NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|663413088|ref|WP_030408522|]
View 

MULTISPECIES: ribonuclease Z [Streptomyces]

Protein Classification

ribonuclease Z( domain architecture ID 10011178)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-306 2.77e-111

ribonuclease Z; Reviewed


:

Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 323.29  E-value: 2.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   4 RELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDG 83
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  84 VPHEVTAHFPASGRAYFERLRHATPFhdtvalreapitspgviagggsgaelpftlearrlshrieaFGYRLTEPDARRM 163
Cdd:PRK00055  82 RTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------------LGYRIAEKDKPGK 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 164 LP-DRLAAHGI-GGPDVGRLQRDGEL-----RGVRLADV-SEPRVGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHA 235
Cdd:PRK00055 121 LDaEKLKALGVpPGPLFGKLKRGEDVtledgRIINPADVlGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663413088 236 DAELAEVAGHLTAYQAGRVAAESGVRHLVLTHFSQRYQ-DTELFAAEAREAgFEgELTAARDLMRIPVPKRR 306
Cdd:PRK00055 201 DEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTgDPEELLKEAREI-FP-NTELAEDLMRVEVPFRR 270
 
Name Accession Description Interval E-value
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-306 2.77e-111

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 323.29  E-value: 2.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   4 RELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDG 83
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  84 VPHEVTAHFPASGRAYFERLRHATPFhdtvalreapitspgviagggsgaelpftlearrlshrieaFGYRLTEPDARRM 163
Cdd:PRK00055  82 RTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------------LGYRIAEKDKPGK 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 164 LP-DRLAAHGI-GGPDVGRLQRDGEL-----RGVRLADV-SEPRVGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHA 235
Cdd:PRK00055 121 LDaEKLKALGVpPGPLFGKLKRGEDVtledgRIINPADVlGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663413088 236 DAELAEVAGHLTAYQAGRVAAESGVRHLVLTHFSQRYQ-DTELFAAEAREAgFEgELTAARDLMRIPVPKRR 306
Cdd:PRK00055 201 DEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTgDPEELLKEAREI-FP-NTELAEDLMRVEVPFRR 270
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-302 5.63e-109

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: 318.39  E-value: 5.63e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088    5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGV 84
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   85 PHEVTAHFPASGRAYFERLRHATPFHDTVALREAPITSPGVIAGGGSgaelpFTLEARRLSHRIEAFGYRLTEPD-ARRM 163
Cdd:TIGR02651  81 KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDG-----FKVEAFPLDHSIPSLGYRFEEKDrPGKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  164 LPDRLAAHGI-GGPDVGRLQR-------DGELrgVRLADVS-EPRVGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLH 234
Cdd:TIGR02651 156 DREKAKELGIpPGPLYGKLKRgetvtliDGRI--IDPEDVLgPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663413088  235 ADAELAEVAGHLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREagFEGELTAARDLMRIPV 302
Cdd:TIGR02651 234 EDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKK--IFPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-301 5.32e-96

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: 283.57  E-value: 5.32e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   6 LVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGVP 85
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  86 HEVTAHFPASGRAYFERLRHATPFHDTVALREAPI-TSPGVIAGGGSgaelpFTLEARRLSHRIEAFGYRLTEpdarrml 164
Cdd:cd07717   81 EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELePDPGLVFEDDG-----FTVTAFPLDHRVPCFGYRFEE------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 165 pdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHADAELAEVAG 244
Cdd:cd07717  149 ------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETG 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663413088 245 HLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREagFEGELTAARDLMRIP 301
Cdd:cd07717  193 HSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEELLKEARA--VFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-302 3.25e-90

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 268.99  E-value: 3.25e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGV 84
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  85 PHEVTAHFPASGRAYFERLRHATPFHDTVALREAPITSPGVIAGGGsgaelpFTLEARRLSHRIEAFGYRLTEPdarrml 164
Cdd:COG1234   82 EKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGG------FTVTAFPLDHPVPAYGYRFEEP------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 165 pdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHADAELAEVAG 244
Cdd:COG1234  150 ------------------------------------GRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETG 193

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663413088 245 HLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREAgFEGELTAARDLMRIPV 302
Cdd:COG1234  194 HSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEELLAEARAV-FPGPVELAEDGMVIEL 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-268 3.69e-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: 52.70  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   34 ILFDPGEGTQRQMLHTSVAAHDLTR----ICLTHFHGDHTLGLPGVIQHMSLD-GVPHEVTAHFPASGRAYFerlrhaTP 108
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDpidaVLLTHDHYDHLAGLLDLREGRPRPlYAPLGVLAHLRRNFPYLF------LL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  109 FHDTVALREAPITSPGVIAGGGsgaeLPFT-LEAR------RLSHRIEAFGYRLTEPdarrmlpdrlaahgiggpdvgrl 181
Cdd:pfam12706  77 EHYGVRVHEIDWGESFTVGDGG----LTVTaTPARhgsprgLDPNPGDTLGFRIEGP----------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  182 qrdgelrgvrladvseprvGQRFAFVMDTRLCDG-VYELADGCDMLVIESTFLhaDAELAEVAGHLTAYQAGRVAAESGV 260
Cdd:pfam12706 130 -------------------GKRVYYAGDTGYFPDeIGERLGGADLLLLDGGAW--RDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 663413088  261 RHLVLTHF 268
Cdd:pfam12706 189 RRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-117 2.61e-07

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: 49.86  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088    23 NGYVLLWDGEGILFDPGEGTQRQMLhTSVAAH---DLTRICLTHFHGDHTLGLPGVIQHMSLDGVPHEVTA-HFPASGRA 98
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLL-AELKKLgpkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAeLLKDLLAL 79

                           90
                   ....*....|....*....
gi 663413088    99 YFERLRHATPFHDTVALRE 117
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKD 98
 
Name Accession Description Interval E-value
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-306 2.77e-111

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 323.29  E-value: 2.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   4 RELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDG 83
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  84 VPHEVTAHFPASGRAYFERLRHATPFhdtvalreapitspgviagggsgaelpftlearrlshrieaFGYRLTEPDARRM 163
Cdd:PRK00055  82 RTEPLTIYGPKGIKEFVETLLRASGS-----------------------------------------LGYRIAEKDKPGK 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 164 LP-DRLAAHGI-GGPDVGRLQRDGEL-----RGVRLADV-SEPRVGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHA 235
Cdd:PRK00055 121 LDaEKLKALGVpPGPLFGKLKRGEDVtledgRIINPADVlGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663413088 236 DAELAEVAGHLTAYQAGRVAAESGVRHLVLTHFSQRYQ-DTELFAAEAREAgFEgELTAARDLMRIPVPKRR 306
Cdd:PRK00055 201 DEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTgDPEELLKEAREI-FP-NTELAEDLMRVEVPFRR 270
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-302 5.63e-109

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: 318.39  E-value: 5.63e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088    5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGV 84
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   85 PHEVTAHFPASGRAYFERLRHATPFHDTVALREAPITSPGVIAGGGSgaelpFTLEARRLSHRIEAFGYRLTEPD-ARRM 163
Cdd:TIGR02651  81 KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDG-----FKVEAFPLDHSIPSLGYRFEEKDrPGKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  164 LPDRLAAHGI-GGPDVGRLQR-------DGELrgVRLADVS-EPRVGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLH 234
Cdd:TIGR02651 156 DREKAKELGIpPGPLYGKLKRgetvtliDGRI--IDPEDVLgPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663413088  235 ADAELAEVAGHLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREagFEGELTAARDLMRIPV 302
Cdd:TIGR02651 234 EDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKK--IFPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-301 5.32e-96

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: 283.57  E-value: 5.32e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   6 LVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGVP 85
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  86 HEVTAHFPASGRAYFERLRHATPFHDTVALREAPI-TSPGVIAGGGSgaelpFTLEARRLSHRIEAFGYRLTEpdarrml 164
Cdd:cd07717   81 EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELePDPGLVFEDDG-----FTVTAFPLDHRVPCFGYRFEE------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 165 pdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHADAELAEVAG 244
Cdd:cd07717  149 ------------------------------------GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETG 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663413088 245 HLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREagFEGELTAARDLMRIP 301
Cdd:cd07717  193 HSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEELLKEARA--VFPNTILAEDFMTIE 247
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-302 3.25e-90

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 268.99  E-value: 3.25e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGV 84
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  85 PHEVTAHFPASGRAYFERLRHATPFHDTVALREAPITSPGVIAGGGsgaelpFTLEARRLSHRIEAFGYRLTEPdarrml 164
Cdd:COG1234   82 EKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGG------FTVTAFPLDHPVPAYGYRFEEP------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 165 pdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHADAELAEVAG 244
Cdd:COG1234  150 ------------------------------------GRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETG 193

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663413088 245 HLTAYQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREAgFEGELTAARDLMRIPV 302
Cdd:COG1234  194 HSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEELLAEARAV-FPGPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-230 3.44e-32

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: 117.75  E-value: 3.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   6 LVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGVP 85
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  86 HEVTAHFPASGRAYFERL--RHATPFHDTVALREAPITSPGVIAGGGsgaelPFTLEARRLSHRIEAFGYRLTEpdarrm 163
Cdd:cd16272   81 KPLTIYGPKGIKEFLEKLlnFPVEILPLGFPLEIEELEEGGEVLELG-----DLKVEAFPVKHSVESLGYRIEA------ 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663413088 164 lpdrlaahgiggpdvgrlqrdgelrgvrladvseprVGQRFAFVMDTRLCDGVYELADGCDMLVIES 230
Cdd:cd16272  150 ------------------------------------EGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 12-302 5.37e-25

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 100.74  E-value: 5.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  12 ASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGVPheVTAH 91
Cdd:COG1235   25 ASTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPIP--VYAT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  92 fPASGRAYFERLRHA-TPFHDTVALREAPITSPGVIAGggsgaelpFTLEARRLSH-RIEAFGYRLTEPdarrmlpdrla 169
Cdd:COG1235  103 -PGTLEALERRFPYLfAPYPGKLEFHEIEPGEPFEIGG--------LTVTPFPVPHdAGDPVGYRIEDG----------- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 170 ahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDT-RLCDGVYELADGCDMLVIESTflHADAElaevAGHLTA 248
Cdd:COG1235  163 -------------------------------GKKLAYATDTgYIPEEVLELLRGADLLILDAT--YDDPE----PGHLSN 205

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663413088 249 YQAGRVAAESGVRHLVLTHFSQRYQDTELFAAEAREAGFEGELTAARDLMRIPV 302
Cdd:COG1235  206 EEALELLARLGPKRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGMEIEL 259
PRK02126 PRK02126
ribonuclease Z; Provisional
 137-285 1.41e-22

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 95.75  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 137 FTLEARRLSHRIEAFGYRLTEPDARRMLPDRLAAHGI---------------GGPDVGRLQ---RDGELRGVRLADVSEP 198
Cdd:PRK02126 153 FRVRAAFLDHGIPCLAFALEEKAHINIDKNRLAELGLppgpwlrelkhavlrGEPDDTPIRvlwRDGGGEHERVRPLGEL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 199 R-------VGQRFAFVMDTRLCDG----VYELADGCDMLVIESTFLHADAELAEVAGHLTAYQAGRVAAESGVRHLVLTH 267
Cdd:PRK02126 233 KervlriePGQKIGYVTDIGYTEEnlarIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFH 312

                        170
                 ....*....|....*....
gi 663413088 268 FSQRYQDT-ELFAAEAREA 285
Cdd:PRK02126 313 FSPRYQGRgAELYREARAA 331
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-227 2.20e-17

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: 78.71  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLDGV 84
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  85 PHEVTAHFPASGRAYFERLRHATPF--------HDTVALREAPITSPGVIAGGGSGAELP-FTLEARRLSHRI--EAFGY 153
Cdd:cd07719   81 KTPLPVYGPPGTRALVDGLLAAYALdidyrariGDEGRPDPGALVEVHEIAAGGVVYEDDgVKVTAFLVDHGPvpPALAY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663413088 154 RLTEPdarrmlpdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLV 227
Cdd:cd07719  161 RFDTP------------------------------------------GRSVVFSGDTGPSENLIELAKGADLLV 192
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-230 2.18e-11

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: 61.30  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   5 ELVVLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQmLHTSVAAHDLTRICLTHFHGDHTLGLpGVIQHM----S 80
Cdd:cd07716    1 KLTVLGCSGSYPGPGGACSGYLLEADGFRILLDCGSGVLSR-LQRYIDPEDLDAVVLSHLHPDHCADL-GVLQYArryhP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  81 LDGVPHEVTAHFPASGRayfERLRHATPFHDTVALReaPITSPGVIAGGgsgaelPFTLEARRLSHRIEAFGYRLTEPda 160
Cdd:cd07716   79 RGARKPPLPLYGPAGPA---ERLAALYGLEDVFDFH--PIEPGEPLEIG------PFTITFFRTVHPVPCYAMRIEDG-- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 161 rrmlpdrlaahgiggpdvgrlqrdgelrgvrladvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIES 230
Cdd:cd07716  146 ----------------------------------------GKVLVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 6-78 5.48e-10

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: 57.94  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   6 LVVLGTASQVPTRQRNHNGYVLLWDGEG-ILFDPGEGTQRQMLH------TSVAAHDLTRICLTHFHGDHTLGLPGVIQH 78
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGsILLDCGEGTLGQLRRhygpeeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-268 3.69e-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: 52.70  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   34 ILFDPGEGTQRQMLHTSVAAHDLTR----ICLTHFHGDHTLGLPGVIQHMSLD-GVPHEVTAHFPASGRAYFerlrhaTP 108
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDpidaVLLTHDHYDHLAGLLDLREGRPRPlYAPLGVLAHLRRNFPYLF------LL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  109 FHDTVALREAPITSPGVIAGGGsgaeLPFT-LEAR------RLSHRIEAFGYRLTEPdarrmlpdrlaahgiggpdvgrl 181
Cdd:pfam12706  77 EHYGVRVHEIDWGESFTVGDGG----LTVTaTPARhgsprgLDPNPGDTLGFRIEGP----------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  182 qrdgelrgvrladvseprvGQRFAFVMDTRLCDG-VYELADGCDMLVIESTFLhaDAELAEVAGHLTAYQAGRVAAESGV 260
Cdd:pfam12706 130 -------------------GKRVYYAGDTGYFPDeIGERLGGADLLLLDGGAW--RDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 663413088  261 RHLVLTHF 268
Cdd:pfam12706 189 RRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-117 2.61e-07

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: 49.86  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088    23 NGYVLLWDGEGILFDPGEGTQRQMLhTSVAAH---DLTRICLTHFHGDHTLGLPGVIQHMSLDGVPHEVTA-HFPASGRA 98
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLL-AELKKLgpkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAeLLKDLLAL 79

                           90
                   ....*....|....*....
gi 663413088    99 YFERLRHATPFHDTVALRE 117
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKD 98
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-114 8.11e-06

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: 45.84  E-value: 8.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  23 NGYVLLWDGEGILFDPG-EGTQRQMLHTSVAAH--DLTRICLTHFHGDHTLGLPGVIQHMSLDGVPHEVTAHFPASGRAY 99
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGlGPADAEALLAALAALglDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPAAG 95

                         90
                 ....*....|....*
gi 663413088 100 FERLRHATPFHDTVA 114
Cdd:COG0491   96 ALFGREPVPPDRTLE 110
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 23-78 1.17e-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: 1.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663413088  23 NGYvLLWD--GEGILFDPGEGTQRQMLHTSVAAH-DLTRICLTHFHGDHTLGLPGVIQH 78
Cdd:cd06262   11 NCY-LVSDeeGEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELKEA 68
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-108 6.37e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 43.13  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   20 RNHNGYVLLWDGEGILFDPG--EGTQRQMLHTSVAAH--DLTRICLTHFHGDHTLGLPGVIQHMSLDGVPHEVTAHFPAS 95
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGgsAEAALLLLLAALGLGpkDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90
                  ....*....|...
gi 663413088   96 GRAYFERLRHATP 108
Cdd:pfam00753  84 EELGLAASRLGLP 96
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 11-72 6.79e-05

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: 42.99  E-value: 6.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663413088  11 TASQVPTRQRNHNGYVLLWDGEGILFDPGEGTqrqmLHTSVAAHDLTRICLTHFHGDHTLGL 72
Cdd:cd07736   26 RARQDPSYRRRPCSALIEVDGERILLDAGLTD----LAERFPPGSIDAILLTHFHMDHVQGL 83
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-245 2.85e-04

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 41.09  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088   8 VLGTASQVPTRQRNHNGYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVIQHMSLdgvphe 87
Cdd:cd07740    2 FLGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQF------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  88 vtahfpasgrayferlrhatpfhdtVALREAPITspgvIAGGGSGAEL----------PFTLEARRLSHRIEAFgyrltE 157
Cdd:cd07740   76 -------------------------VAKRTRPLT----IAGPPGLRERlrramealfpGSSKVPRRFDLEVIEL-----E 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088 158 PDarrmLPDRLAAHGIGGPDVGRLQRDGELRGVRLADvseprvGQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHada 237
Cdd:cd07740  122 PG----EPTTLGGVTVTAFPVVHPSGALPLALRLEAA------GRVLAYSGDTEWTDALVPLARGADLFICECYFFE--- 188


                 ....*...
gi 663413088 238 elAEVAGH 245
Cdd:cd07740  189 --KKVPGH 194
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 201-267 4.96e-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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 40.64  E-value: 4.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663413088 201 GQRFAFVMDTRLCDGVYELADGCDMLVIESTFLHADaelaEVAGHLTAYQAGRVAAESGVRHLVLTH 267
Cdd:cd07741  150 DKKIGYISDTRYFEELIEYYSNCDVLIINVTRPRPR----KGVDHLSVEDVEKILKEIKPKLAILTH 212
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 23-85 1.00e-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: 39.44  E-value: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663413088  23 NGYVLlwdGEG---ILFDPGEG------TQRQMLHTSVAAHdLTRICLTHFHGDHTLGLPGVIQHMSLDGVP 85
Cdd:cd07722   19 NTYLV---GTGkrrILIDTGEGrpsyipLLKSVLDSEGNAT-ISDILLTHWHHDHVGGLPDVLDLLRGPSPR 86
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 24-76 3.82e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293824  Cd Length: 189  Bit Score: 37.66  E-value: 3.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663413088  24 GYVLLWDGEGILFDPGEGTQRQMLHTSVAAHDLTRICLTHFHGDHTLGLPGVI 76
Cdd:cd07738   17 GFIIWINGRGIMVDPPVNSTSYLRQNGISPRLVDHVILTHCHADHDAGTFQKI 69
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 23-73 5.83e-03

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 37.20  E-value: 5.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663413088  23 NGYVLLWDGEGILFD---PGEGTQ--RQMLHTSVAAHDLTRICLTHFHGDHTLGLP 73
Cdd:cd07721   12 NAYLIEDDDGLTLIDtglPGSAKRilKALRELGLSPKDIRRILLTHGHIDHIGSLA 67
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 10-91 6.65e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 36.79  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663413088  10 GTASQVPTRQRNHNGYVLLWDGEG--ILFDPGEGTQRQMLHTSVAAH-----DLTRICLTHFHGDHTLGL---PGVIQHM 79
Cdd:cd07711    8 GYARRDSDGGFRASSTVTLIKDGGknILVDTGTPWDRDLLLKALAEHglspeDIDYVVLTHGHPDHIGNLnlfPNATVIV 87

                         90
                 ....*....|..
gi 663413088  80 SLDGVPHEVTAH 91
Cdd:cd07711   88 GWDICGDSYDDH 99
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 30-79 7.75e-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: 37.14  E-value: 7.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663413088  30 DGEGILFDPGEGTQRQMLHTSVA----AHDLTRI---CLTHFHGDHTLGLPGVIQHM 79
Cdd:COG2333   20 DGKTILIDTGPRPSFDAGERVVLpylrALGIRRLdllVLTHPDADHIGGLAAVLEAF 76
 
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