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Conserved domains on  [gi|489715660|ref|WP_003619785|]
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ribonuclease Z [Lactobacillus delbrueckii]

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 ...
 2-305 3.85e-146

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: 412.77  E-value: 3.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660    2 ELEFLGTCSGQPSKLRNVSSLALKLLdelNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   82 QGDVGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEGGKIVSERGFEVYTEKLDHRIDSWGFRMVEADKAGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  162 DKLAEFKVPNGPLLGKLKRGEQVELADGTVLNGKDFLGPAKKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEGK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489715660  242 LARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPATTLAKDLDKFVV 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSD--EEELLEEAKKIFPNTYIAEDFMEIEI 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 ...
 2-305 3.85e-146

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: 412.77  E-value: 3.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660    2 ELEFLGTCSGQPSKLRNVSSLALKLLdelNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   82 QGDVGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEGGKIVSERGFEVYTEKLDHRIDSWGFRMVEADKAGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  162 DKLAEFKVPNGPLLGKLKRGEQVELADGTVLNGKDFLGPAKKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEGK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489715660  242 LARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPATTLAKDLDKFVV 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSD--EEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-306 1.59e-123

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 354.49  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGTCSGQPSKLRNVSSLALKLLDELneiWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  81 FQGDVGPLTIYGPAGIEQFVKTSLRISktkisypikfvtleeggkivsergfevytekldhriDSWGFRMVEADKAGELL 160
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETLLRAS------------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 161 MDKLAEFKVPNGPLLGKLKRGEQVELADGTVLNGKDFLGPAKKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEG 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715660 241 KLARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGSLaSQMVKQAREIFPATTLAKDLDKFVVP 306
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP-EELLKEAREIFPNTELAEDLMRVEVP 267
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-303 1.02e-111

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: 323.63  E-value: 1.02e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   5 FLGTCSGQPSKLRNVSSLALKLLDElneIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQGD 84
Cdd:cd07717    3 FLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  85 VGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEG-GKIVSERGFEVYTEKLDHRIDSWGFRMVEadkagellmdk 163
Cdd:cd07717   80 TEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE----------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 164 laefkvpngpllgklkrgeqveladgtvlngkdflgpakkGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEGKLA 243
Cdd:cd07717  149 ----------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKA 188

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 244 RDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPATTLAKDLDKF 303
Cdd:cd07717  189 KETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.47e-92

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 275.15  E-value: 1.47e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGTCSGQPSKLRNVSSLalkLLDELNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  81 FQGDVGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEgGKIVSERGFEVYTEKLDHRIDSWGFRMVEadkagell 160
Cdd:COG1234   78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP-GEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 161 mdklaefkvpngpllgklkrgeqveladgtvlngkdflgpakKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEG 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715660 241 KLARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPA-TTLAKDLDKFVV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD--PEELLAEARAVFPGpVELAEDGMVIEL 250
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-135 5.22e-10

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 57.56  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660    31 NEIWLFDCGEATQHQILRT--NIRLRKITKIFISHNHGDHIFGLPGLLSTRsfqgdvgPLTIYGPAGIEQFVKTSLRISK 108
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLEAP-------GAPVYAPEGTAELLKDLLALLG 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 489715660   109 TKISY---PIKFVTLEEGGKI-VSERGFEVY 135
Cdd:smart00849  82 ELGAEaepAPPDRTLKDGDELdLGGGELEVI 112
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 35-270 1.95e-08

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: 53.47  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   35 LFDCGEATQHQILRTN----IRLRKITKIFISHNHGDHIFGLPGLLSTRsfqgdvgPLTIYGPAGIEQFVKTSLRISKTK 110
Cdd:pfam12706   4 LIDPGPDLRQQALPALqpgrLRDDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  111 ISYPIKFVTLEEGGKivsergFEVYTEKLDhridswgFRMVEAdkagelLMDKLAEFKVPNGPLLGklkrgeqVELADGt 190
Cdd:pfam12706  77 EHYGVRVHEIDWGES------FTVGDGGLT-------VTATPA------RHGSPRGLDPNPGDTLG-------FRIEGP- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  191 vlngkdflgpakkGRVVTVIYDTRSTP-SIRRLADHADVLVHEATFDASEGKLarDYYHSTCTQAAETASACHVGHLYLT 269
Cdd:pfam12706 130 -------------GKRVYYAGDTGYFPdEIGERLGGADLLLLDGGAWRDDEMI--HMGHMTPEEAVEAAADLGARRKVLI 194


                  .
gi 489715660  270 H 270
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 ...
 2-305 3.85e-146

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: 412.77  E-value: 3.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660    2 ELEFLGTCSGQPSKLRNVSSLALKLLdelNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSF 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLN---GELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   82 QGDVGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEGGKIVSERGFEVYTEKLDHRIDSWGFRMVEADKAGELLM 161
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  162 DKLAEFKVPNGPLLGKLKRGEQVELADGTVLNGKDFLGPAKKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEGK 241
Cdd:TIGR02651 158 EKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489715660  242 LARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPATTLAKDLDKFVV 305
Cdd:TIGR02651 238 LAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSD--EEELLEEAKKIFPNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-306 1.59e-123

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 354.49  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGTCSGQPSKLRNVSSLALKLLDELneiWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRS 80
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL---FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  81 FQGDVGPLTIYGPAGIEQFVKTSLRISktkisypikfvtleeggkivsergfevytekldhriDSWGFRMVEADKAGELL 160
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETLLRAS------------------------------------GSLGYRIAEKDKPGKLD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 161 MDKLAEFKVPNGPLLGKLKRGEQVELADGTVLNGKDFLGPAKKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEG 240
Cdd:PRK00055 123 AEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715660 241 KLARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGSLaSQMVKQAREIFPATTLAKDLDKFVVP 306
Cdd:PRK00055 203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP-EELLKEAREIFPNTELAEDLMRVEVP 267
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-303 1.02e-111

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: 323.63  E-value: 1.02e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   5 FLGTCSGQPSKLRNVSSLALKLLDElneIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQGD 84
Cdd:cd07717    3 FLGTGSAVPTPERNLSSIALRLEGE---LWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  85 VGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEG-GKIVSERGFEVYTEKLDHRIDSWGFRMVEadkagellmdk 163
Cdd:cd07717   80 TEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDpGLVFEDDGFTVTAFPLDHRVPCFGYRFEE----------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 164 laefkvpngpllgklkrgeqveladgtvlngkdflgpakkGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEGKLA 243
Cdd:cd07717  149 ----------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKA 188

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 244 RDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPATTLAKDLDKF 303
Cdd:cd07717  189 KETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKD--PEELLKEARAVFPNTILAEDFMTI 246
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-305 1.47e-92

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 275.15  E-value: 1.47e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGTCSGQPSKLRNVSSLalkLLDELNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRS 80
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSY---LLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  81 FQGDVGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEgGKIVSERGFEVYTEKLDHRIDSWGFRMVEadkagell 160
Cdd:COG1234   78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP-GEVFEIGGFTVTAFPLDHPVPAYGYRFEE-------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 161 mdklaefkvpngpllgklkrgeqveladgtvlngkdflgpakKGRVVTVIYDTRSTPSIRRLADHADVLVHEATFDASEG 240
Cdd:COG1234  149 ------------------------------------------PGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEA 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715660 241 KLARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGslASQMVKQAREIFPA-TTLAKDLDKFVV 305
Cdd:COG1234  187 ELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD--PEELLAEARAVFPGpVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-233 3.87e-41

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: 140.86  E-value: 3.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   3 LEFLGTCSGQPSKLRNVSSLalkLLDELNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQ 82
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSY---LLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  83 GDVGPLTIYGPAGIEQFVKTSLRISKT--KISYPIKFVTLEEGGKIVSERGFEVYTEKLDHRIDSWGFRMVEADKagell 160
Cdd:cd16272   78 GRKKPLTIYGPKGIKEFLEKLLNFPVEilPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGK----- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489715660 161 mdklaefkvpngpllgklkrgeqveladgtvlngkdflgpakkgrvvTVIY--DTRSTPSIRRLADHADVLVHEA 233
Cdd:cd16272  153 -----------------------------------------------SIVYsgDTGPCENLVELAKGADLLIHEC 180
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 5-234 7.67e-26

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: 101.86  E-value: 7.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   5 FLGTCSGQPSKLRNVSSLALKLLDELNeIwLFDCGEATQHQILR------TNIRLRKITKIFISHNHGDHIFGLPGLLST 78
Cdd:cd07718    3 FLGTGSAIPSKYRNVSGILLRIPGDGS-I-LLDCGEGTLGQLRRhygpeeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  79 RS--FQGDVGPLTIYGPAGIEQFVKTSLRISkTKISYPIKFVTLEEGGKIVSER----------------GFEVYTEKLD 140
Cdd:cd07718   81 RKklFKPPSPPLYVVAPRQLRRWLREYSSLE-DLGLHDISFISNRVSQSLPESDdplsrdllsnlleelgLKSIETVPVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 141 HRIDSWGFRMveadkagellmdklaefkvpngpllgklkrgeqvELADGtvlngkdflgpakkGRVVtviY--DTRSTPS 218
Cdd:cd07718  160 HCPDAYGIVL----------------------------------THEDG--------------WKIV---YsgDTRPCEA 188

                        250
                 ....*....|....*.
gi 489715660 219 IRRLADHADVLVHEAT 234
Cdd:cd07718  189 LVEAGKGADLLIHEAT 204
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-231 3.58e-24

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: 96.82  E-value: 3.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   5 FLGTCSGQPSKLRNVSSLALKLlDelNEIWLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQGD 84
Cdd:cd07719    4 LLGTGGPIPDPDRAGPSTLVVV-G--GRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  85 VGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEGGKIVSERGFEVYTEKLDHRIDswGFRmVEAdkagellmdkl 164
Cdd:cd07719   81 KTPLPVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDD--GVK-VTA----------- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489715660 165 aeFKVPNGPllgklkrgeqVELA-----DGtvlngkdflgpakKGRVVTVIYDTRSTPSIRRLADHADVLVH 231
Cdd:cd07719  147 --FLVDHGP----------VPPAlayrfDT-------------PGRSVVFSGDTGPSENLIELAKGADLLVH 193
PRK02126 PRK02126
ribonuclease Z; Provisional
 35-293 1.46e-23

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 98.45  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  35 LFDCGEATqHQILRtniRLRKITKIFISHNHGDHIFGLPGLLstRSFQGDVGPLTIYGPAGIEQFVKTSL---------- 104
Cdd:PRK02126  31 LFDLGDLH-HLPPR---ELLRISHIFVSHTHMDHFIGFDRLL--RHCLGRPRRLRLFGPPGFADQVEHKLagytwnlven 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 105 ---------------RISKTKISYPIKF------VTLEEGGKIVSERGFEVYTEKLDHRIDSWGFRmVEADKAGELLMDK 163
Cdd:PRK02126 105 ypttfrvhevelhdgRIRRALFSCRRAFareaeeELSLPDGVLLDEPWFRVRAAFLDHGIPCLAFA-LEEKAHINIDKNR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 164 LAEFKVPNGPLLGKLKRG-EQVELADGTVL----NGKDF------LGPAK-------KGRVVTVIYDTRSTPS----IRR 221
Cdd:PRK02126 184 LAELGLPPGPWLRELKHAvLRGEPDDTPIRvlwrDGGGEhervrpLGELKervlriePGQKIGYVTDIGYTEEnlarIVE 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489715660 222 LADHADVLVHEATFDASEGKLARDYYHSTCTQAAETASACHVGHLYLTHVSARYVGSlASQMVKQAREIFPA 293
Cdd:PRK02126 264 LAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGR-GAELYREARAAFAG 334
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-305 2.40e-22

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 93.81  E-value: 2.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGT---------------CSGQPSKL-RNVSSLalkLLDELNEIWLFDCGEATQHQILRTNIRLRKITKIFISHN 64
Cdd:COG1235    1 MKVTFLGSgssggvpqigcdcpvCASTDPRYgRTRSSI---LVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  65 HGDHIFGLPGLlstRSFQGDvGPLTIYGPAGIEQFVKTSLRISKTKISYPIKFVTLEEGGKIVSErGFEVYTEKLDH-RI 143
Cdd:COG1235   78 HADHIAGLDDL---RPRYGP-NPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIG-GLTVTPFPVPHdAG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 144 DSWGFRmVEADkagellmdklaefkvpngpllgklkrgeqveladgtvlngkdflgpakkGRVVTVIYDTRS-TPSIRRL 222
Cdd:COG1235  153 DPVGYR-IEDG-------------------------------------------------GKKLAYATDTGYiPEEVLEL 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 223 ADHADVLVHEATFDASEgklardYYHSTCTQAAETASACHVGHLYLTHVSARYVGSLASQMVKQAREIFPATTLAKDLDK 302
Cdd:COG1235  183 LRGADLLILDATYDDPE------PGHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGME 256


                 ...
gi 489715660 303 FVV 305
Cdd:COG1235  257 IEL 259
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-235 4.73e-16

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: 74.99  E-value: 4.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  35 LFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGLPG-LLSTRSFQGDVGPLTIYGPAGIEQFVKTSLRI-----SK 108
Cdd:cd07740   29 LIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFfLLDAQFVAKRTRPLTIAGPPGLRERLRRAMEAlfpgsSK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 109 TKISYPIKFVTLEEgGKIVSERGFEVYTekldhridswgFRMVEADKAGELLMDKLAEfkvpngpllgklkrgeqvelad 188
Cdd:cd07740  109 VPRRFDLEVIELEP-GEPTTLGGVTVTA-----------FPVVHPSGALPLALRLEAA---------------------- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489715660 189 gtvlngkdflgpakkGRVVTVIYDTRSTPSIRRLADHADVLVHEATF 235
Cdd:cd07740  155 ---------------GRVLAYSGDTEWTDALVPLARGADLFICECYF 186
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-135 5.22e-10

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 57.56  E-value: 5.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660    31 NEIWLFDCGEATQHQILRT--NIRLRKITKIFISHNHGDHIFGLPGLLSTRsfqgdvgPLTIYGPAGIEQFVKTSLRISK 108
Cdd:smart00849   9 GGAILIDTGPGEAEDLLAElkKLGPKKIDAIILTHGHPDHIGGLPELLEAP-------GAPVYAPEGTAELLKDLLALLG 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 489715660   109 TKISY---PIKFVTLEEGGKI-VSERGFEVY 135
Cdd:smart00849  82 ELGAEaepAPPDRTLKDGDELdLGGGELEVI 112
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 59-248 5.54e-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: 55.19  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  59 IFISHNHGDHIFGLP--GLLSTRSFQgdvgpLTIYGPAGIEQFVKTSLRiskTKISYP------------IKFVTLEEGG 124
Cdd:cd07715   61 LLLSHTHWDHIQGFPffAPAYDPGNR-----IHIYGPHKDGGSLEEVLR---RQMSPPyfpvpleellaaIEFHDLEPGE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660 125 KIvSERGFEVYTEKLDHRIDSWGFRmVEADkagellmdklaefkvpngpllgklkrgeqveladgtvlngkdflgpakkG 204
Cdd:cd07715  133 PF-SIGGVTVTTIPLNHPGGALGYR-IEED-------------------------------------------------G 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489715660 205 RVVTVIYDT-------RSTPSIRRLADHADVLVHEATFDASEGKLARDYYH 248
Cdd:cd07715  162 KSVVYATDTehypddgESDEALLEFARGADLLIHDAQYTDEEYPSKRGWGH 212
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 35-156 6.71e-09

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 54.37  E-value: 6.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  35 LFDCGEATQHQiLRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQ---GDVGPLTIYGPAGIEQFVKTSLRISKTki 111
Cdd:cd07716   31 LLDCGSGVLSR-LQRYIDPEDLDAVVLSHLHPDHCADLGVLQYARRYHprgARKPPLPLYGPAGPAERLAALYGLEDV-- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489715660 112 sypIKFVTLEEGGKiVSERGFEVYTEKLDHRIDSWGFRMVEADKA 156
Cdd:cd07716  108 ---FDFHPIEPGEP-LEIGPFTITFFRTVHPVPCYAMRIEDGGKV 148
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 35-270 1.95e-08

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: 53.47  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   35 LFDCGEATQHQILRTN----IRLRKITKIFISHNHGDHIFGLPGLLSTRsfqgdvgPLTIYGPAGIEQFVKTSLRISKTK 110
Cdd:pfam12706   4 LIDPGPDLRQQALPALqpgrLRDDPIDAVLLTHDHYDHLAGLLDLREGR-------PRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  111 ISYPIKFVTLEEGGKivsergFEVYTEKLDhridswgFRMVEAdkagelLMDKLAEFKVPNGPLLGklkrgeqVELADGt 190
Cdd:pfam12706  77 EHYGVRVHEIDWGES------FTVGDGGLT-------VTATPA------RHGSPRGLDPNPGDTLG-------FRIEGP- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  191 vlngkdflgpakkGRVVTVIYDTRSTP-SIRRLADHADVLVHEATFDASEGKLarDYYHSTCTQAAETASACHVGHLYLT 269
Cdd:pfam12706 130 -------------GKRVYYAGDTGYFPdEIGERLGGADLLLLDGGAWRDDEMI--HMGHMTPEEAVEAAADLGARRKVLI 194


                  .
gi 489715660  270 H 270
Cdd:pfam12706 195 H 195
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 26-134 4.13e-08

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: 52.29  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  26 LLDELNEIWLFDCGEATQHQILRTNIRL-RKITKIFISHNHGDHIFGLPGLLstrsfqgDVGPLTIYGPAG----IEQFV 100
Cdd:cd06262   15 VSDEEGEAILIDPGAGALEKILEAIEELgLKIKAILLTHGHFDHIGGLAELK-------EAPGAPVYIHEAdaelLEDPE 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489715660 101 KTSLRISKTKISYPIKFVTLEEGGKI-VSERGFEV 134
Cdd:cd06262   88 LNLAFFGGGPLPPPEPDILLEDGDTIeLGGLELEV 122
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-149 1.15e-07

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: 50.94  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGT-CSG------------QPSKLRNV---SSLALKLlDELNeiWLFDCGEATQHQILRTNIRlrKITKIFISHN 64
Cdd:cd16279    1 MKLTFLGTgTSSgvpvigcdcgvcDSSDPKNRrlrSSILIET-GGKN--ILIDTGPDFRQQALRAGIR--KLDAVLLTHA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  65 HGDHIFGLPGLlstRSFQGDVG-PLTIYGPAGIEQFVKTSLRISKTKISYP------IKFVTLEEGGKIvseRGFEVYTE 137
Cdd:cd16279   76 HADHIHGLDDL---RPFNRLQQrPIPVYASEETLDDLKRRFPYFFAATGGGgvpkldLHIIEPDEPFTI---GGLEITPL 149

                        170
                 ....*....|...
gi 489715660 138 KLDH-RIDSWGFR 149
Cdd:cd16279  150 PVLHgKLPSLGFR 162
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
34-96 1.60e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.42  E-value: 1.60e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489715660  34 WLFDCGEAT--QHQILRTNIRLRKITKIFISHNHGDHIFGLPGLLSTRSfqgdvgPLTIYGPAGI 96
Cdd:COG1237   34 ILFDTGQSDvlLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLELNP------KAPVYAHPDA 92
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 34-127 1.24e-06

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: 48.77  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  34 WLFDCGeatQHQILRTN-----IRLRKITKIFISHNHGDHIFGLPGLLSTRSfqgdvgPLTIYGPAGIEQfVKTSLRISK 108
Cdd:cd07713   32 ILFDTG---QSGVLLHNakklgIDLSDIDAVVLSHGHYDHTGGLKALLELNP------KAPVYAHPDAFE-PRYSKRGGG 101

                         90
                 ....*....|....*....
gi 489715660 109 TKISYPIKFVTLEEGGKIV 127
Cdd:cd07713  102 KKGIGIGREELEKAGARLV 120
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-135 5.81e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 46.21  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   35 LFDCGEATQHQILR----TNIRLRKITKIFISHNHGDHIFGLPGLLSTRSFQGDVGPLTIYGPAGIEQFVKTSLRISKTK 110
Cdd:pfam00753  19 LIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90       100
                  ....*....|....*....|....*
gi 489715660  111 ISYPIKFVTLEEGGKIVSERGFEVY 135
Cdd:pfam00753  99 PVVPLPPDVVLEEGDGILGGGLGLL 123
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-92 1.95e-05

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: 45.28  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGtCSGQPSKLRNvSSLALKLLDELNEIwLFDCG--------EATQHQILRTNIR-----LRKITKIFISHNHGD 67
Cdd:cd07735    1 FELVVLG-CSGGPDEGNT-SSFLLDPAGSDGDI-LLDAGtgvgalslEEMFNDILFPSQKaayelYQRIRHYLITHAHLD 77

                         90       100
                 ....*....|....*....|....*
gi 489715660  68 HIFGLPgLLSTRSFQGDVGPLTIYG 92
Cdd:cd07735   78 HIAGLP-LLSPNDGGQRGSPKTIYG 101
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
1-94 1.16e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 43.02  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGtCSG--QPSKLrnvsSLALKLLDELNEIWLFDCG---------EATQHQILRTNIRLRKITKIFISHNHGDHI 69
Cdd:COG5212   12 MEVRVLG-CSGgiSDGNL----TTYLLRPLGSDDYVLLDAGtvvsglelaEQKGAFKGRQGYVLEHIKGYLISHAHLDHI 86

                         90       100
                 ....*....|....*....|....*
gi 489715660  70 FGLPgLLSTRSfqgdvGPLTIYGPA 94
Cdd:COG5212   87 AGLP-ILSPDD-----SPKTIYALP 105
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-76 7.16e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.79  E-value: 7.16e-04
                         10        20
                 ....*....|....*....|...
gi 489715660  54 RKITKIFISHNHGDHIFGLPGLL 76
Cdd:cd07739   51 KTLTTIYITHGHPDHYFGLEVLL 73
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-93 7.88e-04

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: 39.53  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660   1 MELEFLGT-CSGQ-----------------PSKLRNVSSLALKLLDElneIWLFDCGEATQHQILRtnirLRKITKIFIS 62
Cdd:cd07736    1 MKLTFLGTgDAGGvpvygcdcsacqrarqdPSYRRRPCSALIEVDGE---RILLDAGLTDLAERFP----PGSIDAILLT 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489715660  63 HNHGDHIFglpGLLSTRSFQGDvgPLTIYGP 93
Cdd:cd07736   74 HFHMDHVQ---GLFHLRWGVGD--PIPVYGP 99
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-135 9.79e-04

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: 39.67  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  31 NEIWLFDCG-EATQHQILRTNIRLR--KITKIFISHNHGDHIFGLPGLlstrsfQGDVGPlTIYGPAGIEQFVKTSLRIS 107
Cdd:COG0491   24 DGAVLIDTGlGPADAEALLAALAALglDIKAVLLTHLHPDHVGGLAAL------AEAFGA-PVYAHAAEAEALEAPAAGA 96

                         90       100
                 ....*....|....*....|....*....
gi 489715660 108 KTKISYPIKFVTLEEGGKI-VSERGFEVY 135
Cdd:COG0491   97 LFGREPVPPDRTLEDGDTLeLGGPGLEVI 125
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 31-76 1.98e-03

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: 39.07  E-value: 1.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489715660  31 NEIWLFDCGEATQHQILRTNI-------RLRKITKIFISHNHGDHIFGLPGLL 76
Cdd:COG2333   21 GKTILIDTGPRPSFDAGERVVlpylralGIRRLDLLVLTHPDADHIGGLAAVL 73
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 28-101 4.13e-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: 37.44  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  28 DELNEIWLFDCGEATQhqILRTNIRLR-KITKIFISHNHGDHIFGLPGLLSTrsfqgdVGPLTIYGPA-----GIEQFVK 101
Cdd:cd07723   17 EATGEAAVVDPGEAEP--VLAALEKNGlTLTAILTTHHHWDHTGGNAELKAL------FPDAPVYGPAedripGLDHPVK 88
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-77 4.56e-03

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: 37.51  E-value: 4.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489715660  34 WLFDCGE------ATQHQILRTNIRLRkITKIFISHNHGDHIFGLPGLLS 77
Cdd:cd07722   30 ILIDTGEgrpsyiPLLKSVLDSEGNAT-ISDILLTHWHHDHVGGLPDVLD 78
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-72 7.28e-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: 37.25  E-value: 7.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489715660  34 WLFDCGEATQHQILRTNIRLRKITKIFISHNHGDHIFGL 72
Cdd:cd07730   62 VPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGL 100
PRK02113 PRK02113
MBL fold metallo-hydrolase;
35-134 7.34e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 37.45  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715660  35 LFDCGEATQHQILRTNIRlrKITKIFISHNHGDHIFGLPGLlstRSFqGDVGPLTIYGpagiEQFVKTSLRISK----TK 110
Cdd:PRK02113  48 LIDCGPDFREQMLRLPFG--KIDAVLITHEHYDHVGGLDDL---RPF-CRFGEVPIYA----EQYVAERLRSRMpycfVE 117

                         90       100
                 ....*....|....*....|....*
gi 489715660 111 ISYP-IKFVTLEEggkIVSERGFEV 134
Cdd:PRK02113 118 HSYPgVPNIPLRE---IEPDRPFLV 139
 
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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