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Conserved domains on  [gi|224131708|ref|XP_002321158|]
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tRNase Z TRZ2, chloroplastic [Populus trichocarpa]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
131-345 6.74e-33

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 123.00  E-value: 6.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIHRAMGQVELNFdlVALDVGETYELrNDVVVRP 209
Cdd:COG1234   56 IFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKASGTDLDFPLEF--HEIEPGEVFEI-GGFTVTA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 210 FRTQHVIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTTAeymlDPRNADALR-AKVLIT 288
Cdd:COG1234  133 FPLDHPVPAYGYRFEEPGRS-------------------------------LVYSGDTRP----CEALVELAKgADLLIH 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 224131708 289 EATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYS-IEDIREAVSK 345
Cdd:COG1234  178 EATFLDEE--AELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdPEELLAEARA 233
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
131-345 6.74e-33

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 123.00  E-value: 6.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIHRAMGQVELNFdlVALDVGETYELrNDVVVRP 209
Cdd:COG1234   56 IFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKASGTDLDFPLEF--HEIEPGEVFEI-GGFTVTA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 210 FRTQHVIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTTAeymlDPRNADALR-AKVLIT 288
Cdd:COG1234  133 FPLDHPVPAYGYRFEEPGRS-------------------------------LVYSGDTRP----CEALVELAKgADLLIH 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 224131708 289 EATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYS-IEDIREAVSK 345
Cdd:COG1234  178 EATFLDEE--AELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdPEELLAEARA 233
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 98-290 3.46e-31

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: 116.59  E-value: 3.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  98 LSIGGQETCIIIPEFKCAFDIGR--CPTRAIH------QNFVFITHAHLDHIGGLPMYVASRGLYS-LKPPTIFVPPCIK 168
Cdd:cd16272   13 LTRNTSSYLLETGGTRILLDCGEgtVYRLLKAgvdpdkLDAIFLSHFHLDHIGGLPTLLFARRYGGrKKPLTIYGPKGIK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 169 DDVEKLFDIHRAMGQVELNFDLVALDVGETYELRNDVVVRPFRTQHVIPSQGYVIYSVRKKlkkqyihlkgkqieklkks 248
Cdd:cd16272   93 EFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKS------------------- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 224131708 249 gveitdiilspeVAFTGDTTAEYMLDPRnadALRAKVLITEA 290
Cdd:cd16272  154 ------------IVYSGDTGPCENLVEL---AKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 131-342 4.28e-28

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: 111.54  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIhramGQVELNFDLVALDVGETYELR--NDVVV 207
Cdd:TIGR02651  55 IFITHLHGDHILGLPGLLSTMSFQGRKEPlTIYGPPGIKEFIETSLRV----SYTYLNYPIKIHEIEEGGLVFedDGFKV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  208 RPFRTQHVIPSQGYVIYSVRKKL-----KKQYIHLKGKQIEKLKKSGVEIT---DIILSPE-----------VAFTGDT- 267
Cdd:TIGR02651 131 EAFPLDHSIPSLGYRFEEKDRPGkfdreKAKELGIPPGPLYGKLKRGETVTlidGRIIDPEdvlgpprkgrkIAYTGDTr 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  268 ----TAEYMldpRNADalrakVLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYSIED--IRE 341
Cdd:TIGR02651 211 pceeVIEFA---KNAD-----LLIHEATFLDED--KKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEelLEE 280


                  .
gi 224131708  342 A 342
Cdd:TIGR02651 281 A 281
PRK00055 PRK00055
ribonuclease Z; Reviewed
 131-337 1.41e-13

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 70.21  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLY-SLKPPTIFVPPCIKDDVEKLFDIHRAMG-QVELNFDLVALDVGETYELrnDVVVR 208
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLLSTRSLSgRTEPLTIYGPKGIKEFVETLLRASGSLGyRIAEKDKPGKLDAEKLKAL--GVPPG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 209 PFrtqhvipsqgyviysvRKKLKkqyihlKGKQIEkLKKSGVEITDIILSPE-----VAFTGDT--TAEYMLDPRNADal 281
Cdd:PRK00055 135 PL----------------FGKLK------RGEDVT-LEDGRIINPADVLGPPrkgrkVAYCGDTrpCEALVELAKGAD-- 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224131708 282 rakVLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYSIE 337
Cdd:PRK00055 190 ---LLVHEATFGDED--EELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGD 240
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 131-330 8.79e-09

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: 54.62  E-value: 8.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPMyvasrgLYSLKPPTIFVPPCIKDDVEKLFDihRAMGQVELNFDLVALDVGETYELRN-DVVVRP 209
Cdd:pfam12706  32 VLLTHDHYDHLAGLLD------LREGRPRPLYAPLGVLAHLRRNFP--YLFLLEHYGVRVHEIDWGESFTVGDgGLTVTA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  210 FRTQH---------VIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTtaEYMlDPRNADA 280
Cdd:pfam12706 104 TPARHgsprgldpnPGDTLGFRIEGPGKR-------------------------------VYYAGDT--GYF-PDEIGER 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 224131708  281 LR-AKVLITEATFLDEDFTTEHarqrGHTHLFEIIENAKWIRSKAILLTHF 330
Cdd:pfam12706 150 LGgADLLLLDGGAWRDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 131-223 3.04e-05

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: 44.08  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708   131 VFITHAHLDHIGGLPmyvasrGLYSLKPPTIFVPPCIKDDVEKLFDIHRAMGQVELNF-DLVALDVGETYELrNDVVVRP 209
Cdd:smart00849  39 IILTHGHPDHIGGLP------ELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPApPDRTLKDGDELDL-GGGELEV 111

                           90
                   ....*....|....*
gi 224131708   210 FRTQHVIP-SQGYVI 223
Cdd:smart00849 112 IHTPGHTPgSIVLYL 126
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
131-345 6.74e-33

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 123.00  E-value: 6.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIHRAMGQVELNFdlVALDVGETYELrNDVVVRP 209
Cdd:COG1234   56 IFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEALLKASGTDLDFPLEF--HEIEPGEVFEI-GGFTVTA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 210 FRTQHVIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTTAeymlDPRNADALR-AKVLIT 288
Cdd:COG1234  133 FPLDHPVPAYGYRFEEPGRS-------------------------------LVYSGDTRP----CEALVELAKgADLLIH 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 224131708 289 EATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYS-IEDIREAVSK 345
Cdd:COG1234  178 EATFLDEE--AELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDdPEELLAEARA 233
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 98-290 3.46e-31

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: 116.59  E-value: 3.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  98 LSIGGQETCIIIPEFKCAFDIGR--CPTRAIH------QNFVFITHAHLDHIGGLPMYVASRGLYS-LKPPTIFVPPCIK 168
Cdd:cd16272   13 LTRNTSSYLLETGGTRILLDCGEgtVYRLLKAgvdpdkLDAIFLSHFHLDHIGGLPTLLFARRYGGrKKPLTIYGPKGIK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 169 DDVEKLFDIHRAMGQVELNFDLVALDVGETYELRNDVVVRPFRTQHVIPSQGYVIYSVRKKlkkqyihlkgkqieklkks 248
Cdd:cd16272   93 EFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKS------------------- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 224131708 249 gveitdiilspeVAFTGDTTAEYMLDPRnadALRAKVLITEA 290
Cdd:cd16272  154 ------------IVYSGDTGPCENLVEL---AKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 131-342 4.28e-28

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: 111.54  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIhramGQVELNFDLVALDVGETYELR--NDVVV 207
Cdd:TIGR02651  55 IFITHLHGDHILGLPGLLSTMSFQGRKEPlTIYGPPGIKEFIETSLRV----SYTYLNYPIKIHEIEEGGLVFedDGFKV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  208 RPFRTQHVIPSQGYVIYSVRKKL-----KKQYIHLKGKQIEKLKKSGVEIT---DIILSPE-----------VAFTGDT- 267
Cdd:TIGR02651 131 EAFPLDHSIPSLGYRFEEKDRPGkfdreKAKELGIPPGPLYGKLKRGETVTlidGRIIDPEdvlgpprkgrkIAYTGDTr 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  268 ----TAEYMldpRNADalrakVLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYSIED--IRE 341
Cdd:TIGR02651 211 pceeVIEFA---KNAD-----LLIHEATFLDED--KKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEelLEE 280


                  .
gi 224131708  342 A 342
Cdd:TIGR02651 281 A 281
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 131-344 1.34e-26

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 105.99  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIHRAMGQVELNFDLVALDVGETYElRNDVVVRP 209
Cdd:cd07717   54 IFITHLHGDHILGLPGLLSTMSLLGRTEPlTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGLVFE-DDGFTVTA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 210 FRTQHVIPSQGYVIYSVRKklkkqyihlkgkqieklkksgveitdiilspeVAFTGDT-----TAEYMldpRNADalrak 284
Cdd:cd07717  133 FPLDHRVPCFGYRFEEGRK--------------------------------IAYLGDTrpcegLVELA---KGAD----- 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224131708 285 VLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYSIED--IREAVS 344
Cdd:cd07717  173 LLIHEATFLDDD--AEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEelLKEARA 232
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 131-342 3.33e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 74.55  E-value: 3.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYvasRGLYSLKPPTIFVPPCIKDDVEKLFDIHRAMGQVELNFdlVALDVGETYELrNDVVVRPF 210
Cdd:COG1235   72 ILLTHEHADHIAGLDDL---RPRYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEF--HEIEPGEPFEI-GGLTVTPF 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 211 RTQH-VIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTtaEYMlDPRNADALR-AKVLIT 288
Cdd:COG1235  146 PVPHdAGDPVGYRIEDGGKK-------------------------------LAYATDT--GYI-PEEVLELLRgADLLIL 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 224131708 289 EATFLDEDFtteharqrGHTHLFEIIENAKWIRSKAILLTHFSSRYSIEDIREA 342
Cdd:COG1235  192 DATYDDPEP--------GHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYD 237
PRK00055 PRK00055
ribonuclease Z; Reviewed
 131-337 1.41e-13

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 70.21  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLY-SLKPPTIFVPPCIKDDVEKLFDIHRAMG-QVELNFDLVALDVGETYELrnDVVVR 208
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLLSTRSLSgRTEPLTIYGPKGIKEFVETLLRASGSLGyRIAEKDKPGKLDAEKLKAL--GVPPG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 209 PFrtqhvipsqgyviysvRKKLKkqyihlKGKQIEkLKKSGVEITDIILSPE-----VAFTGDT--TAEYMLDPRNADal 281
Cdd:PRK00055 135 PL----------------FGKLK------RGEDVT-LEDGRIINPADVLGPPrkgrkVAYCGDTrpCEALVELAKGAD-- 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224131708 282 rakVLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFSSRYSIE 337
Cdd:PRK00055 190 ---LLVHEATFGDED--EELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGD 240
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 131-330 8.79e-09

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: 54.62  E-value: 8.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPMyvasrgLYSLKPPTIFVPPCIKDDVEKLFDihRAMGQVELNFDLVALDVGETYELRN-DVVVRP 209
Cdd:pfam12706  32 VLLTHDHYDHLAGLLD------LREGRPRPLYAPLGVLAHLRRNFP--YLFLLEHYGVRVHEIDWGESFTVGDgGLTVTA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  210 FRTQH---------VIPSQGYVIYSVRKKlkkqyihlkgkqieklkksgveitdiilspeVAFTGDTtaEYMlDPRNADA 280
Cdd:pfam12706 104 TPARHgsprgldpnPGDTLGFRIEGPGKR-------------------------------VYYAGDT--GYF-PDEIGER 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 224131708  281 LR-AKVLITEATFLDEDFTTEHarqrGHTHLFEIIENAKWIRSKAILLTHF 330
Cdd:pfam12706 150 LGgADLLLLDGGAWRDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
131-307 1.29e-08

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 55.74  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRglyslKPPTIF-VPPCIKDDVEKLF------DIHRAMGQVELNF-DLVALDVGETYELR 202
Cdd:COG5212   76 YLISHAHLDHIAGLPILSPDD-----SPKTIYaLPETIDALRNHYFnwviwpDFTDIGSAPHLPKyRYVPLKPGQTFPLG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 203 N-DVVVRPFRTQHVIPSQGYVIYSvrkklKKQYihlkgkqieklkksgveitdiilspeVAFTGDTTAEYMLDPRNADAL 281
Cdd:COG5212  151 GtGLRVTAFPLSHSVPSSAFLIES-----GGGA--------------------------FLYSGDTGPDEVEKSTNLDAL 199

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 224131708 282 --------RAKVL---ITEATFLDEDfttEHARQRGH 307
Cdd:COG5212  200 wealaplvRSKKLkaiIIEVSFPNEQ---PDALLFGH 233
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 131-223 1.37e-08

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: 54.06  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPP-TIFVPPCIKDDVEKLFDIHR------------AMGQVELNFDLVALDVGE 197
Cdd:cd07719   55 VFLTHLHSDHVADLPALLLTAWLAGRKTPlPVYGPPGTRALVDGLLAAYAldidyrarigdeGRPDPGALVEVHEIAAGG 134

                         90       100
                 ....*....|....*....|....*...
gi 224131708 198 TYELRNDVVVRPFRTQH--VIPSQGYVI 223
Cdd:cd07719  135 VVYEDDGVKVTAFLVDHgpVPPALAYRF 162
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 131-297 2.28e-08

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: 53.42  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSL--KPPTIFVPPCIKDDVEKLFDIH-RAMGQVELNFDL--VALDVGETYELrNDV 205
Cdd:cd07740   53 IFITHLHGDHFGGLPFFLLDAQFVAKrtRPLTIAGPPGLRERLRRAMEALfPGSSKVPRRFDLevIELEPGEPTTL-GGV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 206 VVRPFRTQHVIPSQGYVIYSVrkklkkqyihLKGKQIeklkksgveitdiilspevAFTGDTTAEYMLDP--RNADalra 283
Cdd:cd07740  132 TVTAFPVVHPSGALPLALRLE----------AAGRVL-------------------AYSGDTEWTDALVPlaRGAD---- 178

                        170
                 ....*....|....
gi 224131708 284 kVLITEATFLDEDF 297
Cdd:cd07740  179 -LFICECYFFEKKV 191
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 131-290 3.30e-08

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: 52.83  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGL-PMYVASR---GLYSLKPPTIFVPPCIKDDVEKLFDIHRAmgqvelnFDLVALDVGETYELrNDVV 206
Cdd:cd07716   54 VVLSHLHPDHCADLgVLQYARRyhpRGARKPPLPLYGPAGPAERLAALYGLEDV-------FDFHPIEPGEPLEI-GPFT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 207 VRPFRTQHVIPSqgyviYSVRkklkkqyihlkgkqIEKLKKSgveitdiilspeVAFTGDT--TAEymLDP--RNADalr 282
Cdd:cd07716  126 ITFFRTVHPVPC-----YAMR--------------IEDGGKV------------LVYTGDTgyCDE--LVEfaRGAD--- 169


                 ....*...
gi 224131708 283 akVLITEA 290
Cdd:cd07716  170 --LLLCEA 175
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 131-225 3.58e-08

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


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 53.56  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPmYVASRglysLKPPtIFVPPCIKDDVEKLFDIHRAMGQVELNfdlvALDVGETYELrNDVVVRPF 210
Cdd:cd07714   59 IFITHGHEDHIGALP-YLLPE----LNVP-IYATPLTLALIKKKLEEFKLIKKVKLN----EIKPGERIKL-GDFEVEFF 127

                         90       100
                 ....*....|....*....|....
gi 224131708 211 RTQHVIP---------SQGYVIYS 225
Cdd:cd07714  128 RVTHSIPdsvglaiktPEGTIVHT 151
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 131-223 3.67e-08

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 53.75  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMYVASRGLYSLKPPTIF-VPPCIKDDVEKLF--DIHRAMGQVELNF----DLVALDVGETYELrN 203
Cdd:cd07735   69 YLITHAHLDHIAGLPLLSPNDGGQRGSPKTIYgLPETIDALKKHIFnwVIWPDFTSIPSGKypylRLEPIEPEYPIAL-T 147

                         90       100
                 ....*....|....*....|.
gi 224131708 204 DVVVRPFRTQHVIP-SQGYVI 223
Cdd:cd07735  148 GLSVTAFPVSHGVPvSTAFLI 168
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 131-290 3.51e-07

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849  Cd Length: 199  Bit Score: 49.95  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPMY---VASRGLYSLKPPTIFVPPCIKDDVEKLF-------------DIHRAMGQVelnfdlVALD 194
Cdd:cd16291   59 VIISHFHLDHCGALPYFtevVGYDGPIYMTHPTKAICPILLEDYRKIAverkgetnfftsqMIKDCMKKV------IAVN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 195 VGETYELRNDVVVRPFRTQHVIpsqGYVIYSVRkklkkqyihlkgkqieklkksgveitdiILSPEVAFTGD--TTAEYM 272
Cdd:cd16291  133 LHETVQVDDELEIKAYYAGHVL---GAAMFYVR----------------------------VGDESVVYTGDynMTPDRH 181

                        170
                 ....*....|....*...
gi 224131708 273 LDPRNADALRAKVLITEA 290
Cdd:cd16291  182 LGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 122-326 3.59e-07

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 51.73  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 122 PTRAIHQNFVFITHAHLDHIGGLPMYVAS--RGLYSLKPPT-----IFVPPCIK-----DDVEKLF---DIHRAMGQvel 186
Cdd:COG1236   45 PFRPSDVDAVVLTHAHLDHSGALPLLVKEgfRGPIYATPATadlarILLGDSAKiqeeeAEAEPLYteeDAERALEL--- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 187 nfdLVALDVGETYELrNDVVVRPFRTQHVIPSQgyviySVRkklkkqyIHLKGKQIeklkksgveitdiilspevAFTGD 266
Cdd:COG1236  122 ---FQTVDYGEPFEI-GGVRVTFHPAGHILGSA-----QVE-------LEVGGKRI-------------------VFSGD 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224131708 267 --TTAEYMLDPrnADAL-RAKVLITEATFLDEDFTTEHARQRghtHLFEIIENAKWIRSKAIL 326
Cdd:COG1236  167 ygREDDPLLAP--PEPVpPADVLITESTYGDRLHPPREEVEA---ELAEWVRETLARGGTVLI 224
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 129-211 1.24e-05

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 45.53  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 129 NFVFITHAHLDHIGGLPMYVAsrglYSLKPPtIFVPP--------------------CIKDDVEKLF---DIHRAMGQVe 185
Cdd:cd16295   53 DAVILTHAHLDHSGRLPLLVK----EGFRGP-IYATPatkdlaelllldsakiqeeeAEHPPAEPLYteeDVEKALKHF- 126

                         90       100
                 ....*....|....*....|....*.
gi 224131708 186 lnfdlVALDVGETYELRNDVVVRPFR 211
Cdd:cd16295  127 -----RPVEYGEPFEIGPGVKVTFYD 147
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 131-223 3.04e-05

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: 44.08  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708   131 VFITHAHLDHIGGLPmyvasrGLYSLKPPTIFVPPCIKDDVEKLFDIHRAMGQVELNF-DLVALDVGETYELrNDVVVRP 209
Cdd:smart00849  39 IILTHGHPDHIGGLP------ELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPApPDRTLKDGDELDL-GGGELEV 111

                           90
                   ....*....|....*
gi 224131708   210 FRTQHVIP-SQGYVI 223
Cdd:smart00849 112 IHTPGHTPgSIVLYL 126
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 131-230 3.16e-05

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 44.24  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPM---YVASRGLYSLKPPTIFVPPCIKDDVEKLF-------------DIHRAMGQVelnfdlVALD 194
Cdd:cd07734   53 ILISHFHLDHCGALPYlfrGFIFRGPIYATHPTVALGRLLLEDYVKSAerigqdqslytpeDIEEALKHI------VPLG 126

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 224131708 195 VGETYELRNDVVVRPFRTQHVIPSQGYVIYSVRKKL 230
Cdd:cd07734  127 YGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKL 162
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
131-223 5.95e-05

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 45.05  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLPmYVASRglysLKPP------TIFVppcikddVEKLFDIHRAMGQVELNfdlvALDVGETYELrND 204
Cdd:COG0595   67 IVLTHGHEDHIGALP-YLLKE----LNVPvygtplTLAL-------LEAKLKEHGLLKKVKLH----VVKPGDRIKF-GP 129

                         90       100
                 ....*....|....*....|
gi 224131708 205 VVVRPFRTQHVIP-SQGYVI 223
Cdd:COG0595  130 FKVEFFRVTHSIPdSLGLAI 149
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 131-307 1.20e-04

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: 42.87  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLP----MYVASRGLyslkppTIFVPPCIKDDVEKLFD-----------IHRAMGQVElNFDLVAldv 195
Cdd:cd07715   61 LLLSHTHWDHIQGFPffapAYDPGNRI------HIYGPHKDGGSLEEVLRrqmsppyfpvpLEELLAAIE-FHDLEP--- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 196 GETYELrNDVVVRPFRTQHVIPSQGYviysvrkklkkqyihlkgkQIEKLKKSGVEITDIILSPEVAftgdttaeyMLDP 275
Cdd:cd07715  131 GEPFSI-GGVTVTTIPLNHPGGALGY-------------------RIEEDGKSVVYATDTEHYPDDG---------ESDE 181

                        170       180       190
                 ....*....|....*....|....*....|...
gi 224131708 276 RNADALR-AKVLITEATFLDEDFttEHARQRGH 307
Cdd:cd07715  182 ALLEFARgADLLIHDAQYTDEEY--PSKRGWGH 212
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 131-225 1.34e-04

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPmYVASRglYSLKPptIFVPP----CIKDDV-EKLFDIHRamgqvelnfDLVALDVGETYELRNDV 205
Cdd:TIGR00649  62 IFITHGHEDHIGAVP-YLLHQ--VGFFP--IYGTPltiaLIKSKIkEHGLNVRT---------DLLEIHEGEPVEFGENT 127

                          90       100
                  ....*....|....*....|....*....
gi 224131708  206 VVRPFRTQHVIPSQ---------GYVIYS 225
Cdd:TIGR00649 128 AIEFFRITHSIPDSvgfalhtplGYIVYT 156
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 129-329 5.89e-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: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 129 NFVFITHAHLDHIGGLPMYVASRGLYSLKPPTIFVPP--CIKDDVEKLFDIHRamgqvELNFDLVALDVGETYELrNDVV 206
Cdd:cd07741   55 DAIILSHRHLDHSNDANVLIEAMTEGGFKKRGTLLAPedALNGEPVVLLYYHR-----RKLEEIEILEEGDEYEL-GGIK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 207 VRPFRTQHVIPsqgyVIYSVRkklkkqyIHLKGKQIeklkksgveitdiilspevAFTGDT--TAEYMLDPRNADalrak 284
Cdd:cd07741  129 IEATRHKHSDP----TTYGFI-------FRTSDKKI-------------------GYISDTryFEELIEYYSNCD----- 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 224131708 285 VLITEATFLDEDfttehaRQRGHTHLFEIIENAKWIRSKAILLTH 329
Cdd:cd07741  174 VLIINVTRPRPR------KGVDHLSVEDVEKILKEIKPKLAILTH 212
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 131-223 7.88e-04

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: 40.15  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 131 VFITHAHLDHIGGLP---MYVASRGlyslKPPTIFVPPCIKDDVEKLFDIHRAM--GQVELNFDLVALDVGETYELrNDV 205
Cdd:cd16279   70 VLLTHAHADHIHGLDdlrPFNRLQQ----RPIPVYASEETLDDLKRRFPYFFAAtgGGGVPKLDLHIIEPDEPFTI-GGL 144

                         90
                 ....*....|....*....
gi 224131708 206 VVRPFRTQH-VIPSQGYVI 223
Cdd:cd16279  145 EITPLPVLHgKLPSLGFRF 163
PRK02126 PRK02126
ribonuclease Z; Provisional
 252-334 1.10e-03

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 40.67  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 252 ITDIILSPEVAftgDTTAEYMldpRNADalrakVLITEATFLDEDftTEHARQRGHTHLFEIIENAKWIRSKAILLTHFS 331
Cdd:PRK02126 248 VTDIGYTEENL---ARIVELA---AGVD-----LLFIEAVFLDED--AEKARRKNHLTARQAGRLAREAGVKRLLPFHFS 314


                 ...
gi 224131708 332 SRY 334
Cdd:PRK02126 315 PRY 317
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
129-167 1.49e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.87  E-value: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 224131708 129 NFVFITHAHLDHIGGLPMYVASRglyslKPPTIFVPPCI 167
Cdd:COG1237   59 DAVVLSHGHYDHTGGLPALLELN-----PKAPVYAHPDA 92
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 130-214 1.91e-03

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.13  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708 130 FVFITHAHLDHIGglpmyVASRGLYSLKPPTIFVPPCIKDDVEKLfDIHRAmgqvelnfdlVALDVGETYELrNDVVVRP 209
Cdd:COG2220   51 AVLVTHDHYDHLD-----DATLRALKRTGATVVAPLGVAAWLRAW-GFPRV----------TELDWGESVEL-GGLTVTA 113


                 ....*
gi 224131708 210 FRTQH 214
Cdd:COG2220  114 VPARH 118
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 131-144 3.06e-03

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 38.68  E-value: 3.06e-03
                         10
                 ....*....|....
gi 224131708 131 VFITHAHLDHIGGL 144
Cdd:cd07720   95 VLLTHLHPDHIGGL 108
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
131-230 3.59e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.12  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224131708  131 VFITHAHLDHIGGLPMYVASRGLYSLKPPTIFVPPciKDDVEKLFDIHRAMGQVELNFDLVALDVGETYELRNDVVVRPF 210
Cdd:pfam00753  47 VILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL--LDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLV 124

                          90       100
                  ....*....|....*....|
gi 224131708  211 RTQHVIPSQGYVIYSVRKKL 230
Cdd:pfam00753 125 THGPGHGPGHVVVYYGGGKV 144
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 131-146 3.71e-03

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 38.96  E-value: 3.71e-03
                         10
                 ....*....|....*.
gi 224131708 131 VFITHAHLDHIGGLPM 146
Cdd:COG1782   57 VVLTHAHLDHSGLLPL 72
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 131-145 7.87e-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: 37.53  E-value: 7.87e-03
                         10
                 ....*....|....*
gi 224131708 131 VFITHAHLDHIGGLP 145
Cdd:COG2333   56 LVLTHPDADHIGGLA 70
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 131-179 9.61e-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: 36.74  E-value: 9.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 224131708 131 VFITHAHLDHIGGLPmyvASRGLYSLKPPTIFVPPCIKDDVEKLFDIHR 179
Cdd:cd07722   60 ILLTHWHHDHVGGLP---DVLDLLRGPSPRVYKFPRPEEDEDPDEDGGD 105
 
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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