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Conserved domains on  [gi|22325471|ref|NP_178532|]
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Metallo-hydrolase/oxidoreductase superfamily protein [Arabidopsis thaliana]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

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];
93-330 1.26e-33

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 124.54  E-value: 1.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  93 TCVIV--PELKCVFDIGRCPSRAIQQ--------KFLFITHAHLDHIGGLPMYVASRGLYNLEPP-KIFVPPSIKEDVEK 161
Cdd:COG1234  20 SSYLLeaGGERLLIDCGEGTQRQLLRagldprdiDAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 162 LLEIHRTmgQVELNVELIPLAVGETYELrNDIVVRPFATHHVIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgveit 241
Cdd:COG1234 100 LLKASGT--DLDFPLEFHEIEPGEVFEI-GGFTVTAFPLDHPVPAYGYRFEEPGRS------------------------ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 242 dtilspeIAFTGDTTseymLDPRNADALR-AKVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSS 320
Cdd:COG1234 153 -------LVYSGDTR----PCEALVELAKgADLLIHEATFLDE--EAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSP 219

                       250
                ....*....|....*
gi 22325471 321 RY-----HVEEIREA 330
Cdd:COG1234 220 RYddpeeLLAEARAV 234
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
93-330 1.26e-33

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 124.54  E-value: 1.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  93 TCVIV--PELKCVFDIGRCPSRAIQQ--------KFLFITHAHLDHIGGLPMYVASRGLYNLEPP-KIFVPPSIKEDVEK 161
Cdd:COG1234  20 SSYLLeaGGERLLIDCGEGTQRQLLRagldprdiDAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 162 LLEIHRTmgQVELNVELIPLAVGETYELrNDIVVRPFATHHVIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgveit 241
Cdd:COG1234 100 LLKASGT--DLDFPLEFHEIEPGEVFEI-GGFTVTAFPLDHPVPAYGYRFEEPGRS------------------------ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 242 dtilspeIAFTGDTTseymLDPRNADALR-AKVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSS 320
Cdd:COG1234 153 -------LVYSGDTR----PCEALVELAKgADLLIHEATFLDE--EAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSP 219

                       250
                ....*....|....*
gi 22325471 321 RY-----HVEEIREA 330
Cdd:COG1234 220 RYddpeeLLAEARAV 234
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 89-278 3.15e-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: 118.90  E-value: 3.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  89 GGHETCVIVPELKCVFDIGRCPSRAIQQ--------KFLFITHAHLDHIGGLPMYVASRGLYN-LEPPKIFVPPSIKEDV 159
Cdd:cd16272  16 NTSSYLLETGGTRILLDCGEGTVYRLLKagvdpdklDAIFLSHFHLDHIGGLPTLLFARRYGGrKKPLTIYGPKGIKEFL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 160 EKLLEIHRTMGQVELNVELIPLAVGETYELRNDIVVRPFATHHVIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgve 239
Cdd:cd16272  96 EKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKS---------------------- 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22325471 240 itdtilspeIAFTGDTTSEYMLDPRnadALRAKVLITEA 278
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 ...
 120-330 8.55e-27

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: 107.69  E-value: 8.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   120 FITHAHLDHIGGLPMYVASRGLYN-LEPPKIFVPPSIKEDVEKLLEIHRTMGQVELNVelIPLAVGETYELRNDIVVRPF 198
Cdd:TIGR02651  56 FITHLHGDHILGLPGLLSTMSFQGrKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKI--HEIEEGGLVFEDDGFKVEAF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   199 ATHHVIPSQGYVIYSVRK-------KLQKqyAHLKGKQIEKIKKSGVEIT---DTILSPE-----------IAFTGDT-T 256
Cdd:TIGR02651 134 PLDHSIPSLGYRFEEKDRpgkfdreKAKE--LGIPPGPLYGKLKRGETVTlidGRIIDPEdvlgpprkgrkIAYTGDTrP 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22325471   257 SEYMLD-PRNADalrakVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSSRYH--VEEIREA 330
Cdd:TIGR02651 212 CEEVIEfAKNAD-----LLIHEATFLDE--DKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSdeEELLEEA 281
PRK00055 PRK00055
ribonuclease Z; Reviewed
 119-326 3.20e-14

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 71.75  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  119 LFITHAHLDHIGGLPMYVASRGLY-NLEPPKIFVPPSIKEDVEKLLEIHRTMG--------QVELNVELIplavgetyel 189
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLLSTRSLSgRTEPLTIYGPKGIKEFVETLLRASGSLGyriaekdkPGKLDAEKL---------- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  190 rndivvrpfATHHVIPSQgyviysVRKKLQkqyahlKGKQIEKIKKSGVEITDtILSPE-----IAFTGDTtsEYM--LD 262
Cdd:PRK00055 127 ---------KALGVPPGP------LFGKLK------RGEDVTLEDGRIINPAD-VLGPPrkgrkVAYCGDT--RPCeaLV 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22325471  263 P--RNADalrakVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSSRYHVEE 326
Cdd:PRK00055 183 ElaKGAD-----LLVHEATFGDE--DEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP 241
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 120-318 5.04e-10

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: 58.48  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   120 FITHAHLDHIGGLPMyvasrgLYNLEPPKIFVPPSIKEDVEKLLeiHRTMGQVELNVELIPLAVGETYELRN-DIVVRPF 198
Cdd:pfam12706  33 LLTHDHYDHLAGLLD------LREGRPRPLYAPLGVLAHLRRNF--PYLFLLEHYGVRVHEIDWGESFTVGDgGLTVTAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   199 ATHHvipsqgyviysvrkklqkqyAHLKGKQIEKIKKSGVEITDTILSpeIAFTGDTtsEYMlDPRNADALR-AKVLITE 277
Cdd:pfam12706 105 PARH--------------------GSPRGLDPNPGDTLGFRIEGPGKR--VYYAGDT--GYF-PDEIGERLGgADLLLLD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 22325471   278 ATFLDESFSTEHaqalGHTHISQIIENAKWIRSKTVLLTHF 318
Cdd:pfam12706 160 GGAWRDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 117-211 2.15e-06

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: 47.55  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471    117 KFLFITHAHLDHIGGLPmyvasrGLYNLEPPKIFVPPSIKEDVEKLLEIHRTMGQVELNVEL-IPLAVGETYELrNDIVV 195
Cdd:smart00849  37 DAIILTHGHPDHIGGLP------ELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPdRTLKDGDELDL-GGGEL 109

                           90
                   ....*....|....*..
gi 22325471    196 RPFATHHVIP-SQGYVI 211
Cdd:smart00849 110 EVIHTPGHTPgSIVLYL 126
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
93-330 1.26e-33

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 124.54  E-value: 1.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  93 TCVIV--PELKCVFDIGRCPSRAIQQ--------KFLFITHAHLDHIGGLPMYVASRGLYNLEPP-KIFVPPSIKEDVEK 161
Cdd:COG1234  20 SSYLLeaGGERLLIDCGEGTQRQLLRagldprdiDAIFITHLHGDHIAGLPGLLSTRSLAGREKPlTIYGPPGTKEFLEA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 162 LLEIHRTmgQVELNVELIPLAVGETYELrNDIVVRPFATHHVIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgveit 241
Cdd:COG1234 100 LLKASGT--DLDFPLEFHEIEPGEVFEI-GGFTVTAFPLDHPVPAYGYRFEEPGRS------------------------ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 242 dtilspeIAFTGDTTseymLDPRNADALR-AKVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSS 320
Cdd:COG1234 153 -------LVYSGDTR----PCEALVELAKgADLLIHEATFLDE--EAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSP 219

                       250
                ....*....|....*
gi 22325471 321 RY-----HVEEIREA 330
Cdd:COG1234 220 RYddpeeLLAEARAV 234
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 89-278 3.15e-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: 118.90  E-value: 3.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  89 GGHETCVIVPELKCVFDIGRCPSRAIQQ--------KFLFITHAHLDHIGGLPMYVASRGLYN-LEPPKIFVPPSIKEDV 159
Cdd:cd16272  16 NTSSYLLETGGTRILLDCGEGTVYRLLKagvdpdklDAIFLSHFHLDHIGGLPTLLFARRYGGrKKPLTIYGPKGIKEFL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 160 EKLLEIHRTMGQVELNVELIPLAVGETYELRNDIVVRPFATHHVIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgve 239
Cdd:cd16272  96 EKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKS---------------------- 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22325471 240 itdtilspeIAFTGDTTSEYMLDPRnadALRAKVLITEA 278
Cdd:cd16272 154 ---------IVYSGDTGPCENLVEL---AKGADLLIHEC 180
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 120-330 6.96e-28

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: 109.08  E-value: 6.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 120 FITHAHLDHIGGLPMYVASRGLYNLEPP-KIFVPPSIKEDVEKLLEIHRTMGQVELNVELIPLAVGETYElRNDIVVRPF 198
Cdd:cd07717  55 FITHLHGDHILGLPGLLSTMSLLGRTEPlTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEPDPGLVFE-DDGFTVTAF 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 199 ATHHVIPSQGYVIYSVRKklqkqYAHlkgkqiekikksgveITDTILSPEIAftgdttsEYMldpRNADalrakVLITEA 278
Cdd:cd07717 134 PLDHRVPCFGYRFEEGRK-----IAY---------------LGDTRPCEGLV-------ELA---KGAD-----LLIHEA 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 22325471 279 TFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSSRY-HVEEI-REA 330
Cdd:cd07717 179 TFLDD--DAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYkDPEELlKEA 230
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 120-330 8.55e-27

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: 107.69  E-value: 8.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   120 FITHAHLDHIGGLPMYVASRGLYN-LEPPKIFVPPSIKEDVEKLLEIHRTMGQVELNVelIPLAVGETYELRNDIVVRPF 198
Cdd:TIGR02651  56 FITHLHGDHILGLPGLLSTMSFQGrKEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKI--HEIEEGGLVFEDDGFKVEAF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   199 ATHHVIPSQGYVIYSVRK-------KLQKqyAHLKGKQIEKIKKSGVEIT---DTILSPE-----------IAFTGDT-T 256
Cdd:TIGR02651 134 PLDHSIPSLGYRFEEKDRpgkfdreKAKE--LGIPPGPLYGKLKRGETVTlidGRIIDPEdvlgpprkgrkIAYTGDTrP 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22325471   257 SEYMLD-PRNADalrakVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSSRYH--VEEIREA 330
Cdd:TIGR02651 212 CEEVIEfAKNAD-----LLIHEATFLDE--DKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSdeEELLEEA 281
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 119-333 1.12e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 75.70  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPMYvasRGLYNLEPPKIFVPPSIKEDVEKLLEIHRTMGQVelNVELIPLAVGETYELrNDIVVRPF 198
Cdd:COG1235  72 ILLTHEHADHIAGLDDL---RPRYGPNPIPVYATPGTLEALERRFPYLFAPYPG--KLEFHEIEPGEPFEI-GGLTVTPF 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 199 ATHH-VIPSQGYVIYSVRKKlqkqyahlkgkqiekikksgveitdtilspeIAFTGDTtsEYMlDPRNADALR-AKVLIT 276
Cdd:COG1235 146 PVPHdAGDPVGYRIEDGGKK-------------------------------LAYATDT--GYI-PEEVLELLRgADLLIL 191

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22325471 277 EATFLDESFstehaqalGHTHISQIIENAKWIRSKTVLLTHFSSRYHVEEIREAVLK 333
Cdd:COG1235 192 DATYDDPEP--------GHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDYDELE 240
PRK00055 PRK00055
ribonuclease Z; Reviewed
 119-326 3.20e-14

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 71.75  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  119 LFITHAHLDHIGGLPMYVASRGLY-NLEPPKIFVPPSIKEDVEKLLEIHRTMG--------QVELNVELIplavgetyel 189
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLLSTRSLSgRTEPLTIYGPKGIKEFVETLLRASGSLGyriaekdkPGKLDAEKL---------- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  190 rndivvrpfATHHVIPSQgyviysVRKKLQkqyahlKGKQIEKIKKSGVEITDtILSPE-----IAFTGDTtsEYM--LD 262
Cdd:PRK00055 127 ---------KALGVPPGP------LFGKLK------RGEDVTLEDGRIINPAD-VLGPPrkgrkVAYCGDT--RPCeaLV 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22325471  263 P--RNADalrakVLITEATFLDEsfSTEHAQALGHTHISQIIENAKWIRSKTVLLTHFSSRYHVEE 326
Cdd:PRK00055 183 ElaKGAD-----LLVHEATFGDE--DEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP 241
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 120-318 5.04e-10

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: 58.48  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   120 FITHAHLDHIGGLPMyvasrgLYNLEPPKIFVPPSIKEDVEKLLeiHRTMGQVELNVELIPLAVGETYELRN-DIVVRPF 198
Cdd:pfam12706  33 LLTHDHYDHLAGLLD------LREGRPRPLYAPLGVLAHLRRNF--PYLFLLEHYGVRVHEIDWGESFTVGDgGLTVTAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   199 ATHHvipsqgyviysvrkklqkqyAHLKGKQIEKIKKSGVEITDTILSpeIAFTGDTtsEYMlDPRNADALR-AKVLITE 277
Cdd:pfam12706 105 PARH--------------------GSPRGLDPNPGDTLGFRIEGPGKR--VYYAGDT--GYF-PDEIGERLGgADLLLLD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 22325471   278 ATFLDESFSTEHaqalGHTHISQIIENAKWIRSKTVLLTHF 318
Cdd:pfam12706 160 GGAWRDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 103-211 5.82e-10

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: 57.91  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 103 VFDIGR-CPSRAIQQKF-------LFITHAHLDHIGGLPMYVASRGLYNLEPP-KIFVPPSIKEDVEKLLEIHR------ 167
Cdd:cd07719  31 LVDAGSgVVRRLAQAGLplgdldaVFLTHLHSDHVADLPALLLTAWLAGRKTPlPVYGPPGTRALVDGLLAAYAldidyr 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 22325471 168 ------TMGQVELNVELIPLAVGETYELRNDIVVRPFATHH--VIPSQGYVI 211
Cdd:cd07719 111 arigdeGRPDPGALVEVHEIAAGGVVYEDDGVKVTAFLVDHgpVPPALAYRF 162
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 119-213 2.21e-09

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


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 57.42  E-value: 2.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPmYVASRglynLEPPkIFVPPSIKEDVEKLLEIHRTMGQVELNVelipLAVGETYELrNDIVVRPF 198
Cdd:cd07714  59 IFITHGHEDHIGALP-YLLPE----LNVP-IYATPLTLALIKKKLEEFKLIKKVKLNE----IKPGERIKL-GDFEVEFF 127

                        90       100
                ....*....|....*....|....
gi 22325471 199 ATHHVIP---------SQGYVIYS 213
Cdd:cd07714 128 RVTHSIPdsvglaiktPEGTIVHT 151
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
120-348 8.74e-09

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 56.12  E-value: 8.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 120 FITHAHLDHIGGLPMYVASRglynlePPK-IFVPPSIKEDVEKLLEIHRT---MG----QVELNV-ELIPLAVGETYELR 190
Cdd:COG5212  77 LISHAHLDHIAGLPILSPDD------SPKtIYALPETIDALRNHYFNWVIwpdFTdigsAPHLPKyRYVPLKPGQTFPLG 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 191 N-DIVVRPFATHHVIPSQGYVIYSvrkklQKQYahlkgkqiekikksgveitdtilspeIAFTGDTTSEYMLDPRNADAL 269
Cdd:COG5212 151 GtGLRVTAFPLSHSVPSSAFLIES-----GGGA--------------------------FLYSGDTGPDEVEKSTNLDAL 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 270 --------RAKVL---ITEATFLDEsfsTEHAQALGH----------THISQIIENAkwIRSKTVLLTHFSSRYH-VEEI 327
Cdd:COG5212 200 wealaplvRSKKLkaiIIEVSFPNE---QPDALLFGHltpallleelAKLAKYAGGA--LKGLPVVITHIKPSLKaEEEI 274

                       250       260
                ....*....|....*....|.
gi 22325471 328 REAVLKLQSKVSAKVIPLTEG 348
Cdd:COG5212 275 LKELRALNDALGVNFIILEQG 295
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 89-283 6.79e-08

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: 52.50  E-value: 6.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  89 GGHETCVivpELKC-----VFD----IGRCPSRAIQQKF-----LFITHAHLDHIGGLP----MYVASRGLYnleppkIF 150
Cdd:cd07715  20 GGNTSCV---EVRAggellILDagtgIRELGNELMKEGPpgeahLLLSHTHWDHIQGFPffapAYDPGNRIH------IY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 151 VPPSIKEDVEKLLEihRTMGQ----VEL-----NVELIPLAVGETYELrNDIVVRPFATHHVIPSQGYviysvrkklqkq 221
Cdd:cd07715  91 GPHKDGGSLEEVLR--RQMSPpyfpVPLeellaAIEFHDLEPGEPFSI-GGVTVTTIPLNHPGGALGY------------ 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22325471 222 yahlkgkQIEKIKKSGVEITDTILSPEIAftgdttseyMLDPRNADALR-AKVLITEATFLDE 283
Cdd:cd07715 156 -------RIEEDGKSVVYATDTEHYPDDG---------ESDEALLEFARgADLLIHDAQYTDE 202
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 119-285 1.22e-07

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 51.49  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPMYVASRGLYNL--EPPKIFVPPSIKEDVEKLLEIHRTMGQVEL---NVELIPLAVGETYELrNDI 193
Cdd:cd07740  53 IFITHLHGDHFGGLPFFLLDAQFVAKrtRPLTIAGPPGLRERLRRAMEALFPGSSKVPrrfDLEVIELEPGEPTTL-GGV 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 194 VVRPFATHHVIPSQGYVIYS-VRKKLqkqyahlkgkqiekikksgveitdtilspeIAFTGDTTSEYMLDP--RNADalr 270
Cdd:cd07740 132 TVTAFPVVHPSGALPLALRLeAAGRV------------------------------LAYSGDTEWTDALVPlaRGAD--- 178

                       170
                ....*....|....*
gi 22325471 271 akVLITEATFLDESF 285
Cdd:cd07740 179 --LFICECYFFEKKV 191
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 119-278 4.59e-07

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: 49.36  E-value: 4.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGL-PMYVASRGLYN---LEPPKIFVPPSIKEDVEKLLEIHRTmgqvelnVELIPLAVGETYELrNDIV 194
Cdd:cd07716  54 VVLSHLHPDHCADLgVLQYARRYHPRgarKPPLPLYGPAGPAERLAALYGLEDV-------FDFHPIEPGEPLEI-GPFT 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 195 VRPFATHHVIPSqgyviYSVRkklqkqyahlkgkqIEKIKKSgveitdtilspeIAFTGDT--TSEymLDP--RNADalr 270
Cdd:cd07716 126 ITFFRTVHPVPC-----YAMR--------------IEDGGKV------------LVYTGDTgyCDE--LVEfaRGAD--- 169


                ....*...
gi 22325471 271 akVLITEA 278
Cdd:cd07716 170 --LLLCEA 175
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 120-295 8.41e-07

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: 49.52  E-value: 8.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 120 FITHAHLDHIGGLPMYVASRGLYNLEPPKIFVPPSIKEDVEK----------LLEIHRTMGQVelnVELIPLAVGETYEL 189
Cdd:cd07735  70 LITHAHLDHIAGLPLLSPNDGGQRGSPKTIYGLPETIDALKKhifnwviwpdFTSIPSGKYPY---LRLEPIEPEYPIAL 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 190 rNDIVVRPFATHHVIP-SQGYVIYSVRKklqkqyahlkgkqiekikksgveitdtilspEIAFTGDTTS-EYMLDPRNAD 267
Cdd:cd07735 147 -TGLSVTAFPVSHGVPvSTAFLIRDGGD-------------------------------SFLFFGDTGPdSVSKSPRLDA 194

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 22325471 268 ALRA---------KVLITEATFLDEsfsTEHAQALGH 295
Cdd:cd07735 195 LWRAlaplipkklKAIIIECSFPNS---RPDALLYGH 228
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 117-211 2.15e-06

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: 47.55  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471    117 KFLFITHAHLDHIGGLPmyvasrGLYNLEPPKIFVPPSIKEDVEKLLEIHRTMGQVELNVEL-IPLAVGETYELrNDIVV 195
Cdd:smart00849  37 DAIILTHGHPDHIGGLP------ELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPdRTLKDGDELDL-GGGEL 109

                           90
                   ....*....|....*..
gi 22325471    196 RPFATHHVIP-SQGYVI 211
Cdd:smart00849 110 EVIHTPGHTPgSIVLYL 126
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 118-196 3.46e-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: 43.99  E-value: 3.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 118 FLFITHAHLDHIGGLPMYVAsRGlYNlepPKIFVPP------------SIK---EDVEK-LLEIHRTMGQVELNVEL-IP 180
Cdd:cd16295  54 AVILTHAHLDHSGRLPLLVK-EG-FR---GPIYATPatkdlaelllldSAKiqeEEAEHpPAEPLYTEEDVEKALKHfRP 128

                        90
                ....*....|....*.
gi 22325471 181 LAVGETYELRNDIVVR 196
Cdd:cd16295 129 VEYGEPFEIGPGVKVT 144
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
119-211 3.63e-05

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 45.44  E-value: 3.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPmYVASRglynLEPPkIFVPPSIKEDVEKLLEIHRTMGQVELNVelipLAVGETYELrNDIVVRPF 198
Cdd:COG0595  67 IVLTHGHEDHIGALP-YLLKE----LNVP-VYGTPLTLALLEAKLKEHGLLKKVKLHV----VKPGDRIKF-GPFKVEFF 135

                        90
                ....*....|....
gi 22325471 199 ATHHVIP-SQGYVI 211
Cdd:COG0595 136 RVTHSIPdSLGLAI 149
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 121-278 4.94e-05

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: 43.79  E-value: 4.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 121 ITHAHLDHIGGLPMY---VASRGLYNLEPPKIFVPPSIKEDVEKLL-------------EIHRTMGQVelnvelIPLAVG 184
Cdd:cd16291  61 ISHFHLDHCGALPYFtevVGYDGPIYMTHPTKAICPILLEDYRKIAverkgetnfftsqMIKDCMKKV------IAVNLH 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 185 ETYELRNDIVVRPFATHHVIpsqGYVIYSVRkklqkqYAHLKgkqiekikksgveitdtilspeIAFTGD--TTSEYMLD 262
Cdd:cd16291 135 ETVQVDDELEIKAYYAGHVL---GAAMFYVR------VGDES----------------------VVYTGDynMTPDRHLG 183

                       170
                ....*....|....*.
gi 22325471 263 PRNADALRAKVLITEA 278
Cdd:cd16291 184 AAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 110-280 9.05e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 44.02  E-value: 9.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 110 PSRAIQQKFLFITHAHLDHIGGLPMYVAS--RGLYNLEPP-----KIFVPPSIK---EDVEKLL-----EIHRTMGQVEl 174
Cdd:COG1236  45 PFRPSDVDAVVLTHAHLDHSGALPLLVKEgfRGPIYATPAtadlaRILLGDSAKiqeEEAEAEPlyteeDAERALELFQ- 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 175 nveliPLAVGETYELrNDIVVRPFATHHVIPSqgyviysvrkklqkqyAhlkgkQIEkikksgVEITDTIlspeIAFTGD 254
Cdd:COG1236 124 -----TVDYGEPFEI-GGVRVTFHPAGHILGS----------------A-----QVE------LEVGGKR----IVFSGD 166

                       170       180
                ....*....|....*....|....*....
gi 22325471 255 --TTSEYMLDPrnADAL-RAKVLITEATF 280
Cdd:COG1236 167 ygREDDPLLAP--PEPVpPADVLITESTY 193
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 119-317 1.31e-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: 42.56  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPMYVASRGLYNLEPPKIFVPPS--IKEDVEKLLEIHRtmgqvELNVELIPLAVGETYELrNDIVVR 196
Cdd:cd07741  57 IILSHRHLDHSNDANVLIEAMTEGGFKKRGTLLAPEdaLNGEPVVLLYYHR-----RKLEEIEILEEGDEYEL-GGIKIE 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 197 PFATHHVIPSQ-GYVIysvrkklqkqyaHLKGKQIekikksgVEITDTILSPEIAftgdttseymLDPRNADalrakVLI 275
Cdd:cd07741 131 ATRHKHSDPTTyGFIF------------RTSDKKI-------GYISDTRYFEELI----------EYYSNCD-----VLI 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22325471 276 TEATFLDESFStehaqaLGHTHISQIIENAKWIRSKTVLLTH 317
Cdd:cd07741 177 INVTRPRPRKG------VDHLSVEDVEKILKEIKPKLAILTH 212
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 121-218 1.86e-04

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: 41.93  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 121 ITHAHLDHIGGLPM---YVASRGLYNLEPPKIFVPPSIKEDVEKLLEI------HRTMGQVELNV-ELIPLAVGETYELR 190
Cdd:cd07734  55 ISHFHLDHCGALPYlfrGFIFRGPIYATHPTVALGRLLLEDYVKSAERigqdqsLYTPEDIEEALkHIVPLGYGQSIDLF 134

                        90       100
                ....*....|....*....|....*...
gi 22325471 191 NDIVVRPFATHHVIPSQGYVIYSVRKKL 218
Cdd:cd07734 135 PALSLTAYNAGHVLGAAMWEIQIYGEKL 162
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
117-218 5.10e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 40.81  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   117 KFLFITHAHLDHIGGLPMYVASRGLYNLEPPKIFVPPsiKEDVEKLLEIHRTMGQVELNVELIPLAVGETYELRNDIVVR 196
Cdd:pfam00753  45 DAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL--LDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL 122

                          90       100
                  ....*....|....*....|..
gi 22325471   197 PFATHHVIPSQGYVIYSVRKKL 218
Cdd:pfam00753 123 LVTHGPGHGPGHVVVYYGGGKV 144
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 117-258 5.28e-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: 41.57  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   117 KFLFITHAHLDHIGGLPmYVASRglYNLEPpkIFVPPS----IKEDV-EKLLEIHRTMGQVElnvELIPLAVGEtyelrn 191
Cdd:TIGR00649  60 KGIFITHGHEDHIGAVP-YLLHQ--VGFFP--IYGTPLtialIKSKIkEHGLNVRTDLLEIH---EGEPVEFGE------ 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471   192 DIVVRPFATHHVIPS---------QGYVIYSVRKKLQKQYAHLKGKQIEKIKKSGVE-----ITDTILSPEiafTGDTTS 257
Cdd:TIGR00649 126 NTAIEFFRITHSIPDsvgfalhtpLGYIVYTGDFKFDNTPVIGEPPDLNRIAEIGKKgvlclISDSTNVEN---PGFTPS 202


                  .
gi 22325471   258 E 258
Cdd:TIGR00649 203 E 203
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
118-195 1.74e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.48  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 118 FLFITHAHLDHIGGLPMYVASRGlynlePPKIFVPPSI------KEDVEKLLEIHRTMGQVE-LNVELIPlaVGETYELR 190
Cdd:COG1237  60 AVVLSHGHYDHTGGLPALLELNP-----KAPVYAHPDAfekrysKRPGGKYIGIPFSREELEkLGARLIL--VKEPTEIA 132


                ....*
gi 22325471 191 NDIVV 195
Cdd:COG1237 133 PGVYL 137
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 119-189 1.83e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 39.46  E-value: 1.83e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22325471 119 LFITHAHLDHIGGLPmYVASrglyNLEPPKIFVPPSIK--EDVEKLLEIHRtmgqvELNVELIPLAVGETYEL 189
Cdd:COG2333  56 LVLTHPDADHIGGLA-AVLE----AFPVGRVLVSGPPDtsETYERLLEALK-----EKGIPVRPCRAGDTWQL 118
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 119-211 2.99e-03

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: 38.22  E-value: 2.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPMYvasRGLYNL--EPPKIFVPPSIKEDVEKLLEI--HRTMGQVELNVELIPLAVGETYELrNDIV 194
Cdd:cd16279  70 VLLTHAHADHIHGLDDL---RPFNRLqqRPIPVYASEETLDDLKRRFPYffAATGGGGVPKLDLHIIEPDEPFTI-GGLE 145

                        90
                ....*....|....*...
gi 22325471 195 VRPFATHH-VIPSQGYVI 211
Cdd:cd16279 146 ITPLPVLHgKLPSLGFRF 163
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 119-218 6.27e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 37.59  E-value: 6.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 119 LFITHAHLDHIGGLPmyvasrglynleppkiFVPPSIK----EDVEKLLEIHRTMGQVELNVE--LIPLAVGETYELrND 192
Cdd:cd07732  79 VLLSHAHLDHYGLLN----------------YLRPDIPvymgEATKRILKALLPFFGEGDPVPrnIRVFESGKSFTI-GD 141

                        90       100
                ....*....|....*....|....*..
gi 22325471 193 IVVRPFATHHVIP-SQGYVIYSVRKKL 218
Cdd:cd07732 142 FTVTPYLVDHSAPgAYAFLIEAPGKRI 168
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 95-189 7.19e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.11  E-value: 7.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471  95 VIVPELKcvfdigrcpSRAIQQ-KFLFITHAHLDHIGGLPmYVasrgLYNLEPPKIFVP--PSIKEDVEKLLEIHRtmgq 171
Cdd:cd07731  36 VVVPYLK---------ARGIKKlDYLILTHPDADHIGGLD-AV----LKNFPVKEVYMPgvTHTTKTYEDLLDAIK---- 97

                        90
                ....*....|....*...
gi 22325471 172 vELNVELIPLAVGETYEL 189
Cdd:cd07731  98 -EKGIPVTPCKAGDRWQL 114
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 117-211 9.59e-03

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 36.98  E-value: 9.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325471 117 KFLFITHAHLDHIGGLPMYVASRGlynlepPKIFVPPSIKEDVEKllEIHRTMGQVELNVELIPLAVGETYELrNDIVVR 196
Cdd:COG0491  53 KAVLLTHLHPDHVGGLAALAEAFG------APVYAHAAEAEALEA--PAAGALFGREPVPPDRTLEDGDTLEL-GGPGLE 123

                        90       100
                ....*....|....*....|...
gi 22325471 197 PFAT-----HHV---IPSQGYVI 211
Cdd:COG0491 124 VIHTpghtpGHVsfyVPDEKVLF 146
 
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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