NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|332554040|gb|EGJ51084|]
View 

metal-dependent hydrolase [Desulfocurvibacter africanus subsp. africanus str. Walvis Bay]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869882)

uncharacterized MBL fold metallo-hydrolase similar to Myxococcus xanthus TaR3

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 4-209 2.29e-96

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: 281.69  E-value: 2.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   4 RFWGVRGSIPVSGKAYTRFGGDSACLEVRGSRGSVILDAGTGLRGLGNALSA-GEPQPIHLLLTHFHWDHILGLLFFKPL 82
Cdd:cd07715    1 RFWGVRGSIPVPGPDTVRYGGNTSCVEVRAGGELLILDAGTGIRELGNELMKeGPPGEAHLLLSHTHWDHIQGFPFFAPA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  83 YDDRFRIAIHGPLPAEET-EATLAALMRQPYFPVPFASVQARLSFAHLREAET--VAGFNVEAIPLSHPSPGQGYAIEDE 159
Cdd:cd07715   81 YDPGNRIHIYGPHKDGGSlEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPfsIGGVTVTTIPLNHPGGALGYRIEED 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332554040 160 SGRLVFLTDNELDGEPA--LDRYAAFAQNASLLVHDAEYTGSEYALRKGWGH 209
Cdd:cd07715  161 GKSVVYATDTEHYPDDGesDEALLEFARGADLLIHDAQYTDEEYPSKRGWGH 212
 
Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 4-209 2.29e-96

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: 281.69  E-value: 2.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   4 RFWGVRGSIPVSGKAYTRFGGDSACLEVRGSRGSVILDAGTGLRGLGNALSA-GEPQPIHLLLTHFHWDHILGLLFFKPL 82
Cdd:cd07715    1 RFWGVRGSIPVPGPDTVRYGGNTSCVEVRAGGELLILDAGTGIRELGNELMKeGPPGEAHLLLSHTHWDHIQGFPFFAPA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  83 YDDRFRIAIHGPLPAEET-EATLAALMRQPYFPVPFASVQARLSFAHLREAET--VAGFNVEAIPLSHPSPGQGYAIEDE 159
Cdd:cd07715   81 YDPGNRIHIYGPHKDGGSlEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPfsIGGVTVTTIPLNHPGGALGYRIEED 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332554040 160 SGRLVFLTDNELDGEPA--LDRYAAFAQNASLLVHDAEYTGSEYALRKGWGH 209
Cdd:cd07715  161 GKSVVYATDTEHYPDDGesDEALLEFARGADLLIHDAQYTDEEYPSKRGWGH 212
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-272 3.50e-60

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 191.26  E-value: 3.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGSIPVSG---------KAYTRFGGDSACLEVRGSRGSVILDAGTGLRGLGNALSAGEPQPIHLLLTHFHWD 71
Cdd:COG1235    1 MKVTFLGSGSSGGVPQigcdcpvcaSTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  72 HILGLLFFKPLYDDRfRIAIHGplpaeeTEATLAALMRQpyFPVPFASVQARLSFAHLREAE--TVAGFNVEAIPLSHPS 149
Cdd:COG1235   81 HIAGLDDLRPRYGPN-PIPVYA------TPGTLEALERR--FPYLFAPYPGKLEFHEIEPGEpfEIGGLTVTPFPVPHDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 150 PG-QGYAIEDESGRLVFLTDNeldgEPALDRYAAFAQNASLLVHDAEYTGSEyalrkgWGHSSQERALELALRAGARRLA 228
Cdd:COG1235  152 GDpVGYRIEDGGKKLAYATDT----GYIPEEVLELLRGADLLILDATYDDPE------PGHLSNEEALELLARLGPKRLV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 332554040 229 LYHHNQDRTDAEVLAMERQCREKAAlaapdlDCFAAAQGMEVEF 272
Cdd:COG1235  222 LTHLSPDNNDHELDYDELEAALLPA------GVEVAYDGMEIEL 259
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 62-262 4.52e-19

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: 84.58  E-value: 4.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   62 HLLLTHFHWDHILGLLFF----------KPLYddrfriaIHGPlpaEETEATLAALMRQPYFPVPFasvqaRLSFAHLRE 131
Cdd:TIGR02651  54 RIFITHLHGDHILGLPGLlstmsfqgrkEPLT-------IYGP---PGIKEFIETSLRVSYTYLNY-----PIKIHEIEE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  132 AETVA---GFNVEAIPLSHPSPGQGYAIEDESGRLVFLTD--------------------------------NELDGEPA 176
Cdd:TIGR02651 119 GGLVFeddGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREkakelgippgplygklkrgetvtlidgriidpEDVLGPPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  177 -------------LDRYAAFAQNASLLVHDAEYTGSEYALRKGWGHSSQERALELALRAGARRLALYHHNQDRTDAEVLA 243
Cdd:TIGR02651 199 kgrkiaytgdtrpCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELL 278

                         250
                  ....*....|....*....
gi 332554040  244 MERQCREKAALAAPDLDCF 262
Cdd:TIGR02651 279 EEAKKIFPNTYIAEDFMEI 297
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 38-232 2.69e-15

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: 72.34  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   38 VILDAGTGLRGlgNALSAGEPQPI------HLLLTHFHWDHILGLLFFKPLYDDRfriaIHGPLPaeeTEATLAAlmrqp 111
Cdd:pfam12706   3 ILIDPGPDLRQ--QALPALQPGRLrddpidAVLLTHDHYDHLAGLLDLREGRPRP----LYAPLG---VLAHLRR----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  112 YFPVPFASVQARLSFAHLREAETVA----GFNVEAIPLSHPSPGQ---------GYAIEDESGRLVFLTDNELDGEPALD 178
Cdd:pfam12706  69 NFPYLFLLEHYGVRVHEIDWGESFTvgdgGLTVTATPARHGSPRGldpnpgdtlGFRIEGPGKRVYYAGDTGYFPDEIGE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332554040  179 RYaafaQNASLLVHDAEYTGSEYalRKGWGHSSQERALELALRAGARRLALYHH 232
Cdd:pfam12706 149 RL----GGADLLLLDGGAWRDDE--MIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00055 PRK00055
ribonuclease Z; Reviewed
 62-262 8.15e-12

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 63.66  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  62 HLLLTHFHWDHILGLLFF----------KPLYddrfriaIHGPlpaEETEATLAALMRQPYFpvpfasvqarLSFAhLRE 131
Cdd:PRK00055  56 KIFITHLHGDHIFGLPGLlstrslsgrtEPLT-------IYGP---KGIKEFVETLLRASGS----------LGYR-IAE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 132 AETVAGFNVEAIPLSHPSPG-------QGYAIEDESGRLVFLTDneLDGEP-------------ALDRYAAFAQNASLLV 191
Cdd:PRK00055 115 KDKPGKLDAEKLKALGVPPGplfgklkRGEDVTLEDGRIINPAD--VLGPPrkgrkvaycgdtrPCEALVELAKGADLLV 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332554040 192 HDAEYTGSEYALRKGWGHSSQERALELALRAGARRLALYHHNQdRTDAEVLAMERQCRE--KAALAAPDLDCF 262
Cdd:PRK00055 193 HEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSP-RYTGDPEELLKEAREifPNTELAEDLMRV 264
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 28-176 2.57e-10

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: 57.95  E-value: 2.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040    28 CLEVRGSRGSVILDAGTG--LRGLGNALSAGEPQPIHLLLTHFHWDHILGLLFFKplydDRFRIAIHGPlpaEETEATLA 105
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGeaEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELL----EAPGAPVYAP---EGTAELLK 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332554040   106 ALMRQPYFPVPFASVQARLSFAHLREAETVAGFNVEAIPLSHPSPGQgYAIEDESGRLVFLTDNELDGEPA 176
Cdd:smart00849  75 DLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGS-IVLYLPEGKILFTGDLLFAGGDG 144
 
Name Accession Description Interval E-value
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 4-209 2.29e-96

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: 281.69  E-value: 2.29e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   4 RFWGVRGSIPVSGKAYTRFGGDSACLEVRGSRGSVILDAGTGLRGLGNALSA-GEPQPIHLLLTHFHWDHILGLLFFKPL 82
Cdd:cd07715    1 RFWGVRGSIPVPGPDTVRYGGNTSCVEVRAGGELLILDAGTGIRELGNELMKeGPPGEAHLLLSHTHWDHIQGFPFFAPA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  83 YDDRFRIAIHGPLPAEET-EATLAALMRQPYFPVPFASVQARLSFAHLREAET--VAGFNVEAIPLSHPSPGQGYAIEDE 159
Cdd:cd07715   81 YDPGNRIHIYGPHKDGGSlEEVLRRQMSPPYFPVPLEELLAAIEFHDLEPGEPfsIGGVTVTTIPLNHPGGALGYRIEED 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332554040 160 SGRLVFLTDNELDGEPA--LDRYAAFAQNASLLVHDAEYTGSEYALRKGWGH 209
Cdd:cd07715  161 GKSVVYATDTEHYPDDGesDEALLEFARGADLLIHDAQYTDEEYPSKRGWGH 212
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-272 3.50e-60

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 191.26  E-value: 3.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGSIPVSG---------KAYTRFGGDSACLEVRGSRGSVILDAGTGLRGLGNALSAGEPQPIHLLLTHFHWD 71
Cdd:COG1235    1 MKVTFLGSGSSGGVPQigcdcpvcaSTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  72 HILGLLFFKPLYDDRfRIAIHGplpaeeTEATLAALMRQpyFPVPFASVQARLSFAHLREAE--TVAGFNVEAIPLSHPS 149
Cdd:COG1235   81 HIAGLDDLRPRYGPN-PIPVYA------TPGTLEALERR--FPYLFAPYPGKLEFHEIEPGEpfEIGGLTVTPFPVPHDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 150 PG-QGYAIEDESGRLVFLTDNeldgEPALDRYAAFAQNASLLVHDAEYTGSEyalrkgWGHSSQERALELALRAGARRLA 228
Cdd:COG1235  152 GDpVGYRIEDGGKKLAYATDT----GYIPEEVLELLRGADLLILDATYDDPE------PGHLSNEEALELLARLGPKRLV 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 332554040 229 LYHHNQDRTDAEVLAMERQCREKAAlaapdlDCFAAAQGMEVEF 272
Cdd:COG1235  222 LTHLSPDNNDHELDYDELEAALLPA------GVEVAYDGMEIEL 259
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-272 2.09e-43

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 148.03  E-value: 2.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGSIPVSGKAytrfggdSACLEVRGSRGSVILDAGTGLrgLGNALSAG-EPQPI-HLLLTHFHWDHILGL-- 76
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRA-------TSSYLLEAGGERLLIDCGEGT--QRQLLRAGlDPRDIdAIFITHLHGDHIAGLpg 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  77 LFFKPLYDDRFR-IAIHGPlpaEETEATLAALMRQPYFPVPFasvqaRLSFAHLREAETV--AGFNVEAIPLSHPSPGQG 153
Cdd:COG1234   72 LLSTRSLAGREKpLTIYGP---PGTKEFLEALLKASGTDLDF-----PLEFHEIEPGEVFeiGGFTVTAFPLDHPVPAYG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 154 YAIEDESGRLVFLTDNELDgepalDRYAAFAQNASLLVHDAEYTGSEYALRKGWGHSSQERALELALRAGARRLALYHHN 233
Cdd:COG1234  144 YRFEEPGRSLVYSGDTRPC-----EALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFS 218

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 332554040 234 QDRTDAEVLAMErqcrekaALAAPDLDCFAAAQGMEVEF 272
Cdd:COG1234  219 PRYDDPEELLAE-------ARAVFPGPVELAEDGMVIEL 250
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 62-262 3.24e-27

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: 105.61  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  62 HLLLTHFHWDHILGLLFF----------KPLYddrfriaIHGPlpaEETEATLAALMRQPYFPVPFasvqaRLSFAHLRE 131
Cdd:cd07717   53 RIFITHLHGDHILGLPGLlstmsllgrtEPLT-------IYGP---KGLKEFLETLLRLSASRLPY-----PIEVHELEP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 132 AETV----AGFNVEAIPLSHPSPGQGYAIEdESGRLVFLTDNELDgepalDRYAAFAQNASLLVHDAEYTGSEYALRKGW 207
Cdd:cd07717  118 DPGLvfedDGFTVTAFPLDHRVPCFGYRFE-EGRKIAYLGDTRPC-----EGLVELAKGADLLIHEATFLDDDAEKAKET 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332554040 208 GHSSQERALELALRAGARRLALYHHNQDRTDAEVLamERQCRE--KAALAAPDLDCF 262
Cdd:cd07717  192 GHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEEL--LKEARAvfPNTILAEDFMTI 246
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 15-194 3.04e-21

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: 88.09  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  15 SGKAYTRFGGDSACLEVRGSRGSVILDAGTG-LRGLGNALSAgEPQPIHLLLTHFHWDHILGL--LFFKPLYDDRFR-IA 90
Cdd:cd16272    6 TGGAVPSLTRNTSSYLLETGGTRILLDCGEGtVYRLLKAGVD-PDKLDAIFLSHFHLDHIGGLptLLFARRYGGRKKpLT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  91 IHGPlpaEETEATLAALMrqpYFPVPFASVQARLSFAHLREAETVA---GFNVEAIPLSHPSPGQGYAIEDESGRLVFLT 167
Cdd:cd16272   85 IYGP---KGIKEFLEKLL---NFPVEILPLGFPLEIEELEEGGEVLelgDLKVEAFPVKHSVESLGYRIEAEGKSIVYSG 158

                        170       180
                 ....*....|....*....|....*..
gi 332554040 168 DNELDgepalDRYAAFAQNASLLVHDA 194
Cdd:cd16272  159 DTGPC-----ENLVELAKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 62-262 4.52e-19

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: 84.58  E-value: 4.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   62 HLLLTHFHWDHILGLLFF----------KPLYddrfriaIHGPlpaEETEATLAALMRQPYFPVPFasvqaRLSFAHLRE 131
Cdd:TIGR02651  54 RIFITHLHGDHILGLPGLlstmsfqgrkEPLT-------IYGP---PGIKEFIETSLRVSYTYLNY-----PIKIHEIEE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  132 AETVA---GFNVEAIPLSHPSPGQGYAIEDESGRLVFLTD--------------------------------NELDGEPA 176
Cdd:TIGR02651 119 GGLVFeddGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREkakelgippgplygklkrgetvtlidgriidpEDVLGPPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  177 -------------LDRYAAFAQNASLLVHDAEYTGSEYALRKGWGHSSQERALELALRAGARRLALYHHNQDRTDAEVLA 243
Cdd:TIGR02651 199 kgrkiaytgdtrpCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELL 278

                         250
                  ....*....|....*....
gi 332554040  244 MERQCREKAALAAPDLDCF 262
Cdd:TIGR02651 279 EEAKKIFPNTYIAEDFMEI 297
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 38-232 2.69e-15

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: 72.34  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   38 VILDAGTGLRGlgNALSAGEPQPI------HLLLTHFHWDHILGLLFFKPLYDDRfriaIHGPLPaeeTEATLAAlmrqp 111
Cdd:pfam12706   3 ILIDPGPDLRQ--QALPALQPGRLrddpidAVLLTHDHYDHLAGLLDLREGRPRP----LYAPLG---VLAHLRR----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  112 YFPVPFASVQARLSFAHLREAETVA----GFNVEAIPLSHPSPGQ---------GYAIEDESGRLVFLTDNELDGEPALD 178
Cdd:pfam12706  69 NFPYLFLLEHYGVRVHEIDWGESFTvgdgGLTVTATPARHGSPRGldpnpgdtlGFRIEGPGKRVYYAGDTGYFPDEIGE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332554040  179 RYaafaQNASLLVHDAEYTGSEYalRKGWGHSSQERALELALRAGARRLALYHH 232
Cdd:pfam12706 149 RL----GGADLLLLDGGAWRDDE--MIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-168 3.11e-12

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: 63.80  E-value: 3.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGS--IPVSG---------KAYTRFGGDSACLEVRGSRGSVILDAGtgLRGLGNALSAGEPQPIhlLLTHFH 69
Cdd:cd07736    1 MKLTFLGTGDAggVPVYGcdcsacqraRQDPSYRRRPCSALIEVDGERILLDAG--LTDLAERFPPGSIDAI--LLTHFH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  70 WDHILGLLffkplyddRFRIAIHGPLP--AEETEATLAALMRQPyfpvpfasvqARLSFAHLREA-ETVA--GFNVEAIP 144
Cdd:cd07736   77 MDHVQGLF--------HLRWGVGDPIPvyGPPDPQGCADLFKHP----------GILDFQPLVAPfQSFElgGLKITPLP 138

                        170       180
                 ....*....|....*....|....
gi 332554040 145 LSHPSPGQGYAIEDESGRLVFLTD 168
Cdd:cd07736  139 LNHSKPTFGYLLESGGKRLAYLTD 162
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 31-194 5.22e-12

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: 63.26  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  31 VRGSRGSVILDAGTGLRGlgNALSAGEPQPIHLLLTHFHWDHILGLlffkplyDD--RFRIAIHGPLPAEETEATLAALM 108
Cdd:cd16279   40 IETGGKNILIDTGPDFRQ--QALRAGIRKLDAVLLTHAHADHIHGL-------DDlrPFNRLQQRPIPVYASEETLDDLK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 109 RQ-PYFPVPFASV-QARLSFAHLREAE--TVAGFNVEAIPLSH-PSPGQGYAIedesGRLVFLTD-NELDgepalDRYAA 182
Cdd:cd16279  111 RRfPYFFAATGGGgVPKLDLHIIEPDEpfTIGGLEITPLPVLHgKLPSLGFRF----GDFAYLTDvSEIP-----EESLE 181

                        170
                 ....*....|..
gi 332554040 183 FAQNASLLVHDA 194
Cdd:cd16279  182 KLRGLDVLILDA 193
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 28-168 7.29e-12

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: 61.90  E-value: 7.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  28 CLEVRGSRGSVILDAGTGLRGLGNALSA--GEPQPIH-LLLTHFHWDHILGLLFFKplydDRFRIAIHGplpaeeTEATL 104
Cdd:cd07733   11 CTYLETEDGKLLIDAGLSGRKITGRLAEigRDPEDIDaILVTHEHADHIKGLGVLA----RKYNVPIYA------TAGTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332554040 105 AAlMRQPYFPVPFASVQarlsFAHLREAETVAGFNVEAIPLSHPS-PGQGYAIEDESGRLVFLTD 168
Cdd:cd07733   81 RA-MERKVGLIDVDQKQ----IFEPGETFSIGDFDVESFGVSHDAaDPVGYRFEEGGRRFGMLTD 140
PRK00055 PRK00055
ribonuclease Z; Reviewed
 62-262 8.15e-12

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 63.66  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  62 HLLLTHFHWDHILGLLFF----------KPLYddrfriaIHGPlpaEETEATLAALMRQPYFpvpfasvqarLSFAhLRE 131
Cdd:PRK00055  56 KIFITHLHGDHIFGLPGLlstrslsgrtEPLT-------IYGP---KGIKEFVETLLRASGS----------LGYR-IAE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 132 AETVAGFNVEAIPLSHPSPG-------QGYAIEDESGRLVFLTDneLDGEP-------------ALDRYAAFAQNASLLV 191
Cdd:PRK00055 115 KDKPGKLDAEKLKALGVPPGplfgklkRGEDVTLEDGRIINPAD--VLGPPrkgrkvaycgdtrPCEALVELAKGADLLV 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332554040 192 HDAEYTGSEYALRKGWGHSSQERALELALRAGARRLALYHHNQdRTDAEVLAMERQCRE--KAALAAPDLDCF 262
Cdd:PRK00055 193 HEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSP-RYTGDPEELLKEAREifPNTELAEDLMRV 264
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-194 1.47e-11

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: 61.89  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  15 SGKAYTRFGGDSACLEVRGSRGSVILDAGT----GLRGLG---NALSAgepqpihLLLTHFHWDHILGLLFFkpLYDDRF 87
Cdd:cd07740    5 SGDAFGSGGRLNTCFHVASEAGRFLIDCGAssliALKRAGidpNAIDA-------IFITHLHGDHFGGLPFF--LLDAQF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  88 ------RIAIHGPLPAEEteaTLAALMrQPYFPvPFASVQAR--LSFAHLREAE--TVAGFNVEAIPLSHPSPGQGYAIE 157
Cdd:cd07740   76 vakrtrPLTIAGPPGLRE---RLRRAM-EALFP-GSSKVPRRfdLEVIELEPGEptTLGGVTVTAFPVVHPSGALPLALR 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332554040 158 -DESGRLVFLTDnelDGEPAlDRYAAFAQNASLLVHDA 194
Cdd:cd07740  151 lEAAGRVLAYSG---DTEWT-DALVPLARGADLFICEC 184
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-193 3.64e-11

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: 61.84  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGSIPvsgkaytrfGGDSACLEVR--GSRGSVILDAGTGLRGLGNALSAGEPQPI-------------HLLL 65
Cdd:cd07735    1 FELVVLGCSGGPD---------EGNTSSFLLDpaGSDGDILLDAGTGVGALSLEEMFNDILFPsqkaayelyqrirHYLI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  66 THFHWDHILGLLFFKP-LYDDRFR-IAIHGplpaeeTEATLAALMRQ-------PYFPVPFASVQARLSFAHLREAETVA 136
Cdd:cd07735   72 THAHLDHIAGLPLLSPnDGGQRGSpKTIYG------LPETIDALKKHifnwviwPDFTSIPSGKYPYLRLEPIEPEYPIA 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 137 GFN--VEAIPLSHPSPGQ-GYAIEDESGRLVFLTDNELDGEPALDRYAAFAQNASLLVHD 193
Cdd:cd07735  146 LTGlsVTAFPVSHGVPVStAFLIRDGGDSFLFFGDTGPDSVSKSPRLDALWRALAPLIPK 205
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
21-231 1.08e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.69  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   21 RFGGDSACLEVRGSRGSVILDAGTGLRG----LGNALSAGEPQPIHLLLTHFHWDHILGLLFFKPLYDDR-FRIAIHGPL 95
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAalllLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   96 PAEETEATLAALMRQPYFPVPFASVQARLSFAHLREAETVaGFNVEAIPLSHPSPGQgyaIEDESGRLVFLTDNELDGEP 175
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGL-GLLVTHGPGHGPGHVV---VYYGGGKVLFTGDLLFAGEI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332554040  176 ALDRYAAFAQNAsllvhdaeytgseyalRKGWGHSSQERALELALRAGARRLALYH 231
Cdd:pfam00753 157 GRLDLPLGGLLV----------------LHPSSAESSLESLLKLAKLKAAVIVPGH 196
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 36-192 2.10e-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: 58.68  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  36 GSVIL-DAGTG-LRGLGNA-LSAGEPQpiHLLLTHFHWDHILGLL-FFKPLYDDRFR--IAIHGPLPAEETEATLAALMR 109
Cdd:cd07719   27 GRVYLvDAGSGvVRRLAQAgLPLGDLD--AVFLTHLHSDHVADLPaLLLTAWLAGRKtpLPVYGPPGTRALVDGLLAAYA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 110 QPYFPVPFASVQARLSFAHLREAETVA---------GFNVEAIPLSHPS--PGQGYAIEDESGRLVFLTDNELDgePALD 178
Cdd:cd07719  105 LDIDYRARIGDEGRPDPGALVEVHEIAaggvvyeddGVKVTAFLVDHGPvpPALAYRFDTPGRSVVFSGDTGPS--ENLI 182

                        170
                 ....*....|....
gi 332554040 179 RyaaFAQNASLLVH 192
Cdd:cd07719  183 E---LAKGADLLVH 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 28-176 2.57e-10

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: 57.95  E-value: 2.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040    28 CLEVRGSRGSVILDAGTG--LRGLGNALSAGEPQPIHLLLTHFHWDHILGLLFFKplydDRFRIAIHGPlpaEETEATLA 105
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGeaEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELL----EAPGAPVYAP---EGTAELLK 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332554040   106 ALMRQPYFPVPFASVQARLSFAHLREAETVAGFNVEAIPLSHPSPGQgYAIEDESGRLVFLTDNELDGEPA 176
Cdd:smart00849  75 DLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGS-IVLYLPEGKILFTGDLLFAGGDG 144
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 23-194 8.14e-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: 53.60  E-value: 8.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  23 GGDSAC---LeVRGSRGSVILDAGTG-LRGLGNALSAGEPQpiHLLLTHFHWDHILGL------LFFKPLYDDRFRIAIH 92
Cdd:cd07716   13 GPGGACsgyL-LEADGFRILLDCGSGvLSRLQRYIDPEDLD--AVVLSHLHPDHCADLgvlqyaRRYHPRGARKPPLPLY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  93 GPlpaEETEATLAALmrqPYFPVPFAsvqarLSFAHLREAETVAGFNVEAIPLSHPSPGQGYAIEDESGRLVFLTDNELD 172
Cdd:cd07716   90 GP---AGPAERLAAL---YGLEDVFD-----FHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYC 158

                        170       180
                 ....*....|....*....|..
gi 332554040 173 gePALdryAAFAQNASLLVHDA 194
Cdd:cd07716  159 --DEL---VEFARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 33-168 2.04e-07

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: 49.98  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  33 GSRGSVILDAGTG-LRGLGNALSAGEPQPIHLLLTHFHWDHILGLLFFKPLYDdrFRIAIHgplPAEETEATLAALMRQP 111
Cdd:cd06262   18 EEGEAILIDPGAGaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG--APVYIH---EADAELLEDPELNLAF 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332554040 112 YFPVPFASVQArlsFAHLREAETV--AGFNVEAIPL-SHpSPG-QGYAIEDEsgRLVFLTD 168
Cdd:cd06262   93 FGGGPLPPPEP---DILLEDGDTIelGGLELEVIHTpGH-TPGsVCFYIEEE--GVLFTGD 147
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-165 9.06e-07

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: 48.53  E-value: 9.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  31 VRGSRGSVILDAGTGLRGLG---NALSAGEPQPIHLLLTHFHWDHILGLLFFKplydDRFRIAIHGPlpaEETEATLAAL 107
Cdd:COG0491   20 IVGGDGAVLIDTGLGPADAEallAALAALGLDIKAVLLTHLHPDHVGGLAALA----EAFGAPVYAH---AAEAEALEAP 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332554040 108 MRQPYFPVPFASVQARLsfaHLREAETVAGFNVEAIPLSHPSPG-QGYAIEDEsgRLVF 165
Cdd:COG0491   93 AAGALFGREPVPPDRTL---EDGDTLELGGPGLEVIHTPGHTPGhVSFYVPDE--KVLF 146
PRK02113 PRK02113
MBL fold metallo-hydrolase;
26-231 2.81e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 41.31  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  26 SACLEVRGSRgsVILDAGTGLRGlgNALSAGEPQPIHLLLTHFHWDHILGLlffkplyDDRFRIAIHGPLPAEETEATLA 105
Cdd:PRK02113  37 SALVETEGAR--ILIDCGPDFRE--QMLRLPFGKIDAVLITHEHYDHVGGL-------DDLRPFCRFGEVPIYAEQYVAE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 106 AL-MRQPY------FP----VPFASVQARLSFahlreaeTVAGFNVEAIPLSHPS-PGQGYAIedesGRLVFLTDNELDG 173
Cdd:PRK02113 106 RLrSRMPYcfvehsYPgvpnIPLREIEPDRPF-------LVNHTEVTPLRVMHGKlPILGYRI----GKMAYITDMLTMP 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 174 EPALDRYaafaQNASLLVHDaeytgseyALRKGWGHSSQ--ERALELALRAGARRLALYH 231
Cdd:PRK02113 175 EEEYEQL----QGIDVLVMN--------ALRIAPHPTHQslEEALENIKRIGAKETYLIH 222
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 31-79 5.78e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 39.92  E-value: 5.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 332554040  31 VRGSRGSVILDAGTGLRGLGNALSAGEPQPIHLLLTHFHWDHILGLLFF 79
Cdd:cd07712   14 LRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEF 62
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-168 8.86e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 39.44  E-value: 8.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  31 VRGSRGSVIL-DAGTG---LRGLGNALSAGEPQPIHLLLTHFHWDHILGLLFFKPLYDDRFrIAihgplPAEEteatlAA 106
Cdd:cd07743   13 YVFGDKEALLiDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKV-YA-----PKIE-----KA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332554040 107 LMRQPY-FPV------PFASVQARLSFAH-------LREAE-TVAGFNVEAIPLS-HpSPGQ-GYAIEDesgRLVFLTD 168
Cdd:cd07743   82 FIENPLlEPSylggayPPKELRNKFLMAKpskvddiIEEGElELGGVGLEIIPLPgH-SFGQiGILTPD---GVLFAGD 156
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-81 2.46e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 38.32  E-value: 2.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332554040  31 VRGSRGSVILDAGTGLRG---LGNALSAGEPQPI-HLLLTHFHWDHILGLLFFKP 81
Cdd:cd16282   20 IVGDDGVVVIDTGASPRLaraLLAAIRKVTDKPVrYVVNTHYHGDHTLGNAAFAD 74
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
63-205 3.77e-03

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 38.50  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040  63 LLLTHFHWDHILGLLFFKPlyddRFRIAIHG-PLPAEETEATL--AALMRQPYFPVpfasVQArlsfahlREAETVAGFN 139
Cdd:COG0595   67 IVLTHGHEDHIGALPYLLK----ELNVPVYGtPLTLALLEAKLkeHGLLKKVKLHV----VKP-------GDRIKFGPFK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040 140 VEAIPLSHPSP-GQGYAIEDESGRLVFLTD-----NELDGEPA-LDRYAAFA-QNASLLVHD---AE---YTGSEYALRK 205
Cdd:COG0595  132 VEFFRVTHSIPdSLGLAIRTPAGTIVHTGDfkfdqTPVDGEPTdLARLAELGeEGVLALLSDstnAErpgFTPSEREVGP 211
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-109 5.59e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 37.86  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332554040   1 MHVRFWGVRGSIpvsgkaytrfGGDSACLEVRGSRgsVILDAGT--GLRGLGNALSAGEPQPI-HLLLTHFHWDHIlGLL 77
Cdd:COG1236    1 MKLTFLGAAGEV----------TGSCYLLETGGTR--ILIDCGLfqGGKERNWPPFPFRPSDVdAVVLTHAHLDHS-GAL 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 332554040  78 ffkP-LYDDRFRIAIHGplpaeeTEATlAALMR 109
Cdd:COG1236   68 ---PlLVKEGFRGPIYA------TPAT-ADLAR 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH