NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446341237|ref|WP_000419092|]
View 

MULTISPECIES: ribonuclease BN [Salmonella]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 3-305 0e+00

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


The actual alignment was detected with superfamily member TIGR02649:

Pssm-ID: 451500  Cd Length: 303  Bit Score: 627.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    3 LIFLGTSAGVPTRSRNVTAILLHLQHPTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   83 AGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGALNAR 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  163 ALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446341237  243 ANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGCQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
 
Name Accession Description Interval E-value
true_RNase_BN TIGR02649
ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 ...
 3-305 0e+00

ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN. [Transcription, RNA processing]


Pssm-ID: 131697  Cd Length: 303  Bit Score: 627.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    3 LIFLGTSAGVPTRSRNVTAILLHLQHPTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   83 AGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGALNAR 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  163 ALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446341237  243 ANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGCQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 1.74e-138

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 392.24  E-value: 1.74e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLHLQHptqpGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGG----ELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  81 SMAGNPHPLTVYGPQGVREFIATTLRLSGSwtdfplqieeisagdilddglrkvtafrlehplecYGYRVVEHDKPGALN 160
Cdd:PRK00055  78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 ARALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDkGCQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG-DPEELLKEAREIFPNTELAEDLMRVEV 266
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 2.09e-117

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: 337.88  E-value: 2.09e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   3 LIFLGTSAGVPTRSRNVTAILLHLQHPtqpgVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE----LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  83 AGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISA--GDILDDGLRKVTAFRLEHPLECYGYRVVEhdkpgaln 160
Cdd:cd07717   77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPdpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 aralkaagvtpgplfqalkagktvtladgrqingadylapavaGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:cd07717  149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDkgCQRLLAECRAIFPATELAYDFSVFP 304
Cdd:cd07717  186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.05e-100

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 295.57  E-value: 1.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLhlQHPTQpgVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLL--EAGGE--RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  81 SMAGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEhdkpgaln 160
Cdd:COG1234   77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 aralkaagvtpgplfqalkagktvtladgrqingadylapavAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKgcQRLLAECRAIFPA-TELAYDFSVFPV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDP--EELLAEARAVFPGpVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-96 5.58e-16

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 77.36  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLHLQHPtQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNG-ERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                         90
                 ....*....|....*.
gi 446341237  81 SMAGNPHPLTVYGPQG 96
Cdd:NF041257  92 AWSGRWTPLRVWGPSG 107
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-271 5.87e-13

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 66.18  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   36 LFDCGEGTQHQMLNtAFHPGKLER-----IFISHLHGDHLFGLPGLLCSRsmagnphPLTVYGPQGVREFIATTLRLSGS 110
Cdd:pfam12706   4 LIDPGPDLRQQALP-ALQPGRLRDdpidaVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  111 WTDFPLQIEEISAGDI--LDDGLRKVTAFRLEH---------PLECYGYRVvehdkpgalnaralkaagvtpgplfqalk 179
Cdd:pfam12706  76 LEHYGVRVHEIDWGESftVGDGGLTVTATPARHgsprgldpnPGDTLGFRI----------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  180 agktvtladgrqingadylapAVAGKSVAIFGDTAPC-EAAFALAQGVDVMVHETTLDASMEEKANarGHSSTRQTATLA 258
Cdd:pfam12706 127 ---------------------EGPGKRVYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAA 183

                         250
                  ....*....|...
gi 446341237  259 REAAVGRLIMTHI 271
Cdd:pfam12706 184 ADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 33-139 9.16e-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: 56.79  E-value: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    33 GVWLFDCGEGTQHQMLNT--AFHPGKLERIFISHLHGDHLFGLPGLLcSRSMAgnphplTVYGPQGVREFIATTLRLSGS 110
Cdd:smart00849  10 GAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL-EAPGA------PVYAPEGTAELLKDLLALLGE 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 446341237   111 WTDF---PLQIEEISAGDILDDGLRKVTAFRL 139
Cdd:smart00849  83 LGAEaepAPPDRTLKDGDELDLGGGELEVIHT 114
 
Name Accession Description Interval E-value
true_RNase_BN TIGR02649
ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 ...
 3-305 0e+00

ribonuclease BN; Members of this protein family are ribonuclease BN of Escherichia coli K-12 and closely related proteins believed to be equivalent in function. Note that E. coli appears to lack RNase Z per se, and this protein of E. coli appears orthologous to (but not functionally equivalent to) RNase Z of Bacillus subtilis and various other species. Meanwhile, the yihY gene product of E. coli previously was incorrectly identified as RNase BN. [Transcription, RNA processing]


Pssm-ID: 131697  Cd Length: 303  Bit Score: 627.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    3 LIFLGTSAGVPTRSRNVTAILLHLQHPTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:TIGR02649   1 LIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   83 AGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGALNAR 162
Cdd:TIGR02649  81 SGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  163 ALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASMEEK 242
Cdd:TIGR02649 161 ALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446341237  243 ANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGCQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:TIGR02649 241 ANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV 303
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-305 1.74e-138

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 392.24  E-value: 1.74e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLHLQHptqpGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGG----ELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  81 SMAGNPHPLTVYGPQGVREFIATTLRLSGSwtdfplqieeisagdilddglrkvtafrlehplecYGYRVVEHDKPGALN 160
Cdd:PRK00055  78 SLSGRTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------LGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 ARALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDkGCQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG-DPEELLKEAREIFPNTELAEDLMRVEV 266
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-305 1.17e-135

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: 386.19  E-value: 1.17e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    2 ELIFLGTSAGVPTRSRNVTAILLHLqhptqPG-VWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-----NGeLWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   81 SMAGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGD-ILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGAL 159
Cdd:TIGR02651  76 SFQGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGlVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  160 NARALKAAGVTPGPLFQALKAGKTVTLADGRQINGADYLAPAVAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASM 239
Cdd:TIGR02651 156 DREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDED 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446341237  240 EEKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKgcQRLLAECRAIFPATELAYDFSVFPV 305
Cdd:TIGR02651 236 KKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDE--EELLEEAKKIFPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-304 2.09e-117

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: 337.88  E-value: 2.09e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   3 LIFLGTSAGVPTRSRNVTAILLHLQHPtqpgVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGE----LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  83 AGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISA--GDILDDGLRKVTAFRLEHPLECYGYRVVEhdkpgaln 160
Cdd:cd07717   77 LGRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPdpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 aralkaagvtpgplfqalkagktvtladgrqingadylapavaGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:cd07717  149 -------------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDA 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDkgCQRLLAECRAIFPATELAYDFSVFP 304
Cdd:cd07717  186 EKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.05e-100

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 295.57  E-value: 1.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLhlQHPTQpgVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLL--EAGGE--RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  81 SMAGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEhdkpgaln 160
Cdd:COG1234   77 SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 161 aralkaagvtpgplfqalkagktvtladgrqingadylapavAGKSVAIFGDTAPCEAAFALAQGVDVMVHETTLDASME 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446341237 241 EKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKgcQRLLAECRAIFPA-TELAYDFSVFPV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDP--EELLAEARAVFPGpVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-232 2.14e-51

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: 167.44  E-value: 2.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   3 LIFLGTSAGVPTRSRNVTAILLhlqhPTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSM 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLL----ETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  83 AGNPHPLTVYGPQGVREFIATTLR--LSGSWTDFPLQIEEI-SAGDILDDGLRKVTAFRLEHPLECYGYRVVEHdkpgal 159
Cdd:cd16272   77 GGRKKPLTIYGPKGIKEFLEKLLNfpVEILPLGFPLEIEELeEGGEVLELGDLKVEAFPVKHSVESLGYRIEAE------ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446341237 160 naralkaagvtpgplfqalkagktvtladgrqingadylapavaGKSVAIFGDTAPCEAAFALAQGVDVMVHE 232
Cdd:cd16272  151 --------------------------------------------GKSIVYSGDTGPCENLVELAKGADLLIHE 179
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-231 2.44e-35

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: 126.09  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   2 ELIFLGTSAGVPTRSRNVTAILLhlQHPTQpgVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRS 81
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLV--VVGGR--VYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  82 MAGNPHPLTVYGPQGVREFIATTL---------RLSGSWTDFP-----LQIEEISAGDIL--DDGLRkVTAFRLEHP--L 143
Cdd:cd07719   77 LAGRKTPLPVYGPPGTRALVDGLLaayaldidyRARIGDEGRPdpgalVEVHEIAAGGVVyeDDGVK-VTAFLVDHGpvP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 144 ECYGYRVvehdkpgalnaralkaagvtpgplfqalkagktvtladgrqingaDYlapavAGKSVAIFGDTAPCEAAFALA 223
Cdd:cd07719  156 PALAYRF---------------------------------------------DT-----PGRSVVFSGDTGPSENLIELA 185


                 ....*...
gi 446341237 224 QGVDVMVH 231
Cdd:cd07719  186 KGADLLVH 193
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-234 4.53e-32

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: 118.03  E-value: 4.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   3 LIFLGTSAGVPTRSRNVTAILLHLQHPtqpGVWLFDCGEGTQHQMLnTAFHPGKLER-------IFISHLHGDHLFGLPG 75
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGD---GSILLDCGEGTLGQLR-RHYGPEEADEvlrnlkcIFISHLHADHHLGLIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  76 LLCSRSMA--GNPHPLTVYGPQGVREFI---------------ATTLRLSGSWTDFPLQIEEISAGDILDD-GLRKVTAF 137
Cdd:cd07718   77 LLAERKKLfkPPSPPLYVVAPRQLRRWLreyssledlglhdisFISNRVSQSLPESDDPLSRDLLSNLLEElGLKSIETV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 138 RLEHPLECYGYrVVEHDKpgalnaralkaagvtpgplfqalkagktvtladgrqingadylapavaGKSVAIFGDTAPCE 217
Cdd:cd07718  157 PVIHCPDAYGI-VLTHED------------------------------------------------GWKIVYSGDTRPCE 187

                        250
                 ....*....|....*..
gi 446341237 218 AAFALAQGVDVMVHETT 234
Cdd:cd07718  188 ALVEAGKGADLLIHEAT 204
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-305 7.32e-32

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 118.84  E-value: 7.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGT--SAGVP--------------TRSRNVTAILLHlqhpTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISH 64
Cdd:COG1235    1 MKVTFLGSgsSGGVPqigcdcpvcastdpRYGRTRSSILVE----ADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  65 LHGDHLFGLPGLlcsrSMAGNPHPLTVYGPQGVREFIATTLRLSGSWTDFPLQIEEISAGDILD-DGLRkVTAFRLEHP- 142
Cdd:COG1235   77 EHADHIAGLDDL----RPRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEiGGLT-VTPFPVPHDa 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 143 LECYGYRvVEHDkpgalnaralkaagvtpgplfqalkagktvtladgrqingadylapavaGKSVAIFGDTAP-CEAAFA 221
Cdd:COG1235  152 GDPVGYR-IEDG-------------------------------------------------GKKLAYATDTGYiPEEVLE 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 222 LAQGVDVMVHETTLDASMEekanarGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGCQRLLAECRAIFPATELAYDFS 301
Cdd:COG1235  182 LLRGADLLILDATYDDPEP------GHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGM 255


                 ....
gi 446341237 302 VFPV 305
Cdd:COG1235  256 EIEL 259
PRK02126 PRK02126
ribonuclease Z; Provisional
 36-293 4.53e-25

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 102.30  E-value: 4.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  36 LFDCGEgtqhqmlNTAFHPGKLER---IFISHLHGDHLFGLPGLLcsRSMAGNPHPLTVYGPQGVREFIATtlRLSG--- 109
Cdd:PRK02126  31 LFDLGD-------LHHLPPRELLRishIFVSHTHMDHFIGFDRLL--RHCLGRPRRLRLFGPPGFADQVEH--KLAGytw 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 110 -----SWTDF--------------------------PLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGA 158
Cdd:PRK02126 100 nlvenYPTTFrvhevelhdgrirralfscrrafareAEEELSLPDGVLLDEPWFRVRAAFLDHGIPCLAFALEEKAHINI 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 159 LNARaLKAAGVTPGPLFQALKAG----------KTVTLADGRQINGADYLAPA--------VAGKSVAIFGDTAPCEAAF 220
Cdd:PRK02126 180 DKNR-LAELGLPPGPWLRELKHAvlrgepddtpIRVLWRDGGGEHERVRPLGElkervlriEPGQKIGYVTDIGYTEENL 258

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446341237 221 A----LAQGVDVMVHETTLDASMEEKANARGHSSTRQTATLAREAAVGRLIMTHISSRYDDKGcQRLLAECRAIFPA 293
Cdd:PRK02126 259 AriveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRG-AELYREARAAFAG 334
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-232 1.98e-21

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: 89.63  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   4 IFLGTSAGVPTRSRNVTAilLHLQhpTQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCS-RSM 82
Cdd:cd07740    1 TFLGSGDAFGSGGRLNTC--FHVA--SEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDaQFV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  83 AGNPHPLTVYGPQGVREFI--ATTLRLSGSWT---DFPLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVvehdkpg 157
Cdd:cd07740   77 AKRTRPLTIAGPPGLRERLrrAMEALFPGSSKvprRFDLEVIELEPGEPTTLGGVTVTAFPVVHPSGALPLAL------- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446341237 158 alnaralkaagvtpgplfqalkagktvtladgrqingadYLAPavAGKSVAIFGDTAPCEAAFALAQGVDVMVHE 232
Cdd:cd07740  150 ---------------------------------------RLEA--AGRVLAYSGDTEWTDALVPLARGADLFICE 183
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 36-155 4.34e-16

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: 74.40  E-value: 4.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  36 LFDCGEGTQHQMLNTAfHPGKLERIFISHLHGDHLFGLPGLLCSRSMA---GNPHPLTVYGPQGVREFIATTLRLSGSwt 112
Cdd:cd07716   31 LLDCGSGVLSRLQRYI-DPEDLDAVVLSHLHPDHCADLGVLQYARRYHprgARKPPLPLYGPAGPAERLAALYGLEDV-- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446341237 113 dfpLQIEEISAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDK 155
Cdd:cd07716  108 ---FDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGK 147
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
1-96 5.58e-16

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 77.36  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPTRSRNVTAILLHLQHPtQPGVWLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSR 80
Cdd:NF041257  13 MRITFLGSGPPPPRRGQANTSILVELGNG-ERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPFG 91

                         90
                 ....*....|....*.
gi 446341237  81 SMAGNPHPLTVYGPQG 96
Cdd:NF041257  92 AWSGRWTPLRVWGPSG 107
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-271 5.87e-13

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 66.18  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   36 LFDCGEGTQHQMLNtAFHPGKLER-----IFISHLHGDHLFGLPGLLCSRsmagnphPLTVYGPQGVREFIATTLRLSGS 110
Cdd:pfam12706   4 LIDPGPDLRQQALP-ALQPGRLRDdpidaVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  111 WTDFPLQIEEISAGDI--LDDGLRKVTAFRLEH---------PLECYGYRVvehdkpgalnaralkaagvtpgplfqalk 179
Cdd:pfam12706  76 LEHYGVRVHEIDWGESftVGDGGLTVTATPARHgsprgldpnPGDTLGFRI----------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  180 agktvtladgrqingadylapAVAGKSVAIFGDTAPC-EAAFALAQGVDVMVHETTLDASMEEKANarGHSSTRQTATLA 258
Cdd:pfam12706 127 ---------------------EGPGKRVYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHM--GHMTPEEAVEAA 183

                         250
                  ....*....|...
gi 446341237  259 REAAVGRLIMTHI 271
Cdd:pfam12706 184 ADLGARRKVLIHI 196
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-150 8.76e-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: 62.88  E-value: 8.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGT--SAGVPT----------------RSRnvTAILLHLQHptqpGVWLFDCGEGTQHQMLntAFHPGKLERIFI 62
Cdd:cd16279    1 MKLTFLGTgtSSGVPVigcdcgvcdssdpknrRLR--SSILIETGG----KNILIDTGPDFRQQAL--RAGIRKLDAVLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  63 SHLHGDHLFGLPGL--LCSRsmagNPHPLTVYGPQGVREFIATTL------RLSGSWTDFPLQI----EEISAGDIlddg 130
Cdd:cd16279   73 THAHADHIHGLDDLrpFNRL----QQRPIPVYASEETLDDLKRRFpyffaaTGGGGVPKLDLHIiepdEPFTIGGL---- 144

                        170       180
                 ....*....|....*....|.
gi 446341237 131 lrKVTAFRLEH-PLECYGYRV 150
Cdd:cd16279  145 --EITPLPVLHgKLPSLGFRF 163
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 33-139 9.16e-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: 56.79  E-value: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237    33 GVWLFDCGEGTQHQMLNT--AFHPGKLERIFISHLHGDHLFGLPGLLcSRSMAgnphplTVYGPQGVREFIATTLRLSGS 110
Cdd:smart00849  10 GAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELL-EAPGA------PVYAPEGTAELLKDLLALLGE 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 446341237   111 WTDF---PLQIEEISAGDILDDGLRKVTAFRL 139
Cdd:smart00849  83 LGAEaepAPPDRTLKDGDELDLGGGELEVIHT 114
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 60-248 3.68e-09

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 55.58  E-value: 3.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  60 IFISHLHGDHLFGLP---GLLCSRSMagnphpLTVYGPQGVREFIATTLR--LSGSWtdFPLQIEEISAGDILDD----- 129
Cdd:cd07715   61 LLLSHTHWDHIQGFPffaPAYDPGNR------IHIYGPHKDGGSLEEVLRrqMSPPY--FPVPLEELLAAIEFHDlepge 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 130 -----GLRkVTAFRLEHPLECYGYRvVEHDkpgalnaralkaagvtpgplfqalkagktvtladgrqingadylapavaG 204
Cdd:cd07715  133 pfsigGVT-VTTIPLNHPGGALGYR-IEED-------------------------------------------------G 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446341237 205 KSVAIFGDT-------APCEAAFALAQGVDVMVHETT-LDASMEEKANaRGH 248
Cdd:cd07715  162 KSVVYATDTehypddgESDEALLEFARGADLLIHDAQyTDEEYPSKRG-WGH 212
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-155 2.09e-08

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: 54.14  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVPtrSRNVTAILLHlqHPTQPGVWLFDCGEG----TQHQMLNTAFHPG---------KLERIFISHLHG 67
Cdd:cd07735    1 FELVVLGCSGGPD--EGNTSSFLLD--PAGSDGDILLDAGTGvgalSLEEMFNDILFPSqkaayelyqRIRHYLITHAHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  68 DHLFGLPglLCSRSMAGNP-HPLTVYGPQGVREFIATTLrLSGS-WTDFP---------LQIEEISAGDILDDGLRKVTA 136
Cdd:cd07735   77 DHIAGLP--LLSPNDGGQRgSPKTIYGLPETIDALKKHI-FNWViWPDFTsipsgkypyLRLEPIEPEYPIALTGLSVTA 153

                        170       180
                 ....*....|....*....|
gi 446341237 137 FRLEHP-LECYGYRvVEHDK 155
Cdd:cd07735  154 FPVSHGvPVSTAFL-IRDGG 172
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-270 9.93e-07

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 48.73  E-value: 9.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   3 LIFLGTSAGvptrsRNVTA--------ILLHLqhptqPGVWLF-DCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGL 73
Cdd:cd07741    1 IIFLGTGGG-----RFVVItqlrasggIWIEL-----NGKNIHiDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  74 PGLLCSRSMAGNPHPLTVYGPQ----GVREFIATTLRlsgswtDFPLQIEEISAGDILDDGLRKVTAFRLEHPLE-CYGY 148
Cdd:cd07741   71 NVLIEAMTEGGFKKRGTLLAPEdalnGEPVVLLYYHR------RKLEEIEILEEGDEYELGGIKIEATRHKHSDPtTYGF 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 149 RvvehdkpgalnaralkaagvtpgplFQAlkagktvtladgrqingadylapavAGKSVAIFGDTAPCEAAFALAQGVDV 228
Cdd:cd07741  145 I-------------------------FRT-------------------------SDKKIGYISDTRYFEELIEYYSNCDV 174

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446341237 229 MVHETTLdasmEEKANARGHSSTRQTATLAREAAVGRLIMTH 270
Cdd:cd07741  175 LIINVTR----PRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-155 3.46e-06

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: 46.46  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGT--SAGVPT---------RSRNVT--------AILLHLQhptqpGVWLFDCGegtqHQMLNTAFHPGKLERIF 61
Cdd:cd07736    1 MKLTFLGTgdAGGVPVygcdcsacqRARQDPsyrrrpcsALIEVDG-----ERILLDAG----LTDLAERFPPGSIDAIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  62 ISHLHGDHLFGLPGLlcsRsmAGNPHPLTVYGPQ------------GVREFIATTlrlsgswTDFplqiEEISAGDIldd 129
Cdd:cd07736   72 LTHFHMDHVQGLFHL---R--WGVGDPIPVYGPPdpqgcadlfkhpGILDFQPLV-------APF----QSFELGGL--- 132

                        170       180
                 ....*....|....*....|....*.
gi 446341237 130 glrKVTAFRLEHPLECYGYrVVEHDK 155
Cdd:cd07736  133 ---KITPLPLNHSKPTFGY-LLESGG 154
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 33-137 1.37e-05

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: 44.97  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  33 GVWLFDCGEGTQHQMLNTAF-HPGKLERIFISHLHGDHLFGLPGLLcsrsmagNPHPLTVYGPQGVREFI----ATTLRL 107
Cdd:cd06262   21 EAILIDPGAGALEKILEAIEeLGLKIKAILLTHGHFDHIGGLAELK-------EAPGAPVYIHEADAELLedpeLNLAFF 93

                         90       100       110
                 ....*....|....*....|....*....|
gi 446341237 108 SGSWTDFPLQIEEISAGDILDDGLRKVTAF 137
Cdd:cd06262   94 GGGPLPPPEPDILLEDGDTIELGGLELEVI 123
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
1-154 3.01e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 41.87  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237   1 MELIFLGTSAGVptRSRNVTAILLhlQHPTQPGVWLFDCGEGT-------QHQMLNTAfHPGKLERI---FISHLHGDHL 70
Cdd:COG5212   12 MEVRVLGCSGGI--SDGNLTTYLL--RPLGSDDYVLLDAGTVVsglelaeQKGAFKGR-QGYVLEHIkgyLISHAHLDHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  71 FGLPGLLCSRSmagnphPLTVYGPQGVREFIATTLRLSGSWTDFP----------LQIEEISAGD---ILDDGLRkVTAF 137
Cdd:COG5212   87 AGLPILSPDDS------PKTIYALPETIDALRNHYFNWVIWPDFTdigsaphlpkYRYVPLKPGQtfpLGGTGLR-VTAF 159

                        170
                 ....*....|....*..
gi 446341237 138 RLEHPLECYGYrVVEHD 154
Cdd:COG5212  160 PLSHSVPSSAF-LIESG 175
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-76 3.16e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.10  E-value: 3.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446341237   1 MELIFLGtSAGVPTRSrnvtAILLhlqhPTQPGVWLFDCGEGTQHQMLNTA---FHPGKLERIFISHLHGDHLFGLPGL 76
Cdd:COG1236    1 MKLTFLG-AAGEVTGS----CYLL----ETGGTRILIDCGLFQGGKERNWPpfpFRPSDVDAVVLTHAHLDHSGALPLL 70
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 35-204 5.79e-04

Ribonuclease Z, N-terminus of human 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 the N-terminus of human ELAC2 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: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 39.94  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  35 WLFDCGEGTQHQMLNTAFHPGKLERIFISHLHGDHLFGLPGLLCSRSMAGNPHPLtvygpqgvrefiattlrLSGSWTDF 114
Cdd:cd16296   24 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-----------------LSGPNKQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237 115 PLQIEeiSAGDILDDGLRKVTAFRLEHPLECYGYRVVEHDKPGalnaraLKAAGVTPGPLFQALKAGKTVTLaDGRQING 194
Cdd:cd16296   87 PDKIG--VRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELG------LPVGTAAIAPIIAAVKDGKSITF-EGREILA 157

                        170
                 ....*....|
gi 446341237 195 ADYLAPAVAG 204
Cdd:cd16296  158 EELCTPPDPG 167
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-77 4.01e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 37.73  E-value: 4.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446341237   36 LFDCGEGTQHQML----NTAFHPGKLERIFISHLHGDHLFGLPGLL 77
Cdd:pfam00753  19 LIDTGGSAEAALLlllaALGLGPKDIDAVILTHGHFDHIGGLGELA 64
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 33-137 5.06e-03

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 37.36  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341237  33 GVWLFDCG-EGTQHQMLNTAF--HPGKLERIFISHLHGDHLFGLpGLLCSRSMAgnphplTVYGPQGVREFIATTLRLSG 109
Cdd:COG0491   25 GAVLIDTGlGPADAEALLAALaaLGLDIKAVLLTHLHPDHVGGL-AALAEAFGA------PVYAHAAEAEALEAPAAGAL 97

                         90       100
                 ....*....|....*....|....*...
gi 446341237 110 SWTDFPLQIEEISAGDILDDGLRKVTAF 137
Cdd:COG0491   98 FGREPVPPDRTLEDGDTLELGGPGLEVI 125
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-77 5.47e-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) 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: 37.48  E-value: 5.47e-03
                         10        20
                 ....*....|....*....|..
gi 446341237  56 KLERIFISHLHGDHLFGLPGLL 77
Cdd:cd07739   52 TLTTIYITHGHPDHYFGLEVLL 73
 
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