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Conserved domains on  [gi|523688053|ref|WP_020807140|]
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MULTISPECIES: ribonuclease J [Lactobacillus]

Protein Classification

ribonuclease J( domain architecture ID 11426779)

ribonuclease J 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

CATH:  3.40.50.10710|3.60.15.10|3.10.20.580
EC:  3.1.-.-
Gene Ontology:  GO:0004521|GO:0003723|GO:0046872|GO:0004534|GO:0006364|GO:0008270|GO:0006396
PubMed:  11471246|18204464|11471246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-552 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 716.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   1 MSQKIKIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALP 80
Cdd:COG0595    2 KKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  81 YILRDYDIPVFGSKLTIELAKIAVqRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTG 160
Cdd:COG0595   82 YLLKELNVPVYGTPLTLALLEAKL-KEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 161 DFKFDPSAKDGFRTDFVRLSEIAQKGVLALLSDSTNAEANFPNDRQTSIEKYIFNIFENYNGRIIAAAKASNIVRVQEIF 240
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 241 QAAAATGRHVFLTGRDAGKIVYTAMKLGYLNVPKGLLVHSKDLKKIPDKELVILETGRMGEPLKSLQKMATNRHRMIKIK 320
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 321 KGDLVFIATTPSHSVETMVAQTSDMIYRAGGTVKELGRDK-HTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDL 399
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKvHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 400 AIEAGMNKKDIFLPHNGDAYALEKGRFYRTDAVPGEDIMIDGSGVGDVGNIVLRDREVLSDDGVFIAAVTIDRKKKKIIS 479
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523688053 480 EPRVSTRGFVYIKANHALMNGASDVIKEAVNNNFEHKKFDWTELKQDVRNDVEKYLYKQTGRRPVVLPVVMEV 552
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-552 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 716.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   1 MSQKIKIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALP 80
Cdd:COG0595    2 KKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  81 YILRDYDIPVFGSKLTIELAKIAVqRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTG 160
Cdd:COG0595   82 YLLKELNVPVYGTPLTLALLEAKL-KEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 161 DFKFDPSAKDGFRTDFVRLSEIAQKGVLALLSDSTNAEANFPNDRQTSIEKYIFNIFENYNGRIIAAAKASNIVRVQEIF 240
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 241 QAAAATGRHVFLTGRDAGKIVYTAMKLGYLNVPKGLLVHSKDLKKIPDKELVILETGRMGEPLKSLQKMATNRHRMIKIK 320
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 321 KGDLVFIATTPSHSVETMVAQTSDMIYRAGGTVKELGRDK-HTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDL 399
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKvHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 400 AIEAGMNKKDIFLPHNGDAYALEKGRFYRTDAVPGEDIMIDGSGVGDVGNIVLRDREVLSDDGVFIAAVTIDRKKKKIIS 479
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523688053 480 EPRVSTRGFVYIKANHALMNGASDVIKEAVNNNFEHKKFDWTELKQDVRNDVEKYLYKQTGRRPVVLPVVMEV 552
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 5-422 1.24e-123

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: 370.92  E-value: 1.24e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    5 IKIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALPYILR 84
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   85 DYDI-PVFGSKLTIELAKIAVQRENRRRKNDLfHVIDADTEIEF-KNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDF 162
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDL-LEIHEGEPVEFgENTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  163 KFDPSAKDGFRTDFVRLSEIAQKGVLALLSDSTNAEANFPNDRQTSIEKYIFNIFENYNGRIIAAAKASNIVRVQEIFQA 242
Cdd:TIGR00649 160 KFDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  243 AAATGRHVFLTGRDAGKIVYTAMKLGYLNVPKGLLVHSKDLKKIPDKELVILETGRMGEPLKSLQKMATNRHRMIKIKKG 322
Cdd:TIGR00649 240 ARKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  323 DLVFIATTPSHSVETMVAQTSDMIYRAGGTVKELGRdKHTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDLAIE 402
Cdd:TIGR00649 320 DTVVFSAPPIPGNENIAVSITLDIRLNRAGARVIKG-IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAEE 398

                         410       420
                  ....*....|....*....|
gi 523688053  403 AGMNKKDIFLPHNGDAYALE 422
Cdd:TIGR00649 399 EGYPGENIFILRNGEVLEIN 418
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 10-417 2.29e-89

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: 276.21  E-value: 2.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  10 LGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIP 89
Cdd:cd07714    3 LGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  90 VFGSKLTIELAKiAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDFKFDPSAK 169
Cdd:cd07714   83 IYATPLTLALIK-KKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 170 DGFRTDFVRLSEIAQKGVLALLSDStnaeanfpndrqtsiekyifnifenyngriiaaakasnivrvqeifqaaaatgrh 249
Cdd:cd07714  162 DGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 250 vfltgrdagkivytamklgylnvpkgllvhskdlkkipdkelviletgrmgeplkslqkmatnrhrmikikkgdlvfiat 329
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 330 tpshsvetmvaqtsdmiyraggtvkelgrdKHTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDLAIEAGMNKKD 409
Cdd:cd07714  187 ------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPEEN 236


                 ....*...
gi 523688053 410 IFLPHNGD 417
Cdd:cd07714  237 IFLLENGD 244
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 451-552 9.71e-36

Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers.


Pssm-ID: 436030  Cd Length: 102  Bit Score: 129.54  E-value: 9.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  451 VLRDREVLSDDGVFIAAVTIDRKKKKIISEPRVSTRGFVYIKANHALMNGASDVIKEAVNNNFEHKKFDWTELKQDVRND 530
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 523688053  531 VEKYLYKQTGRRPVVLPVVMEV 552
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 19-193 1.26e-20

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: 89.53  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    19 NMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDldffrdygdKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIE 98
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---------KIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    99 LAK----IAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDIstKEGEIVYTGDFKFDPSAKDGFRT 174
Cdd:smart00849  72 LLKdllaLLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVD 149

                          170
                   ....*....|....*....
gi 523688053   175 DFVRLSEIAQKGVLALLSD 193
Cdd:smart00849 150 GGDAAASDALESLLKLLKL 168
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-552 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 716.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   1 MSQKIKIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALP 80
Cdd:COG0595    2 KKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  81 YILRDYDIPVFGSKLTIELAKIAVqRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTG 160
Cdd:COG0595   82 YLLKELNVPVYGTPLTLALLEAKL-KEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 161 DFKFDPSAKDGFRTDFVRLSEIAQKGVLALLSDSTNAEANFPNDRQTSIEKYIFNIFENYNGRIIAAAKASNIVRVQEIF 240
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 241 QAAAATGRHVFLTGRDAGKIVYTAMKLGYLNVPKGLLVHSKDLKKIPDKELVILETGRMGEPLKSLQKMATNRHRMIKIK 320
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 321 KGDLVFIATTPSHSVETMVAQTSDMIYRAGGTVKELGRDK-HTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDL 399
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKvHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 400 AIEAGMNKKDIFLPHNGDAYALEKGRFYRTDAVPGEDIMIDGSGVGDVGNIVLRDREVLSDDGVFIAAVTIDRKKKKIIS 479
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523688053 480 EPRVSTRGFVYIKANHALMNGASDVIKEAVNNNFEHKKFDWTELKQDVRNDVEKYLYKQTGRRPVVLPVVMEV 552
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 5-422 1.24e-123

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: 370.92  E-value: 1.24e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    5 IKIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALPYILR 84
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   85 DYDI-PVFGSKLTIELAKIAVQRENRRRKNDLfHVIDADTEIEF-KNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDF 162
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDL-LEIHEGEPVEFgENTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  163 KFDPSAKDGFRTDFVRLSEIAQKGVLALLSDSTNAEANFPNDRQTSIEKYIFNIFENYNGRIIAAAKASNIVRVQEIFQA 242
Cdd:TIGR00649 160 KFDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  243 AAATGRHVFLTGRDAGKIVYTAMKLGYLNVPKGLLVHSKDLKKIPDKELVILETGRMGEPLKSLQKMATNRHRMIKIKKG 322
Cdd:TIGR00649 240 ARKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  323 DLVFIATTPSHSVETMVAQTSDMIYRAGGTVKELGRdKHTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDLAIE 402
Cdd:TIGR00649 320 DTVVFSAPPIPGNENIAVSITLDIRLNRAGARVIKG-IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAEE 398

                         410       420
                  ....*....|....*....|
gi 523688053  403 AGMNKKDIFLPHNGDAYALE 422
Cdd:TIGR00649 399 EGYPGENIFILRNGEVLEIN 418
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 10-417 2.29e-89

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: 276.21  E-value: 2.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  10 LGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIP 89
Cdd:cd07714    3 LGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  90 VFGSKLTIELAKiAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDFKFDPSAK 169
Cdd:cd07714   83 IYATPLTLALIK-KKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 170 DGFRTDFVRLSEIAQKGVLALLSDStnaeanfpndrqtsiekyifnifenyngriiaaakasnivrvqeifqaaaatgrh 249
Cdd:cd07714  162 DGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 250 vfltgrdagkivytamklgylnvpkgllvhskdlkkipdkelviletgrmgeplkslqkmatnrhrmikikkgdlvfiat 329
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053 330 tpshsvetmvaqtsdmiyraggtvkelgrdKHTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDLAIEAGMNKKD 409
Cdd:cd07714  187 ------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPEEN 236


                 ....*...
gi 523688053 410 IFLPHNGD 417
Cdd:cd07714  237 IFLLENGD 244
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 451-552 9.71e-36

Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers.


Pssm-ID: 436030  Cd Length: 102  Bit Score: 129.54  E-value: 9.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  451 VLRDREVLSDDGVFIAAVTIDRKKKKIISEPRVSTRGFVYIKANHALMNGASDVIKEAVNNNFEHKKFDWTELKQDVRND 530
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 523688053  531 VEKYLYKQTGRRPVVLPVVMEV 552
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 19-193 1.26e-20

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: 89.53  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    19 NMYAVQVEDEIFIMDAGLKYPDSSLLGIDVVIPDldffrdygdKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIE 98
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---------KIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053    99 LAK----IAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDIstKEGEIVYTGDFKFDPSAKDGFRT 174
Cdd:smart00849  72 LLKdllaLLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVD 149

                          170
                   ....*....|....*....
gi 523688053   175 DFVRLSEIAQKGVLALLSD 193
Cdd:smart00849 150 GGDAAASDALESLLKLLKL 168
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 6-164 5.77e-17

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: 79.58  E-value: 5.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   6 KIMILGGARENGKNMYAVQVEDEIFIMDAGLKYPDSSLLGIDV-------VIPDLD----------FFRDYGD-KIAGIF 67
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDPESKYFDEVldflelgLLPDIVglyrdplllgGLRSEEDpSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  68 LTHGHADSIGALPYIlrDYDIPVFGSKLTIELAKIAVQ--RENRRRKNDlFHVIDADTEIEFKNANVSFFKTTHSIPDSL 145
Cdd:cd07732   81 LSHAHLDHYGLLNYL--RPDIPVYMGEATKRILKALLPffGEGDPVPRN-IRVFESGKSFTIGDFTVTPYLVDHSAPGAY 157

                        170
                 ....*....|....*....
gi 523688053 146 GIDISTKEGEIVYTGDFKF 164
Cdd:cd07732  158 AFLIEAPGKRIFYTGDFRF 176
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 6-176 6.93e-16

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 79.85  E-value: 6.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   6 KIMILGGARENGKNMYAVQVEDEIFIMDAGL--KYPDSSLLGIDVVIPDLDFfrdygdkiagIFLTHGHADSIGALPYIL 83
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLfqGGKERNWPPFPFRPSDVDA----------VVLTHAHLDHSGALPLLV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  84 RD-YDIPVFGSKLTIELAKI------AVQRENRR-----------RKNDLFHVIDADTEIEFKNANVSFFKTTHsIPDSL 145
Cdd:COG1236   72 KEgFRGPIYATPATADLARIllgdsaKIQEEEAEaeplyteedaeRALELFQTVDYGEPFEIGGVRVTFHPAGH-ILGSA 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 523688053 146 GIDISTKEGEIVYTGDFKFDPsakDGFRTDF 176
Cdd:COG1236  151 QVELEVGGKRIVFSGDYGRED---DPLLAPP 178
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 9-167 1.41e-15

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: 75.57  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   9 ILGGARENGKNMYAVQVEDEIFIMDAGLkYPDSSLLGIDvviPDLDFFRDYGDkIAGIFLTHGHADSIGALPYILRD-YD 87
Cdd:cd16295    3 FLGAAREVTGSCYLLETGGKRILLDCGL-FQGGKELEEL---NNEPFPFDPKE-IDAVILTHAHLDHSGRLPLLVKEgFR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  88 IPVFGSKLTIELAKIA------VQRENRRRKN--------------DLFHVIDADTEIEF-KNANVSFFKTTHsIPDSLG 146
Cdd:cd16295   78 GPIYATPATKDLAELLlldsakIQEEEAEHPPaeplyteedvekalKHFRPVEYGEPFEIgPGVKVTFYDAGH-ILGSAS 156

                        170       180
                 ....*....|....*....|..
gi 523688053 147 IDISTKEGE-IVYTGDFKFDPS 167
Cdd:cd16295  157 VELEIGGGKrILFSGDLGRKNT 178
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-176 1.53e-13

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 69.24  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  19 NMYAVQVED-EIFIMDAGlkypDSSLLGIdvvipdLDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTI 97
Cdd:cd06262   11 NCYLVSDEEgEAILIDPG----AGALEKI------LEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  98 ELAKIAVQRENRRRKNDL-----FHVIDADTEIEFKNANVSFFKTT-HSiPDSLGIDIstKEGEIVYTGDFKFDPSakdG 171
Cdd:cd06262   81 ELLEDPELNLAFFGGGPLpppepDILLEDGDTIELGGLELEVIHTPgHT-PGSVCFYI--EEEGVLFTGDTLFAGS---I 154


                 ....*
gi 523688053 172 FRTDF 176
Cdd:cd06262  155 GRTDL 159
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 21-161 7.82e-13

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.77  E-value: 7.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  21 YAVQVEDEIFIMDAGlkypdssllgidvviPDL-DFFRDYG---DKIAGIFLTHGHADSIGALPYILRDY---DIPVFGS 93
Cdd:COG1235   38 ILVEADGTRLLIDAG---------------PDLrEQLLRLGldpSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYAT 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523688053  94 KLTIE-LAKIAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGD 161
Cdd:COG1235  103 PGTLEaLERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
21-161 1.01e-12

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 68.30  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  21 YAVQVEDEIFIMDAG-------LKYpdssllGIDVvipdldffrdygDKIAGIFLTHGHADSIGALPYIL-------RDY 86
Cdd:COG1234   22 YLLEAGGERLLIDCGegtqrqlLRA------GLDP------------RDIDAIFITHLHGDHIAGLPGLLstrslagREK 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523688053  87 DIPVFGSKLTIELAKIAVQRENRRRKNDL-FHVIDADTEIEFKNANVSFFKTTHSIPdSLGIDISTKEGEIVYTGD 161
Cdd:COG1234   84 PLTIYGPPGTKEFLEALLKASGTDLDFPLeFHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGD 158
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-161 1.14e-11

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: 64.33  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  19 NMYAVQVEDEIFIMDAGLKYPDSSLLgidvvipdLDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIE 98
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523688053  99 LAKIAVQRENRRRKN-DLFHVIDADTEIEFKNANVSFFKTT-HSiPDSLGIDIstKEGEIVYTGD 161
Cdd:COG0491   88 ALEAPAAGALFGREPvPPDRTLEDGDTLELGGPGLEVIHTPgHT-PGHVSFYV--PDEKVLFTGD 149
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 21-161 5.61e-10

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: 58.81  E-value: 5.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  21 YAVQVEDEIFIMDAGlkyPDS--SLLGIDVVIPDLDFfrdygdkiagIFLTHGHADSIGALPYIL-------RDYDIPVF 91
Cdd:cd16272   20 YLLETGGTRILLDCG---EGTvyRLLKAGVDPDKLDA----------IFLSHFHLDHIGGLPTLLfarryggRKKPLTIY 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523688053  92 G---SKLTIELAKIAVQRENRRRKNDLFHVIDADTEI-EFKNANVSFFKTTHSIPdSLGIDISTKEGEIVYTGD 161
Cdd:cd16272   87 GpkgIKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVlELGDLKVEAFPVKHSVE-SLGYRIEAEGKSIVYSGD 159
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 61-161 6.76e-09

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 55.53  E-value: 6.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  61 DKIAGIFLTHGHAD---SIGALPYILRDYD-------IPVFGSKLTIELAKIAVQRENRRRkndlFHVIDADTEIEFKNA 130
Cdd:cd07716   49 EDLDAVVLSHLHPDhcaDLGVLQYARRYHPrgarkppLPLYGPAGPAERLAALYGLEDVFD----FHPIEPGEPLEIGPF 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 523688053 131 NVSFFKTTHSIPdSLGIDISTKEGEIVYTGD 161
Cdd:cd07716  125 TITFFRTVHPVP-CYAMRIEDGGKVLVYTGD 154
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 61-166 7.04e-08

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: 52.86  E-value: 7.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  61 DKIAGIFLTHGHADSIGALP-----YILRDYDIPVFGSKLTIELAK----IAVQRENRRRKNDL-FHVIDADTEIEFKNA 130
Cdd:cd16279   65 RKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASEETLDDLKrrfpYFFAATGGGGVPKLdLHIIEPDEPFTIGGL 144

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 523688053 131 NVSFFKTTHSIPDSLGIDIstkeGEIVYTGDFKFDP 166
Cdd:cd16279  145 EITPLPVLHGKLPSLGFRF----GDFAYLTDVSEIP 176
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 53-134 1.49e-07

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 51.38  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  53 LDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIELAKIavqrenrrRKNDLfHVIDADTEIEFKNANV 132
Cdd:cd16275   38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGF--------RCPNL-IPLEDGDTIKIGDTEI 108


                 ..
gi 523688053 133 SF 134
Cdd:cd16275  109 TC 110
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
19-164 1.80e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 51.99  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   19 NMYAVQVEDEIFIMDAGLKYPDSSLLgidvvipDLDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTI- 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLL-------LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAr 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523688053   98 -----ELAKIAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSI-PDSLGIDISTKEGEIVYTGDFKF 164
Cdd:pfam00753  80 elldeELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPgHGPGHVVVYYGGGKVLFTGDLLF 152
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 361-413 3.23e-07

Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. This, the fifth motif, appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 which are involved in the processing of mRNA. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases.


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 47.61  E-value: 3.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 523688053  361 HTSGHATGRDLQLLIDTLKPKFLIPVIGEYRLLEIHKDLAIEAgmNKKDIFLP 413
Cdd:pfam07521  13 GFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEE--LGIEVFVP 63
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-91 4.78e-07

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 50.68  E-value: 4.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523688053  19 NMYAVQVEDEIFIMDAGLKypdSSLLGIDVVIPDLDFFrdyGDKIAGIFLTHGHADSIGALPYILRDYDIPVF 91
Cdd:cd07721   12 NAYLIEDDDGLTLIDTGLP---GSAKRILKALRELGLS---PKDIRRILLTHGHIDHIGSLAALKEAPGAPVY 78
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 21-161 6.93e-07

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: 49.82  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  21 YAVQVEDEIFIMDAGlkypDSSL-----LGIDVvipdldffrdygDKIAGIFLTHGHADSIGALPYIL-------RDYDI 88
Cdd:cd07719   21 TLVVVGGRVYLVDAG----SGVVrrlaqAGLPL------------GDLDAVFLTHLHSDHVADLPALLltawlagRKTPL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  89 PVFG--------SKLTIELAKIAVQR-----ENRRRKNDLFHVID-ADTEIEFKNAN--VSFFKTTHS-IPDSLGIDIST 151
Cdd:cd07719   85 PVYGppgtralvDGLLAAYALDIDYRarigdEGRPDPGALVEVHEiAAGGVVYEDDGvkVTAFLVDHGpVPPALAYRFDT 164

                        170
                 ....*....|
gi 523688053 152 KEGEIVYTGD 161
Cdd:cd07719  165 PGRSVVFSGD 174
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 33-161 1.04e-06

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: 50.24  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  33 DAGLKYPDSSllGIDVVIPdldFFRDYG-DKIAGIFLTHGHADSIGALPYILRDYDI-PVFGSKLTIELAKIAVQRENRR 110
Cdd:COG2333   27 DTGPRPSFDA--GERVVLP---YLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVgRVLVSGPPDTSETYERLLEALK 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 523688053 111 RKNDLFHVIDADTEIEFKNANVSFFKTTHSIP-------DSLGIDISTKEGEIVYTGD 161
Cdd:COG2333  102 EKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLegsdennNSLVLRLTYGGFSFLLTGD 159
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 10-194 2.61e-06

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: 48.10  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  10 LGGARENGKNMYAVQVEDEIFIMDAGLkypDSSLLGIDVVIPDLDFFRDygdKIAGIFLTHGHADSIGALPYILR--DYD 87
Cdd:cd07734    3 LGGGQEVGRSCFLVEFKGRTVLLDCGM---NPGKEDPEACLPQFELLPP---EIDAILISHFHLDHCGALPYLFRgfIFR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  88 IPVFGSKLTIELAKIaVQRENRRRKNDLFHVIDADT--EIE-----------------FKNANVSFFKTTHsIPDSLGID 148
Cdd:cd07734   77 GPIYATHPTVALGRL-LLEDYVKSAERIGQDQSLYTpeDIEealkhivplgygqsidlFPALSLTAYNAGH-VLGAAMWE 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 523688053 149 ISTKEGEIVYTGDFKFDPsakdgfrTDFVRLSEIAQKGVLALLSDS 194
Cdd:cd07734  155 IQIYGEKLVYTGDFSNTE-------DRLLPAASILPPRPDLLITES 193
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 27-206 3.41e-06

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: 48.75  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  27 DEIFIMDAGLKYPDSSLLGIDVVIPDLDFFRDYG--DKIAGIFLTHGHADSIGALP------YILRDYDIPVFGSKLTIE 98
Cdd:cd07735   28 DGDILLDAGTGVGALSLEEMFNDILFPSQKAAYElyQRIRHYLITHAHLDHIAGLPllspndGGQRGSPKTIYGLPETID 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  99 LAK-----------IAVQRENRRRKNDLfHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDFKFDPS 167
Cdd:cd07735  108 ALKkhifnwviwpdFTSIPSGKYPYLRL-EPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGDTGPDSV 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 523688053 168 AKDgFRTDFV--RLSEIAQKGVLALLsdstnAEANFPNDRQ 206
Cdd:cd07735  187 SKS-PRLDALwrALAPLIPKKLKAII-----IECSFPNSRP 221
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 19-163 4.23e-06

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 46.87  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  19 NMYAVQVEDEIFIMDAGLkypdsSLLGIDVVIPDLDffRDYGDkIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIE 98
Cdd:cd07733   10 NCTYLETEDGKLLIDAGL-----SGRKITGRLAEIG--RDPED-IDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523688053  99 lakiAVQRENRRRKNDLFHVIDADTEIEFKNANVSFFKTTHSIPDSLGIDISTKEGEIVYTGDFK 163
Cdd:cd07733   82 ----AMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTDLK 142
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 23-161 9.81e-06

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: 46.36  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  23 VQVEDEIFIMDAGLKYPDSSllgiDVVIPdldFFRDYG-DKIAGIFLTHGHADSIGALPYILRDYDI-PVFGSKLTIELA 100
Cdd:cd07731   15 IQTPGKTILIDTGPRDSFGE----DVVVP---YLKARGiKKLDYLILTHPDADHIGGLDAVLKNFPVkEVYMPGVTHTTK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523688053 101 KIAVQRENRRRKNDLFHVIDADTEIEFKNANVSFF-----KTTHSIPDSLGIDISTKEGEIVYTGD 161
Cdd:cd07731   88 TYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLsppkdDYDDLNNNSCVLRLTYGGTSFLLTGD 153
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 57-166 9.27e-05

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: 43.84  E-value: 9.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053   57 RDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIE-LAKIAVQRENRRRKNDLFHVIDADTEIEFKNANVSFF 135
Cdd:pfam12706  23 RLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAhLRRNFPYLFLLEHYGVRVHEIDWGESFTVGDGGLTVT 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 523688053  136 KTT--HSIP--------DSLGIDISTKEGEIVYTGDFKFDP 166
Cdd:pfam12706 103 ATParHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFP 143
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 59-188 1.24e-04

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


Pssm-ID: 293824  Cd Length: 189  Bit Score: 43.05  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  59 YGDKIAGIFLTHGHADSI-GALPYILRDYDIPVFGSKLTIE--LAKI-AVQRENRRRKNDLFHVIDADT--EIEFKNANV 132
Cdd:cd07738   45 SPRLVDHVILTHCHADHDaGTFQKILEEEKITLYTTRTINEsfLRKYaALTGLPPDFLEELFDFRPVIIgeKTKINGAEF 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 523688053 133 SFFKTTHSIPdSLGIDISTKEGEIVYTGDFKFDPSakdgfrtdfvRLSEIAQKGVL 188
Cdd:cd07738  125 EFDYSFHSIP-TIRFKVSYGGKSIAYSGDTRYDPD----------GLKSLYEQGIL 169
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 50-170 1.61e-04

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. 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: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 42.50  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  50 IPDLDFFRD---YGdKIAGI---FLTHGHADSIGALPyilRDYDIPVFGSKLTIELAKiavqrENRRRKNDLFHVIDADT 123
Cdd:cd16298   19 IPGTGFTVDafqYG-VIEGCtayFLTHFHSDHYCGLT---KKFKFPIYCSKITGNLVK-----SKLKVEEQYINVLPMNT 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 523688053 124 EIEFKNANVSFFKTTHSiPDSLGIDISTKEGEIV-YTGDFKFDPSAKD 170
Cdd:cd16298   90 ECIVNGVKVVLLDANHC-PGAVMILFRLPSGTLVlHTGDFRADPSMER 136
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 46-94 3.08e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 41.68  E-value: 3.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 523688053  46 IDVVIPD--LDFFRDYGDKIAGIFLTHGHADSIGALPYILRDY-DIPVFGSK 94
Cdd:cd07723   25 VDPGEAEpvLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPA 76
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 23-160 4.89e-04

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 42.22  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  23 VQVEDEIFIMDAGlkyPDSSL------LGIDVvipdldffrdygDKIAGIFLTHGHADSIGALPYILRDY-DIPVF---- 91
Cdd:cd07713   25 IETEGKKILFDTG---QSGVLlhnakkLGIDL------------SDIDAVVLSHGHYDHTGGLKALLELNpKAPVYahpd 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  92 -----GSKLTIELAKIAVQRENRRRKNDLFHVIDADTEI----------------EFKNANVSFFKTTHSIPD------S 144
Cdd:cd07713   90 afeprYSKRGGGKKGIGIGREELEKAGARLVLVEEPTEIapgvyltgeiprvtdfEKGNPGLFVKEDGGLVPDdfedeqA 169

                        170
                 ....*....|....*.
gi 523688053 145 LGIDisTKEGEIVYTG 160
Cdd:cd07713  170 LVID--TKKGLVVITG 183
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-95 5.48e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 41.36  E-value: 5.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  26 EDEIFIMDAGLkyPDSSLLGIDVVIpdldffRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKL 95
Cdd:cd07743   17 DKEALLIDSGL--DEDAGRKIRKIL------EELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKI 78
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 68-135 6.75e-04

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 41.50  E-value: 6.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523688053  68 LTHGHADSIGALPyILRDYDIPVFGSKLTIELAKiavqRENRRRKNdlfHVIDADTEIEFKNANVSFF 135
Cdd:cd16304   69 VTHAHDDRIGGIK-ALQKRGIPVYSTKLTAQLAK----KQGYPSPD---GILKDDTTLKFGNTKIETF 128
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 62-170 9.03e-04

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: 41.28  E-value: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  62 KIAGIFLTHGHADSIGALPYIL-------RDYDIPVFGSKLTIELAKIAVQRENRRRKNDL-FHVIDADTEIEFKNAN-- 131
Cdd:cd07717   50 KIDRIFITHLHGDHILGLPGLLstmsllgRTEPLTIYGPKGLKEFLETLLRLSASRLPYPIeVHELEPDPGLVFEDDGft 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 523688053 132 VSFFKTTHSIPdSLG--IDISTKegeIVYTGDFKFDPSAKD 170
Cdd:cd07717  130 VTAFPLDHRVP-CFGyrFEEGRK---IAYLGDTRPCEGLVE 166
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 53-101 9.84e-04

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 40.73  E-value: 9.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 523688053  53 LDFFRD-YGDKIAGIFLTHGHADSIGALPYiLRDYDIPVFGSKLTIELAK 101
Cdd:cd16285   53 LDWIEKkLGKPVTAAISTHSHDDRTGGIKA-LNARGIPTYATALTNELAK 101
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 19-96 2.70e-03

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 39.20  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523688053  19 NMYAVQVEDEIFIMDAGLKYPDSSLLGidvvipdLDFFRDYGDKIAGI---FLTHGHADSIGALPYILRDYDIPVFGSKL 95
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLATEEDAEAL-------WEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEKSGATVYILDV 88


                 .
gi 523688053  96 T 96
Cdd:cd07725   89 T 89
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 53-100 2.71e-03

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 39.25  E-value: 2.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 523688053  53 LDFFRDYGDKIAGIFLTHGHADSIGALPYILRDYDIPVFGSKLTIELA 100
Cdd:cd16322   37 LARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLY 84
 
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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