDHVGGLDDLRpFCRFGEVPIYAEQYvAERLRSRmpycfveHSYPGVPNIPlreiEPDRPFLVNH---TEVTPLRVMHGK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  144 -PTFGYllegaseegTIRRLAYLTDTVGLPADSASRLLAapLDLLVLDcSMPPQERPprNHNDLTRALECIESLRPRRAV 222
Cdd:PRK02113 154 lPILGY---------RIGKMAYITDMLTMPEEEYEQLQG--IDVLVMN-ALRIAPHP--THQSLEEALENIKRIGAKETY 219
                        250       260       270
                 ....*....|....*....|....*....|
gi 15598568  223 LTHVGHAVdAWLLDHPAALPEGVELAHDGM 252
Cdd:PRK02113 220 LIHMSHHI-GLHADVEKELPPHVHFAYDGL 248
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
67-225 2.37e-13

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 66.56  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    67 LDGILQTHYHADHAQGLLHLRWGQGLviPVHGPAdpeGLADLYKHPGILDFSQPFGAFERR--QWG--------ALAATA 136
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLREGRPR--PLYAPL---GVLAHLRRNFPYLFLLEHYGVRVHeiDWGesftvgdgGLTVTA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   137 LPLVHSKP---------TFGYLLEGASeegtiRRLAYLTDTVGLPADSASRLlaAPLDLLVLD-CSMPPQERPPRNHNDL 206
Cdd:pfam12706 104 TPARHGSPrgldpnpgdTLGFRIEGPG-----KRVYYAGDTGYFPDEIGERL--GGADLLLLDgGAWRDDEMIHMGHMTP 176
                         170
                  ....*....|....*....
gi 15598568   207 TRALECIESLRPRRAVLTH 225
Cdd:pfam12706 177 EEAVEAAADLGARRKVLIH 195
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
3-225 3.61e-12

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: 63.75  E-value: 3.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   3 LTLLGTGDARQVpvygcdcpACRNARADAGLrrrpcsaLLECAGQRWLIDSG---LVDLCE-RFPPHSLDGILQTHYHAD 78
Cdd:cd07741   1 IIFLGTGGGRFV--------VITQLRASGGI-------WIELNGKNIHIDPGpgaLVRMCRpKLDPTKLDAIILSHRHLD 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  79 HA-----------QGLLHLRwgqGLVIpvhGPADP---EGLADLYKHPGILDFSQPFGAFERRQWGALAATALPLVHSKP 144
Cdd:cd07741  66 HSndanvlieamtEGGFKKR---GTLL---APEDAlngEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSDP 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 145 -TFGYLLEGASeegtiRRLAYLTDTVGLPadsasRLLAAP--LDLLVLDCSMpPQERPPRNHNDLTRALECIESLRPRRA 221
Cdd:cd07741 140 tTYGFIFRTSD-----KKIGYISDTRYFE-----ELIEYYsnCDVLIINVTR-PRPRKGVDHLSVEDVEKILKEIKPKLA 208

                ....
gi 15598568 222 VLTH 225
Cdd:cd07741 209 ILTH 212
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
36-191 6.20e-12

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: 62.46  E-value: 6.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  36 RPCSA-LLECAGQRWLIDSG---LVDLCERFPPHSLDGILQTHYHADH---AQGLLH-LRWGQGL----VIPVHGPADP- 102
Cdd:cd07716  16 GACSGyLLEADGFRILLDCGsgvLSRLQRYIDPEDLDAVVLSHLHPDHcadLGVLQYaRRYHPRGarkpPLPLYGPAGPa 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 103 EGLADLYKHPGILDFsQPFGAFERRQWGALAATALPLVHSKPTFGYLLEGASeegtiRRLAYLTDTVglPADSASRlLAA 182
Cdd:cd07716  96 ERLAALYGLEDVFDF-HPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGG-----KVLVYTGDTG--YCDELVE-FAR 166

                ....*....
gi 15598568 183 PLDLLVLDC 191
Cdd:cd07716 167 GADLLLCEA 175
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
3-188 8.16e-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: 63.24  E-value: 8.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   3 LTLLGTGDArqVPvygcdcpacrnaradagLRRRPCSA-LLECAGQRWLIDSG------LvdLCERFPPHSLDGILQTHY 75
Cdd:cd07717   1 LTFLGTGSA--VP-----------------TPERNLSSiALRLEGELWLFDCGegtqrqL--LRAGLSPSKIDRIFITHL 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  76 HADHA---QGLLHLRWGQGLVIPVH--GpadPEGLADLYKHpgILDFSQPFGAFE------------RRQWGALAATALP 138
Cdd:cd07717  60 HGDHIlglPGLLSTMSLLGRTEPLTiyG---PKGLKEFLET--LLRLSASRLPYPievhelepdpglVFEDDGFTVTAFP 134
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15598568 139 LVHSKPTFGYLLegasEEGtiRRLAYLTDTvgLPADSASRlLAAPLDLLV 188
Cdd:cd07717 135 LDHRVPCFGYRF----EEG--RKIAYLGDT--RPCEGLVE-LAKGADLLI 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
3-191 9.01e-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: 59.20  E-value: 9.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   3 LTLLGTGDArqVPvygcdcpacrnaradaGLRRRPCSALLECAGQRWLID--SGLVD--LCERFPPHSLDGILQTHYHAD 78
Cdd:cd16272   1 LTFLGTGGA--VP----------------SLTRNTSSYLLETGGTRILLDcgEGTVYrlLKAGVDPDKLDAIFLSHFHLD 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  79 HAQGLLHL----RWGQGLV-IPVHGpadPEGLADLYKHpgILDFSQPFGAF-------------ERRQWGALAATALPLV 140
Cdd:cd16272  63 HIGGLPTLlfarRYGGRKKpLTIYG---PKGIKEFLEK--LLNFPVEILPLgfpleieeleeggEVLELGDLKVEAFPVK 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15598568 141 HSKPTFGYLLEgasEEGtiRRLAYLTDTvglPADSASRLLAAPLDLLVLDC 191
Cdd:cd16272 138 HSVESLGYRIE---AEG--KSIVYSGDT---GPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
2-148 3.15e-10

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: 57.91  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   2 RLTLLGTGdarqvpvygcdCPACRNARAdaglrrrPCSALLECAGQRWLIDSG------LVDLceRFPPHSLDGILQTHY 75
Cdd:cd07719   1 RVTLLGTG-----------GPIPDPDRA-------GPSTLVVVGGRVYLVDAGsgvvrrLAQA--GLPLGDLDAVFLTHL 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  76 HADHAQGL---LHLRWGQGLV--IPVHGPAD----PEGLADLYKHPGIL-------------------DFSQPFGAFERr 127
Cdd:cd07719  61 HSDHVADLpalLLTAWLAGRKtpLPVYGPPGtralVDGLLAAYALDIDYrarigdegrpdpgalvevhEIAAGGVVYED- 139
                       170       180
                ....*....|....*....|...
gi 15598568 128 qwGALAATALPLVHS--KPTFGY 148
Cdd:cd07719 140 --DGVKVTAFLVDHGpvPPALAY 160
PRK00055 PRK00055
ribonuclease Z; Reviewed
1-188 1.18e-09

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 57.11  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    1 MRLTLLGTGDarQVPvygcdcpacrnaradagLRRR-PCSALLECAGQRWLIDSG------LvdLCERFPPHSLDGILQT 73
Cdd:PRK00055   2 MELTFLGTGS--GVP-----------------TPTRnVSSILLRLGGELFLFDCGegtqrqL--LKTGIKPRKIDKIFIT 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   74 HYHADHAQGLLHL---RWGQGLV--IPVHGPAdpeGLADLYKhpGILDFSQPFG-AF-ERRQWGAL---AATALPlVHSK 143
Cdd:PRK00055  61 HLHGDHIFGLPGLlstRSLSGRTepLTIYGPK---GIKEFVE--TLLRASGSLGyRIaEKDKPGKLdaeKLKALG-VPPG 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598568  144 PTFGYLLEGAS---EEGTI-------------RRLAYLTDTVglPADSASRlLAAPLDLLV 188
Cdd:PRK00055 135 PLFGKLKRGEDvtlEDGRIinpadvlgpprkgRKVAYCGDTR--PCEALVE-LAKGADLLV 192
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
39-225 4.70e-09

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 54.92  E-value: 4.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  39 SALLECAGQRWLIDSGLVDLCERFPPHSL--------DGILQTHYHADHAqGLLHLRWGQGLVIPVHGpadPEGLADLYK 110
Cdd:COG2220  13 TFLIETGGKRILIDPVFSGRASPVNPLPLdpedlpkiDAVLVTHDHYDHL-DDATLRALKRTGATVVA---PLGVAAWLR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 111 HPGILDFsQPFGAFERRQWGALAATALPLVHS--------KPTFGYLLEGasEEGTIrrlaYLT-DTvGLPADSASRLLA 181
Cdd:COG2220  89 AWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpdrngGLWVGFVIET--DGKTI----YHAgDT-GYFPEMKEIGER 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15598568 182 APLDLLVLDCSmppqerPPRNHNDLTRALECIESLRPRRAVLTH 225
Cdd:COG2220 161 FPIDVALLPIG------AYPFTMGPEEAAEAARDLKPKVVIPIH 198
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
42-201 1.43e-06

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: 47.49  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  42 LECAGQRWLID--SGLVDL----CERFPPHSLDgILQTHYHADHAQGL-----LHLRwgqGLVIPVHGPADPEG-----L 105
Cdd:cd07715  28 VRAGGELLILDagTGIRELgnelMKEGPPGEAH-LLLSHTHWDHIQGFpffapAYDP---GNRIHIYGPHKDGGsleevL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568 106 ADLYKHP----------GILDFSqPFGAFERRQWGALAATALPLVHSKPTFGYLLEgasEEGtiRRLAYLTDT----VGL 171
Cdd:cd07715 104 RRQMSPPyfpvpleellAAIEFH-DLEPGEPFSIGGVTVTTIPLNHPGGALGYRIE---EDG--KSVVYATDTehypDDG 177
                       170       180       190
                ....*....|....*....|....*....|
gi 15598568 172 PADSASRLLAAPLDLLVLDCSMPPQERPPR 201
Cdd:cd07715 178 ESDEALLEFARGADLLIHDAQYTDEEYPSK 207
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
39-168 2.23e-06

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 46.10  E-value: 2.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  39 SALLECAGQRWLIDSGL--------VDLCERfPPHSLDGILQTHYHADHAQGLLHLrwGQGLVIPVHGPAdpEGLADLYK 110
Cdd:cd07733  11 CTYLETEDGKLLIDAGLsgrkitgrLAEIGR-DPEDIDAILVTHEHADHIKGLGVL--ARKYNVPIYATA--GTLRAMER 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598568 111 HPGILDFSQ--PFGAFERRQWGALAATALPLVH--SKPTfGYLLEGASeegtiRRLAYLTDT 168
Cdd:cd07733  86 KVGLIDVDQkqIFEPGETFSIGDFDVESFGVSHdaADPV-GYRFEEGG-----RRFGMLTDL 141
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
1-252 6.76e-06

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 46.35  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568    1 MRLTLLGTGDARQVPVYGCDCPACRNARA-DAGLRRRPCSALLECA-GQRWLIDSGLVDLC---ERFPP--------HS- 66
Cdd:PRK05184   1 MRIIVLGSAAGGGFPQWNCNCPNCRGARAgTIRAKPRTQSSIAVSAdGEDWVLLNASPDIRqqiQATPAlqparglrDTp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   67 LDGILQTHYHADHAQGLLHLRWGQGLviPVHgpADPEGLADL---------YKHPGILDFS--QPFGAFERRQWGALAAT 135
Cdd:PRK05184  81 IAAVVLTDGQIDHTTGLLTLREGQPF--PVY--ATPAVLEDLstgfpifnvLDHYGGVQRRpiALDGPFAVPGLPGLRFT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  136 ALPLVHSKP-------------TFGYLLEgasEEGTIRRLAYLTDTVGLPADSASRLLAAPLdLLV-----LDCSMP--- 194
Cdd:PRK05184 157 AFPVPSKAPpysphrsdpepgdNIGLRIE---DRATGKRLFYAPGLAEVTDALRARLAGADC-VLFdgtlwTDDEMIrag 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598568  195 ------------PQERPprnhndlTRALECIESLRPRRAVLTHVGHAVDAWLLDHP---AALPEGVELAHDGM 252
Cdd:PRK05184 233 vgtktgrrmghlPQSGP-------GGMIAALARLPIARKILIHINNTNPILDEDSPeraELEAAGIEVAHDGM 298
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
39-101 2.79e-05

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: 43.70  E-value: 2.79e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568     39 SALLECAGQRWLIDSG-------LVDLcERFPPHSLDGILQTHYHADHAQGLLHLRWGQGlvIPVHGPAD 101
Cdd:smart00849   2 SYLVRDDGGAILIDTGpgeaedlLAEL-KKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEG 68
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
1-126 1.33e-04

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 41.84  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   1 MRLTLLGTGDARQVPVYGCDCPACRNARADAG--LRRRPCSALLECAGQRWL-------IDSGLVDLCERFPPHSL---- 67
Cdd:cd16274   1 MRIKVLGSAAGGGFPQWNCNCPNCALARAGDGraTARTQSSIAVSADGENWVlinaspdIRQQIEATPELQPRPGLrdtp 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  68 -DGILQTHYHADHAQGLLHLRWGQGLviPVHgpADPEGLADLYKHPGILDFSQPFGAFER 126
Cdd:cd16274  81 iAAVLLTDAEIDHTTGLLSLREGQPL--TVY--ATAPVLEDLTTNFPFFVLLHAYGGVRR 136
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
41-79 2.40e-04

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 40.91  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15598568  41 LLECAGQRWLIDSGL----VDLCER------FPPHSLDGILQTHYHADH 79
Cdd:cd16295  16 LLETGGKRILLDCGLfqggKELEELnnepfpFDPKEIDAVILTHAHLDH 64
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
4-203 4.28e-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: 40.32  E-value: 4.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568   4 TLLGTGDArqvpvYGcdcpacrnaradAGLRRRPCSaLLECAGQRWLIDSG---LVDLcERF--PPHSLDGILQTHYHAD 78
Cdd:cd07740   1 TFLGSGDA-----FG------------SGGRLNTCF-HVASEAGRFLIDCGassLIAL-KRAgiDPNAIDAIFITHLHGD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  79 HAQGL--------LHLRWGQGLVIpvhgpADPEGLADLYKHpgILDFSQPFGAFERRQW---------------GALAAT 135
Cdd:cd07740  62 HFGGLpfflldaqFVAKRTRPLTI-----AGPPGLRERLRR--AMEALFPGSSKVPRRFdlevielepgepttlGGVTVT 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598568 136 ALPLVHSKPTFGYLLEgASEEGtiRRLAYLTDTVglPADsASRLLAAPLDLLVLDCSMppQERPPRNH 203
Cdd:cd07740 135 AFPVVHPSGALPLALR-LEAAG--RVLAYSGDTE--WTD-ALVPLARGADLFICECYF--FEKKVPGH 194
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
39-86 2.40e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.88  E-value: 2.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598568  39 SALLECAGQRWLIDSG---------LVDLCERFPPHSLDGILQTHYHADHAQGLLHL 86
Cdd:cd07731  12 AILIQTPGKTILIDTGprdsfgedvVVPYLKARGIKKLDYLILTHPDADHIGGLDAV 68
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
39-131 2.88e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 38.37  E-value: 2.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598568  39 SALLECAGQRWLIDSGLVDLCER------FPPHSLDGILQTHYHADHAQGLLHLRWgQGLVIPVHGPadPEGLADLYKHP 112
Cdd:cd07713  22 SLLIETEGKKILFDTGQSGVLLHnakklgIDLSDIDAVVLSHGHYDHTGGLKALLE-LNPKAPVYAH--PDAFEPRYSKR 98
                        90
                ....*....|....*....
gi 15598568 113 GILDFSQPFGAFERRQWGA 131
Cdd:cd07713  99 GGGKKGIGIGREELEKAGA 117
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
66-101 6.32e-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: 6.32e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15598568  66 SLDGILQTHYHADHAQGLLHL--RWGQglvIPVHGPAD 101
Cdd:cd07723  43 TLTAILTTHHHWDHTGGNAELkaLFPD---APVYGPAE 77
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
45-101 6.99e-03

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 36.49  E-value: 6.99e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598568  45 AGQRWLIDSG------LVDLCERFPPHsLDGILQTHYHADHAQGLLHLRWGQGlvIPVHGPAD 101
Cdd:cd06262  19 EGEAILIDPGagalekILEAIEELGLK-IKAILLTHGHFDHIGGLAELKEAPG--APVYIHEA 78
 
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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