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Conserved domains on  [gi|41017586|sp|Q9UZP4|]
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RecName: Full=Ribonuclease Z; Short=RNase Z; AltName: Full=tRNA 3 endonuclease; AltName: Full=tRNase Z

Protein Classification

ribonuclease Z( domain architecture ID 10021201)

ribonuclease Z is a tRNA 3-prime endonuclease that is involved in the maturation of tRNA, such as processing of tRNAs that lack an encoded CCA motif at the 3' end, to prepare for the addition of the motif by tRNA nucleotidyltransferase

CATH:  3.60.15.10
EC:  3.1.26.11
Gene Ontology:  GO:0042781|GO:0046872
PubMed:  17597585|11471246|17363966|12032089
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 3-296 2.69e-144

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: 408.15  E-value: 2.69e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586     3 EVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKR 82
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    83 KEPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHEL-PGKARLQFEKYEVWAFEVSHGVPALGYVFKEKDRRGSFDLEKI 161
Cdd:TIGR02651  81 KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIeEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   162 KNLGLEPGPWMKELEEKK-VINIGGRTIRLSEVTGPKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--G 238
Cdd:TIGR02651 161 KELGIPPGPLYGKLKRGEtVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKlaK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586   239 ESYHTTVEEACEIWKKSKAFNLALFHRGPRYSF-KEYKEGATKLCPQAMIPRDFDRIMV 296
Cdd:TIGR02651 241 EYGHSTAAQAAEIAKEANVKRLILTHISPRYSDeEELLEEAKKIFPNTYIAEDFMEIEI 299
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 3-296 2.69e-144

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: 408.15  E-value: 2.69e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586     3 EVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKR 82
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    83 KEPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHEL-PGKARLQFEKYEVWAFEVSHGVPALGYVFKEKDRRGSFDLEKI 161
Cdd:TIGR02651  81 KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIeEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   162 KNLGLEPGPWMKELEEKK-VINIGGRTIRLSEVTGPKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--G 238
Cdd:TIGR02651 161 KELGIPPGPLYGKLKRGEtVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKlaK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586   239 ESYHTTVEEACEIWKKSKAFNLALFHRGPRYSF-KEYKEGATKLCPQAMIPRDFDRIMV 296
Cdd:TIGR02651 241 EYGHSTAAQAAEIAKEANVKRLILTHISPRYSDeEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-297 4.33e-122

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 350.63  E-value: 4.33e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    1 MIEVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLW 80
Cdd:PRK00055   1 MMELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   81 KRKEPLHIYGPENSIEFIKNLLNSGYFapsfdvtvhelpgkarlqfekyevwafevshgvpaLGYVFKEKDRRGSFDLEK 160
Cdd:PRK00055  81 GRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLDAEK 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  161 IKNLGLEPGPWMKELEE-KKVINIGGRTIRLSEVTGPKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR-- 237
Cdd:PRK00055 126 LKALGVPPGPLFGKLKRgEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEEla 205

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41017586  238 GESYHTTVEEACEIWKKSKAFNLALFHRGPRYSF--KEYKEGATKLCPQAMIPRDFDRIMVK 297
Cdd:PRK00055 206 KEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGdpEELLKEAREIFPNTELAEDLMRVEVP 267
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 4-294 4.74e-106

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: 308.99  E-value: 4.74e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   4 VIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKRK 83
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  84 EPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHELPGKARLQFE--KYEVWAFEVSHGVPALGYVFKEkdrrgsfdleki 161
Cdd:cd07717  81 EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGLVFEddGFTVTAFPLDHRVPCFGYRFEE------------ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 162 knlglepgpwmkeleekkviniggrtirlsevtgpkkrGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--GE 239
Cdd:cd07717 149 --------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEkaKE 190

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586 240 SYHTTVEEACEIWKKSKAFNLALFHRGPRYS-FKEYKEGATKLCPQAMIPRDFDRI 294
Cdd:cd07717 191 TGHSTAKQAAEIAKKAGVKKLVLTHFSARYKdPEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
2-296 3.32e-94

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 279.00  E-value: 3.32e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   2 IEVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWK 81
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  82 RKEPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHELPGKARLQFEKYEVWAFEVSHGVPALGYVFKEKDRrgsfdleki 161
Cdd:COG1234  81 REKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGR--------- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 162 knlglepgpwmkeleekkviniggrtirlsevtgpkkrgaKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--GE 239
Cdd:COG1234 152 ----------------------------------------SLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAElaKE 191

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586 240 SYHTTVEEACEIWKKSKAFNLALFHRGPRYS-FKEYKEGATKLCP-QAMIPRDFDRIMV 296
Cdd:COG1234 192 TGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdPEELLAEARAVFPgPVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
2-229 2.38e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 72.73  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    2 IEVIFLGTGGIKPTPERNVPSIAIKV---EGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIqtMN 78
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELgngERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLY--PF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   79 LWK--RKEPLHIYGPENS---------IEFIKNLLN----SGYFAP---SFDVTVHELPGKARLQ--FEK--YEVWAFEV 136
Cdd:NF041257  91 GAWsgRWTPLRVWGPSGRtpelgtkhmVEGMKEMLAwdtdAFSGFPigdGYEIEVNEFDFRDENGvvYEEngVTVRSWPR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  137 SHGvpalgyvfkeKDRRGSFDLEkiknlglepgpWmkeleekkviniggrtirlsevtgpkkRGAKIVYTGDTEPCENVI 216
Cdd:NF041257 171 SHA----------KDGAVSYRLD-----------W---------------------------NGLSFVFTGDGRPNELTV 202

                        250
                 ....*....|...
gi 41017586  217 QFSRRANLLIHEA 229
Cdd:NF041257 203 EYAKGADVFIHEC 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-150 2.25e-12

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: 64.50  E-value: 2.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586     22 SIAIKVEGELILFDVGEGTLRQM--EIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNlwkrkepLHIYGPENSIEFIK 99
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLlaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG-------APVYAPEGTAELLK 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586    100 NLL----NSGYFAPSFDVtVHELPGKARLQFEKYEVWAFEVSHGVP-ALGYVFKEK 150
Cdd:smart00849  75 DLLallgELGAEAEPAPP-DRTLKDGDELDLGGGELEVIHTPGHTPgSIVLYLPEG 129
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 32-264 3.17e-12

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 64.25  E-value: 3.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    32 ILFDVGEGTLRQMEIAgLSPMKIRR-----IFITHFHGDHYLGLPALiqtmnlwKRKEPLHIYGPENSIEFIKNLLNSGY 106
Cdd:pfam12706   3 ILIDPGPDLRQQALPA-LQPGRLRDdpidaVLLTHDHYDHLAGLLDL-------REGRPRPLYAPLGVLAHLRRNFPYLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   107 FAPSFDVTVHELP--GKARLQFEKYEVWAFEVSHGVPalgyvfkekdrrgsfdlekiKNLGLEPGPWmkeleekkvinIG 184
Cdd:pfam12706  75 LLEHYGVRVHEIDwgESFTVGDGGLTVTATPARHGSP--------------------RGLDPNPGDT-----------LG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   185 GRtirlseVTGPKKRgakIVYTGDTEPC-ENVIQFSRRANLLIHEATYLNSEDRGESYHTTVEEACEIWKKSKAFNLALF 263
Cdd:pfam12706 124 FR------IEGPGKR---VYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  .
gi 41017586   264 H 264
Cdd:pfam12706 195 H 195
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 3-296 2.69e-144

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: 408.15  E-value: 2.69e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586     3 EVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKR 82
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    83 KEPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHEL-PGKARLQFEKYEVWAFEVSHGVPALGYVFKEKDRRGSFDLEKI 161
Cdd:TIGR02651  81 KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIeEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   162 KNLGLEPGPWMKELEEKK-VINIGGRTIRLSEVTGPKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--G 238
Cdd:TIGR02651 161 KELGIPPGPLYGKLKRGEtVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKlaK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586   239 ESYHTTVEEACEIWKKSKAFNLALFHRGPRYSF-KEYKEGATKLCPQAMIPRDFDRIMV 296
Cdd:TIGR02651 241 EYGHSTAAQAAEIAKEANVKRLILTHISPRYSDeEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-297 4.33e-122

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 350.63  E-value: 4.33e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    1 MIEVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLW 80
Cdd:PRK00055   1 MMELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   81 KRKEPLHIYGPENSIEFIKNLLNSGYFapsfdvtvhelpgkarlqfekyevwafevshgvpaLGYVFKEKDRRGSFDLEK 160
Cdd:PRK00055  81 GRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLDAEK 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  161 IKNLGLEPGPWMKELEE-KKVINIGGRTIRLSEVTGPKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR-- 237
Cdd:PRK00055 126 LKALGVPPGPLFGKLKRgEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEEla 205

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41017586  238 GESYHTTVEEACEIWKKSKAFNLALFHRGPRYSF--KEYKEGATKLCPQAMIPRDFDRIMVK 297
Cdd:PRK00055 206 KEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGdpEELLKEAREIFPNTELAEDLMRVEVP 267
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 4-294 4.74e-106

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: 308.99  E-value: 4.74e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   4 VIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKRK 83
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  84 EPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHELPGKARLQFE--KYEVWAFEVSHGVPALGYVFKEkdrrgsfdleki 161
Cdd:cd07717  81 EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGLVFEddGFTVTAFPLDHRVPCFGYRFEE------------ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 162 knlglepgpwmkeleekkviniggrtirlsevtgpkkrGAKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--GE 239
Cdd:cd07717 149 --------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEkaKE 190

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586 240 SYHTTVEEACEIWKKSKAFNLALFHRGPRYS-FKEYKEGATKLCPQAMIPRDFDRI 294
Cdd:cd07717 191 TGHSTAKQAAEIAKKAGVKKLVLTHFSARYKdPEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
2-296 3.32e-94

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 279.00  E-value: 3.32e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   2 IEVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWK 81
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  82 RKEPLHIYGPENSIEFIKNLLNSGYFAPSFDVTVHELPGKARLQFEKYEVWAFEVSHGVPALGYVFKEKDRrgsfdleki 161
Cdd:COG1234  81 REKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGR--------- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 162 knlglepgpwmkeleekkviniggrtirlsevtgpkkrgaKIVYTGDTEPCENVIQFSRRANLLIHEATYLNSEDR--GE 239
Cdd:COG1234 152 ----------------------------------------SLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAElaKE 191

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586 240 SYHTTVEEACEIWKKSKAFNLALFHRGPRYS-FKEYKEGATKLCP-QAMIPRDFDRIMV 296
Cdd:COG1234 192 TGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdPEELLAEARAVFPgPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 4-229 7.71e-53

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: 170.91  E-value: 7.71e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   4 VIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKRK 83
Cdd:cd16272   1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  84 EPLHIYGPENSIEFIKNLLNSGYFAP--SFDVTVHELPGKARLQFEK-YEVWAFEVSHGVPALGYVFKEKdrrgsfdlek 160
Cdd:cd16272  81 KPLTIYGPKGIKEFLEKLLNFPVEILplGFPLEIEELEEGGEVLELGdLKVEAFPVKHSVESLGYRIEAE---------- 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586 161 iknlglepgpwmkeleekkviniggrtirlsevtgpkkrGAKIVYTGDTEPCENVIQFSRRANLLIHEA 229
Cdd:cd16272 151 ---------------------------------------GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 3-227 7.92e-50

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: 163.84  E-value: 7.92e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   3 EVIFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLWKR 82
Cdd:cd07719   1 RVTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  83 KEPLHIYGPENSIEFIKNLLNS--------------GYFAPSFDVTVHEL-PGKARLQFEKYEVWAFEVSHGV--PALGY 145
Cdd:cd07719  81 KTPLPVYGPPGTRALVDGLLAAyaldidyrarigdeGRPDPGALVEVHEIaAGGVVYEDDGVKVTAFLVDHGPvpPALAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 146 VFKEKDRRgsfdlekiknlglepgpwmkeleekkviniggrtirlsevtgpkkrgakIVYTGDTEPCENVIQFSRRANLL 225
Cdd:cd07719 161 RFDTPGRS-------------------------------------------------VVFSGDTGPSENLIELAKGADLL 191


                ..
gi 41017586 226 IH 227
Cdd:cd07719 192 VH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-294 1.34e-34

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 126.16  E-value: 1.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   3 EVIFLGTGG----------------IKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDH 66
Cdd:COG1235   2 KVTFLGSGSsggvpqigcdcpvcasTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADH 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  67 YLGLPALIQTMNlwkrKEPLHIYGPENSIEFIKNLLnsGYFAPSF--DVTVHELPGKARLQFEKYEVWAFEVSHG-VPAL 143
Cdd:COG1235  82 IAGLDDLRPRYG----PNPIPVYATPGTLEALERRF--PYLFAPYpgKLEFHEIEPGEPFEIGGLTVTPFPVPHDaGDPV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 144 GYVFKEKDRRgsfdlekiknlglepgpwmkeleekkviniggrtirlsevtgpkkrgakIVYTGDTEP-CENVIQFSRRA 222
Cdd:COG1235 156 GYRIEDGGKK-------------------------------------------------LAYATDTGYiPEEVLELLRGA 186

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41017586 223 NLLIHEATYlnseDRGESYHTTVEEACEIWKKSKAFNLALFHRGPRYSFKE--YKEGATKLCPQAMIP-RDFDRI 294
Cdd:COG1235 187 DLLILDATY----DDPEPGHLSNEEALELLARLGPKRLVLTHLSPDNNDHEldYDELEAALLPAGVEVaYDGMEI 257
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-229 2.73e-30

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: 113.12  E-value: 2.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   5 IFLGTGGIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLW-KRK 83
Cdd:cd07740   1 TFLGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVaKRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  84 EPLHIYGPENSIEFIKNLLNSgYFAPS------FDVTVHELPGKARLQFEKYEVWAFEVSHGVPALGYvfkekdrrgSFD 157
Cdd:cd07740  81 RPLTIAGPPGLRERLRRAMEA-LFPGSskvprrFDLEVIELEPGEPTTLGGVTVTAFPVVHPSGALPL---------ALR 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41017586 158 LEkiknlglepgpwmkeleekkvinIGGRTirlsevtgpkkrgakIVYTGDTEPCENVIQFSRRANLLIHEA 229
Cdd:cd07740 151 LE-----------------------AAGRV---------------LAYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 4-230 3.68e-28

Ribonuclease Z ELAC1, C-terminus of ELAC2, 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. 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 eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 107.63  E-value: 3.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   4 VIFLGTGGIKPTPERNVPSIAIKVEGEL-ILFDVGEGTLRQM------EIAGLSPMKIRRIFITHFHGDHYLGLPALIQt 76
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGsILLDCGEGTLGQLrrhygpEEADEVLRNLKCIFISHLHADHHLGLIRLLA- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  77 mnLWKR-----KEPLHIYGPENSIEFIKnllnsgYFAPSFDVTVHELPGKARLQFEKYEVWAFEVSHgvPALGYVFKEkd 151
Cdd:cd07718  80 --ERKKlfkppSPPLYVVAPRQLRRWLR------EYSSLEDLGLHDISFISNRVSQSLPESDDPLSR--DLLSNLLEE-- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 152 rrgsfdlekiknLGLepgpwmKELEEKKVINIGG-RTIRLSevtgpKKRGAKIVYTGDTEPCENVIQFSRRANLLIHEAT 230
Cdd:cd07718 148 ------------LGL------KSIETVPVIHCPDaYGIVLT-----HEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
PRK02126 PRK02126
ribonuclease Z; Provisional
 28-269 2.95e-27

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 108.46  E-value: 2.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   28 EGELILFDVGEgtlrqmeIAGLSPMKIRR---IFITHFHGDHYLGLPALIQTmNLwKRKEPLHIYGPENSIEFIKNLLnS 104
Cdd:PRK02126  26 ERRALLFDLGD-------LHHLPPRELLRishIFVSHTHMDHFIGFDRLLRH-CL-GRPRRLRLFGPPGFADQVEHKL-A 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  105 GY-------FAPSFDVTVHELPG--------KARLQFEK------------------YEVWAFEVSHGVPALGYVFKEKD 151
Cdd:PRK02126  96 GYtwnlvenYPTTFRVHEVELHDgrirralfSCRRAFAReaeeelslpdgvlldepwFRVRAAFLDHGIPCLAFALEEKA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  152 RRGsFDLEKIKNLGLEPGPWMKELeeKKVI---NIGGRTIRLSEVTGPKKR------------------GAKIVYTGDT- 209
Cdd:PRK02126 176 HIN-IDKNRLAELGLPPGPWLREL--KHAVlrgEPDDTPIRVLWRDGGGEHervrplgelkervlriepGQKIGYVTDIg 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41017586  210 ---EPCENVIQFSRRANLLIHEATYLNSE-DRG-ESYHTTVEEACEIWKKSKAFNLALFHRGPRY 269
Cdd:PRK02126 253 yteENLARIVELAAGVDLLFIEAVFLDEDaEKArRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 28-229 6.75e-20

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: 84.80  E-value: 6.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  28 EGELILFDVGEGTLRQMEiAGLSPMKIRRIFITHFHGDHYLGLPAL---IQTMNLWKRKEPLHIYGPENSIEFIKNLLns 104
Cdd:cd07716  26 DGFRILLDCGSGVLSRLQ-RYIDPEDLDAVVLSHLHPDHCADLGVLqyaRRYHPRGARKPPLPLYGPAGPAERLAALY-- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 105 gYFAPSFDvtVHELPGKARLQFEKYEVWAFEVSHGVPALGyvfkekdrrgsfdlekiknlglepgpwmkeleekkvinig 184
Cdd:cd07716 103 -GLEDVFD--FHPIEPGEPLEIGPFTITFFRTVHPVPCYA---------------------------------------- 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41017586 185 grtIRLSEvtgpkkRGAKIVYTGDTEPCENVIQFSRRANLLIHEA 229
Cdd:cd07716 140 ---MRIED------GGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-147 3.75e-19

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: 83.29  E-value: 3.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   3 EVIFLGTG---GI----------KPTPERNV---PSIAIKVEGELILFDVGEgTLR-QMEIAGLSpmKIRRIFITHFHGD 65
Cdd:cd16279   2 KLTFLGTGtssGVpvigcdcgvcDSSDPKNRrlrSSILIETGGKNILIDTGP-DFRqQALRAGIR--KLDAVLLTHAHAD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  66 HYLGLPAL--IQtmnlWKRKEPLHIYGPENSIEFIKNLLNSGYFAPSF----DVTVHELPGKARLQFEKYEVWAFEVSHG 139
Cdd:cd16279  79 HIHGLDDLrpFN----RLQQRPIPVYASEETLDDLKRRFPYFFAATGGggvpKLDLHIIEPDEPFTIGGLEITPLPVLHG 154


                ....*....
gi 41017586 140 -VPALGYVF 147
Cdd:cd16279 155 kLPSLGFRF 163
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 6-235 4.72e-16

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: 75.23  E-value: 4.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   6 FLGT-GGIkPTPER-------NVPSIAIKVEGELILFDVGEGtLRQMeiaGLSPMKIRR-----IFITHFHGDHYLGLPA 72
Cdd:cd07715   2 FWGVrGSI-PVPGPdtvryggNTSCVEVRAGGELLILDAGTG-IREL---GNELMKEGPpgeahLLLSHTHWDHIQGFPF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  73 LIQtmnLWKRKEPLHIYGPENSIEFIKNLLNSGYFAPSF---------DVTVHELPGKARLQFEKYEVWAFEVSHGVPAL 143
Cdd:cd07715  77 FAP---AYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYFpvpleellaAIEFHDLEPGEPFSIGGVTVTTIPLNHPGGAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 144 GYvfkekdrrgsfdlekiknlglepgpwmkeleekkviniggrtiRLSEvtgpkkRGAKIVYTGDTEP-------CENVI 216
Cdd:cd07715 154 GY-------------------------------------------RIEE------DGKSVVYATDTEHypddgesDEALL 184

                       250
                ....*....|....*....
gi 41017586 217 QFSRRANLLIHEATYLNSE 235
Cdd:cd07715 185 EFARGADLLIHDAQYTDEE 203
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
2-229 2.38e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 72.73  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    2 IEVIFLGTGGIKPTPERNVPSIAIKV---EGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIqtMN 78
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELgngERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLY--PF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   79 LWK--RKEPLHIYGPENS---------IEFIKNLLN----SGYFAP---SFDVTVHELPGKARLQ--FEK--YEVWAFEV 136
Cdd:NF041257  91 GAWsgRWTPLRVWGPSGRtpelgtkhmVEGMKEMLAwdtdAFSGFPigdGYEIEVNEFDFRDENGvvYEEngVTVRSWPR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  137 SHGvpalgyvfkeKDRRGSFDLEkiknlglepgpWmkeleekkviniggrtirlsevtgpkkRGAKIVYTGDTEPCENVI 216
Cdd:NF041257 171 SHA----------KDGAVSYRLD-----------W---------------------------NGLSFVFTGDGRPNELTV 202

                        250
                 ....*....|...
gi 41017586  217 QFSRRANLLIHEA 229
Cdd:NF041257 203 EYAKGADVFIHEC 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-150 2.25e-12

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: 64.50  E-value: 2.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586     22 SIAIKVEGELILFDVGEGTLRQM--EIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNlwkrkepLHIYGPENSIEFIK 99
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLlaELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG-------APVYAPEGTAELLK 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586    100 NLL----NSGYFAPSFDVtVHELPGKARLQFEKYEVWAFEVSHGVP-ALGYVFKEK 150
Cdd:smart00849  75 DLLallgELGAEAEPAPP-DRTLKDGDELDLGGGELEVIHTPGHTPgSIVLYLPEG 129
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 32-264 3.17e-12

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 64.25  E-value: 3.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586    32 ILFDVGEGTLRQMEIAgLSPMKIRR-----IFITHFHGDHYLGLPALiqtmnlwKRKEPLHIYGPENSIEFIKNLLNSGY 106
Cdd:pfam12706   3 ILIDPGPDLRQQALPA-LQPGRLRDdpidaVLLTHDHYDHLAGLLDL-------REGRPRPLYAPLGVLAHLRRNFPYLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   107 FAPSFDVTVHELP--GKARLQFEKYEVWAFEVSHGVPalgyvfkekdrrgsfdlekiKNLGLEPGPWmkeleekkvinIG 184
Cdd:pfam12706  75 LLEHYGVRVHEIDwgESFTVGDGGLTVTATPARHGSP--------------------RGLDPNPGDT-----------LG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   185 GRtirlseVTGPKKRgakIVYTGDTEPC-ENVIQFSRRANLLIHEATYLNSEDRGESYHTTVEEACEIWKKSKAFNLALF 263
Cdd:pfam12706 124 FR------IEGPGKR---VYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  .
gi 41017586   264 H 264
Cdd:pfam12706 195 H 195
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-264 9.38e-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: 63.36  E-value: 9.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   4 VIFLGTGGikptpERNVPS--------IAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQ 75
Cdd:cd07741   1 IIFLGTGG-----GRFVVItqlrasggIWIELNGKNIHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDANVLIE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  76 TMNLWKRKEPLHIYGPENSIEfiknllnsgyfapSFDVTVHelpgkarlqfekyevwafevshgvpalgYVFKEKdrrgs 155
Cdd:cd07741  76 AMTEGGFKKRGTLLAPEDALN-------------GEPVVLL----------------------------YYHRRK----- 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 156 fdLEKIKNlglepgpwmkeLEEKKVINIGGRTIRLSEV--TGPKKRGA-------KIVYTGDTEPCENVIQFSRRANLLI 226
Cdd:cd07741 110 --LEEIEI-----------LEEGDEYELGGIKIEATRHkhSDPTTYGFifrtsdkKIGYISDTRYFEELIEYYSNCDVLI 176

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 41017586 227 HEATYLNSedRGESYHTTVEEACEIWKKSKAFNLALFH 264
Cdd:cd07741 177 INVTRPRP--RKGVDHLSVEDVEKILKEIKPKLAILTH 212
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
22-175 8.01e-11

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 61.44  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  22 SIAIKVEGELILFDVGEGT--LRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIqtmnlwKRKEPLHIYGPENSieFIK 99
Cdd:COG1237  24 SALIETEGKRILFDTGQSDvlLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALL------ELNPKAPVYAHPDA--FEK 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 100 NLLNSGYFAP-SFDVTVHELPGK-ARLQFEKYEVWAFEvshGVpalgYVFKEKDRRGSF-----DLEKIKNLGLEPGPWM 172
Cdd:COG1237  96 RYSKRPGGKYiGIPFSREELEKLgARLILVKEPTEIAP---GV----YLTGEIPRVTDFekgdpGLYVKEDGGLVPDPFL 168


                ...
gi 41017586 173 KEL 175
Cdd:COG1237 169 DEQ 171
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 32-153 2.37e-10

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: 58.04  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  32 ILFDVGEG---TLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQTMNLwkrkePlhIYGPENSIEFIKNLLnsgyfA 108
Cdd:cd07733  21 LLIDAGLSgrkITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNV-----P--IYATAGTLRAMERKV-----G 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 41017586 109 PSFDVTVHELPGKARLQFEKYEVWAFEVSH-GVPALGYVFKEKDRR 153
Cdd:cd07733  89 LIDVDQKQIFEPGETFSIGDFDVESFGVSHdAADPVGYRFEEGGRR 134
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 3-152 5.61e-10

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: 58.76  E-value: 5.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   3 EVIFLGT-GGIkptPERNVPSIAIKVEG--ELILFDVGEG----TLRQMEIAGLSPM---------KIRRIFITHFHGDH 66
Cdd:cd07735   2 ELVVLGCsGGP---DEGNTSSFLLDPAGsdGDILLDAGTGvgalSLEEMFNDILFPSqkaayelyqRIRHYLITHAHLDH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  67 YLGLPALIQTMNLWKRKePLHIYGPENSIEFIKNLLNSGYFAPSFD---------VTVHELPGKARLQFEKYEVWAFEVS 137
Cdd:cd07735  79 IAGLPLLSPNDGGQRGS-PKTIYGLPETIDALKKHIFNWVIWPDFTsipsgkypyLRLEPIEPEYPIALTGLSVTAFPVS 157

                       170
                ....*....|....*.
gi 41017586 138 HGVP-ALGYVFKEKDR 152
Cdd:cd07735 158 HGVPvSTAFLIRDGGD 173
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 24-165 5.29e-09

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 55.88  E-value: 5.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  24 AIKVEGELILFDVG-----EGTLR-QMEIAGLSPM-----KIRRIFITHFHGDHYLGLPALIQTMNLwkrkePlhIYGPE 92
Cdd:cd07714  15 VVEYDDDIIIIDCGlkfpdEDMPGvDYIIPDFSYLeenkdKIKGIFITHGHEDHIGALPYLLPELNV-----P--IYATP 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  93 NSIEFIKNLLNSgyFAPSFDVTVHELPGKARLQFEKYEVWAFEVSHGVP-ALGYVFKEKDrrGS---------------- 155
Cdd:cd07714  88 LTLALIKKKLEE--FKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPdSVGLAIKTPE--GTivhtgdfkfdqtpvdg 163

                       170
                ....*....|..
gi 41017586 156 --FDLEKIKNLG 165
Cdd:cd07714 164 kpTDLEKLAELG 175
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-76 3.40e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 52.76  E-value: 3.40e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586    15 TPERNVPSIAIKVEGELILFDVG----EGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQT 76
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGgsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEA 66
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 25-117 2.30e-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: 50.46  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  25 IKVEGELILFDVGEGT------LRQMEIAGLspmKIRRIFITHFHGDHYLGLPALIQTMNlwkrkepLHIYGPENSIEFI 98
Cdd:COG0491  20 IVGGDGAVLIDTGLGPadaealLAALAALGL---DIKAVLLTHLHPDHVGGLAALAEAFG-------APVYAHAAEAEAL 89

                        90       100
                ....*....|....*....|..
gi 41017586  99 KNLLNSGYFA---PSFDVTVHE 117
Cdd:COG0491  90 EAPAAGALFGrepVPPDRTLED 111
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 25-73 2.73e-07

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 50.30  E-value: 2.73e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 41017586  25 IKVEGELILFDVG-----EGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPAL 73
Cdd:cd07721  16 IEDDDGLTLIDTGlpgsaKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAAL 69
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 22-175 4.93e-07

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: 49.93  E-value: 4.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  22 SIAIKVEGELILFDVG-EGTLRQ-MEIAGLSPMKIRRIFITHFHGDHYLGLPALIqtmnlwKRKEPLHIYGPENSIEFIK 99
Cdd:cd07713  22 SLLIETEGKKILFDTGqSGVLLHnAKKLGIDLSDIDAVVLSHGHYDHTGGLKALL------ELNPKAPVYAHPDAFEPRY 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586 100 NLLNSGYFAPSFDVTVHELPGkARLQFEKYEVWAFEvshGVpalgYVFKEKDRRGSF-----DLEKIKNLGLEPGPWMKE 174
Cdd:cd07713  96 SKRGGGKKGIGIGREELEKAG-ARLVLVEEPTEIAP---GV----YLTGEIPRVTDFekgnpGLFVKEDGGLVPDDFEDE 167


                .
gi 41017586 175 L 175
Cdd:cd07713 168 Q 168
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 14-75 1.03e-06

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 48.06  E-value: 1.03e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41017586  14 PTPERNVPSIAIKVEGELILFDVGEGT-------LRQMEIAGLSPMKIRRIFITHFHGDHYlGLPALIQ 75
Cdd:cd07725   9 PGPLGHVNVYLLRDGDETTLIDTGLATeedaealWEGLKELGLKPSDIDRVLLTHHHPDHI-GLAGKLQ 76
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 25-70 1.90e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 48.31  E-value: 1.90e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41017586  25 IKVEGELILFDVGEGT---------LRQMEIAGLSPMKIRRIFITHFHGDHYLGL 70
Cdd:cd07720  54 VRTGGRLILVDTGAGGlfgptagklLANLAAAGIDPEDIDDVLLTHLHPDHIGGL 108
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 28-136 2.37e-06

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: 47.28  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  28 EGELILFDVGEGTLRQ-MEIAGLSPMKIRRIFITHFHGDHYLGLPALiqtmnlwKRKEPLHIYGPENSIEFI----KNLL 102
Cdd:cd06262  19 EGEAILIDPGAGALEKiLEAIEELGLKIKAILLTHGHFDHIGGLAEL-------KEAPGAPVYIHEADAELLedpeLNLA 91

                        90       100       110
                ....*....|....*....|....*....|....
gi 41017586 103 NSGYFAPSFDVTVHELPGKARLQFEKYEVWAFEV 136
Cdd:cd06262  92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHT 125
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
53-148 1.22e-05

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 46.59  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  53 KIRRIFITHFHGDHYLGLPALIQTMNLwkrkePlhIYGPENSIEFIKNLLNSgyFAPSFDVTVHELPGKARLQFEKYEVW 132
Cdd:COG0595  63 KIKGIVLTHGHEDHIGALPYLLKELNV-----P--VYGTPLTLALLEAKLKE--HGLLKKVKLHVVKPGDRIKFGPFKVE 133

                        90
                ....*....|....*..
gi 41017586 133 AFEVSHGVP-ALGYVFK 148
Cdd:COG0595 134 FFRVTHSIPdSLGLAIR 150
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 57-75 4.12e-05

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 43.64  E-value: 4.12e-05
                        10
                ....*....|....*....
gi 41017586  57 IFITHFHGDHYLGLPALIQ 75
Cdd:cd07739  56 IYITHGHPDHYFGLEVLLE 74
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-99 7.74e-05

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: 42.94  E-value: 7.74e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41017586  28 EGELILFDVGeGTLRQME-----IAGLSPMKIRRIFITHFHGDHYLGLPALiqtmnlwkRKEPLHIYGPENSIEFIK 99
Cdd:cd16282  23 DDGVVVIDTG-ASPRLARallaaIRKVTDKPVRYVVNTHYHGDHTLGNAAF--------ADAGAPIIAHENTREELA 90
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 32-103 1.22e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 42.14  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  32 ILFDVGEG------TLRQMeIAGLSPMKIRRIFITHFHGDHYLGLPALIQ-----TMNLWKRKEPLHIYGPENSIEFIKN 100
Cdd:cd07722  30 ILIDTGEGrpsyipLLKSV-LDSEGNATISDILLTHWHHDHVGGLPDVLDllrgpSPRVYKFPRPEEDEDPDEDGGDIHD 108


                ...
gi 41017586 101 LLN 103
Cdd:cd07722 109 LQD 111
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 22-77 1.84e-04

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 42.15  E-value: 1.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41017586  22 SIAIKV-EGELILFDVGEGTLRQMEIAGLSP----MKIRRI---FITHFHGDHYLGLPALIQTM 77
Cdd:COG2333  13 AILIRTpDGKTILIDTGPRPSFDAGERVVLPylraLGIRRLdllVLTHPDADHIGGLAAVLEAF 76
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-67 1.92e-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) 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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 42.19  E-value: 1.92e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586  18 RNVPSIAIKVEGELILFDVG-----EGTLRQ-MEIAGLSPMKIRRIFITHFHGDHY 67
Cdd:cd16280  20 KWVSAWAIDTGDGLILIDALnnneaADLIVDgLEKLGLDPADIKYILITHGHGDHY 75
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 29-120 1.41e-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: 38.60  E-value: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586  29 GELILFDVGEGT--LRQMEIAGLspmKIRRIFITHFHGDHYLGLPALIqtmnlwKRKEPLHIYGPENS-IEFIKNLLNSG 105
Cdd:cd07723  20 GEAAVVDPGEAEpvLAALEKNGL---TLTAILTTHHHWDHTGGNAELK------ALFPDAPVYGPAEDrIPGLDHPVKDG 90

                        90
                ....*....|....*..
gi 41017586 106 --YFAPSFDVTVHELPG 120
Cdd:cd07723  91 deIKLGGLEVKVLHTPG 107
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 22-78 1.82e-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: 38.65  E-value: 1.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41017586  22 SIAIKVEGELILFDVG--EGTLRQMEIAGLSPMKIRRI---FITHFHGDHYLGLPALIQTMN 78
Cdd:cd07731  12 AILIQTPGKTILIDTGprDSFGEDVVVPYLKARGIKKLdylILTHPDADHIGGLDAVLKNFP 73
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 3-120 2.20e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 38.34  E-value: 2.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   3 EVIFLGTGGIKPTPERNVPSIA----IKVEGELILFDVG-----EGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLpal 73
Cdd:cd07711   1 EVKVLVEGYARRDSDGGFRASStvtlIKDGGKNILVDTGtpwdrDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNL--- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 41017586  74 iqtmNLWKRKEplHIYGPENSIE--FIKNLLNSGYFAPSFDVTVHELPG 120
Cdd:cd07711  78 ----NLFPNAT--VIVGWDICGDsyDDHSLEEGDGYEIDENVEVIPTPG 120
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 28-75 3.11e-03

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 38.24  E-value: 3.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41017586  28 EGELILFDVG-----EGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALIQ 75
Cdd:cd07726  24 EGRPALIDTGpsssvPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAE 76
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 11-66 3.28e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.40  E-value: 3.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41017586  11 GIKPTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDH 66
Cdd:cd07730  41 GYRKDFEEYTPRVPERLYRTPVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDH 96
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 6-74 8.32e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 36.50  E-value: 8.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41017586   6 FLGTG-GIkpTPERNVPSIAIKVEGELILFDVGEGTLRQMEIAGLSPMKIRRIFITHFHGDHYLGLPALI 74
Cdd:cd07738   2 FLGVShGF--DPKGHTSGFIIWINGRGIMVDPPVNSTSYLRQNGISPRLVDHVILTHCHADHDAGTFQKI 69
 
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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