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Conserved domains on  [gi|489146959|ref|WP_003056700|]
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MULTISPECIES: ribonuclease J1 [Streptococcus]

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];
6-555 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 883.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   6 LKPNEVGVFAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGI 85
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  86 PFLLKQANIPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTG 165
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 166 DFKFDFTPV-GDPADLHRMAALGEEGVLCLLSDSTNAEVPTFTNSEKVVGQSILKIIEGIHGRIIFASFASNIYRLQQAA 244
Cdd:COG0595  161 DFKFDQTPVdGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 245 EAAVKTGRKIAVFGRSMEKAIVNGIELGYIKVPKGTFIEANELKNYHANEVLIMCTGSQGESMAALARIANGTHRQVSLQ 324
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 325 PGDTVIFSSSPIPGNTTSVNKLINTIQEAGVEVIHGKVNNIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGL 404
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 405 AMDTGIPKENIFIMENGDVLALTSDSARIAGHFNAQDIYVDGNGIGDIGTAVLRDRRDLSEDGVVLAVATVDFETQMILA 484
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489146959 485 GPDILSRGFIYMRESGDLIRESQRVLFNAIRIALKNKDASIQSVNGAIVNALRPFLYEKTEREPIIIPMVL 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIM 551
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
6-555 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 883.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   6 LKPNEVGVFAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGI 85
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  86 PFLLKQANIPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTG 165
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 166 DFKFDFTPV-GDPADLHRMAALGEEGVLCLLSDSTNAEVPTFTNSEKVVGQSILKIIEGIHGRIIFASFASNIYRLQQAA 244
Cdd:COG0595  161 DFKFDQTPVdGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 245 EAAVKTGRKIAVFGRSMEKAIVNGIELGYIKVPKGTFIEANELKNYHANEVLIMCTGSQGESMAALARIANGTHRQVSLQ 324
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 325 PGDTVIFSSSPIPGNTTSVNKLINTIQEAGVEVIHGKVNNIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGL 404
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 405 AMDTGIPKENIFIMENGDVLALTSDSARIAGHFNAQDIYVDGNGIGDIGTAVLRDRRDLSEDGVVLAVATVDFETQMILA 484
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489146959 485 GPDILSRGFIYMRESGDLIRESQRVLFNAIRIALKNKDASIQSVNGAIVNALRPFLYEKTEREPIIIPMVL 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIM 551
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 11-429 0e+00

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: 541.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   11 VGVFAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLK 90
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   91 QANI-PIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTF-KNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFK 168
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFgENTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  169 FDFTPV-GDPADLHRMAALGEEGVLCLLSDSTNAEVPTFTNSEKVVGQSILKIIEGIHGRIIFASFASNIYRLQQAAEAA 247
Cdd:TIGR00649 161 FDNTPViGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  248 VKTGRKIAVFGRSMEKAIVNGIELGYIKVPKGTFIEANELKNYHANEVLIMCTGSQGESMAALARIANGTHRQVSLQPGD 327
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  328 TVIFSSSPIPGNTT-SVNKLINT-IQEAGVEVIHGkvnnIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGLA 405
Cdd:TIGR00649 321 TVVFSAPPIPGNENiAVSITLDIrLNRAGARVIKG----IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....
gi 489146959  406 MDTGIPKENIFIMENGDVLALTSD 429
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGD 420
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 14-426 4.13e-119

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: 351.71  E-value: 4.13e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  14 FAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQAN 93
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  94 IPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFKFDFTP 173
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 174 V-GDPADLHRMAALGEEGVLCLLSDStnaevptftnsekvvgqsilkiiegihgriifasfasniyrlqqaaeaavktgr 252
Cdd:cd07714  161 VdGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 253 kiavfgrsmekaivngielgyikvpkgtfieanelknyhanevlimctgsqgesmaalariangthrqvslqpgdtvifs 332
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 333 sspipgnttsvnklintiqeagvevihgkvnnIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGLAMDTGIPK 412
Cdd:cd07714  187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 489146959 413 ENIFIMENGDVLAL 426
Cdd:cd07714  235 ENIFLLENGDVLEL 248
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 456-555 4.37e-33

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: 121.84  E-value: 4.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  456 VLRDRRDLSEDGVVLAVATVDFETQMILAGPDILSRGFIYMRESGDLIRESQRVLFNAIRIALKNKDASIQSVNGAIVNA 535
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|
gi 489146959  536 LRPFLYEKTEREPIIIPMVL 555
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIM 100
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 25-185 8.74e-25

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: 101.09  E-value: 8.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959    25 NTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVipdysyivdNLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALA 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKL---------GPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   105 LIRGKLEEHG-----LWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEplGIVIHTPQGKIICTGDFKFDFTPVGDPAD 179
Cdd:smart00849  72 LLKDLLALLGelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPG--SIVLYLPEGKILFTGDLLFAGGDGRTLVD 149


                   ....*.
gi 489146959   180 LHRMAA 185
Cdd:smart00849 150 GGDAAA 155
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 73-166 5.42e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 41.72  E-value: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  73 VITHGHEDHIGGIPFLLKQANIPIyagpLALALIRGKLEEHGLWRdatVHEINHNTELTFKNMSVTFFRTTHS--IPE-- 148
Cdd:PRK00685  45 LLTHGHGDHLGDTVEIAKRTGATV----IANAELANYLSEKGVEK---THPMNIGGTVEFDGGKVKLTPALHSssFIDed 117

                         90       100
                 ....*....|....*....|....*
gi 489146959 149 -------PLGIVIHTPQGKIICTGD 166
Cdd:PRK00685 118 gitylgnPTGFVITFEGKTIYHAGD 142
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
6-555 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 883.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   6 LKPNEVGVFAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGI 85
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  86 PFLLKQANIPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTG 165
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 166 DFKFDFTPV-GDPADLHRMAALGEEGVLCLLSDSTNAEVPTFTNSEKVVGQSILKIIEGIHGRIIFASFASNIYRLQQAA 244
Cdd:COG0595  161 DFKFDQTPVdGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 245 EAAVKTGRKIAVFGRSMEKAIVNGIELGYIKVPKGTFIEANELKNYHANEVLIMCTGSQGESMAALARIANGTHRQVSLQ 324
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 325 PGDTVIFSSSPIPGNTTSVNKLINTIQEAGVEVIHGKVNNIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGL 404
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 405 AMDTGIPKENIFIMENGDVLALTSDSARIAGHFNAQDIYVDGNGIGDIGTAVLRDRRDLSEDGVVLAVATVDFETQMILA 484
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489146959 485 GPDILSRGFIYMRESGDLIRESQRVLFNAIRIALKNKDASIQSVNGAIVNALRPFLYEKTEREPIIIPMVL 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIM 551
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 11-429 0e+00

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: 541.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   11 VGVFAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLK 90
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   91 QANI-PIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTF-KNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFK 168
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFgENTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  169 FDFTPV-GDPADLHRMAALGEEGVLCLLSDSTNAEVPTFTNSEKVVGQSILKIIEGIHGRIIFASFASNIYRLQQAAEAA 247
Cdd:TIGR00649 161 FDNTPViGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  248 VKTGRKIAVFGRSMEKAIVNGIELGYIKVPKGTFIEANELKNYHANEVLIMCTGSQGESMAALARIANGTHRQVSLQPGD 327
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  328 TVIFSSSPIPGNTT-SVNKLINT-IQEAGVEVIHGkvnnIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGLA 405
Cdd:TIGR00649 321 TVVFSAPPIPGNENiAVSITLDIrLNRAGARVIKG----IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....
gi 489146959  406 MDTGIPKENIFIMENGDVLALTSD 429
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGD 420
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 14-426 4.13e-119

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: 351.71  E-value: 4.13e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  14 FAIGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQAN 93
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  94 IPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFKFDFTP 173
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 174 V-GDPADLHRMAALGEEGVLCLLSDStnaevptftnsekvvgqsilkiiegihgriifasfasniyrlqqaaeaavktgr 252
Cdd:cd07714  161 VdGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 253 kiavfgrsmekaivngielgyikvpkgtfieanelknyhanevlimctgsqgesmaalariangthrqvslqpgdtvifs 332
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 333 sspipgnttsvnklintiqeagvevihgkvnnIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGLAMDTGIPK 412
Cdd:cd07714  187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 489146959 413 ENIFIMENGDVLAL 426
Cdd:cd07714  235 ENIFLLENGDVLEL 248
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 456-555 4.37e-33

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: 121.84  E-value: 4.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  456 VLRDRRDLSEDGVVLAVATVDFETQMILAGPDILSRGFIYMRESGDLIRESQRVLFNAIRIALKNKDASIQSVNGAIVNA 535
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|
gi 489146959  536 LRPFLYEKTEREPIIIPMVL 555
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIM 100
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 25-185 8.74e-25

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: 101.09  E-value: 8.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959    25 NTYGIEYQDEIIIVDAGIKFPEDDLLGIDYVipdysyivdNLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALA 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKL---------GPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   105 LIRGKLEEHG-----LWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEplGIVIHTPQGKIICTGDFKFDFTPVGDPAD 179
Cdd:smart00849  72 LLKDLLALLGelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPG--SIVLYLPEGKILFTGDLLFAGGDGRTLVD 149


                   ....*.
gi 489146959   180 LHRMAA 185
Cdd:smart00849 150 GGDAAA 155
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-169 1.09e-19

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: 87.28  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  17 GGLGEIGKNTYGIEYQDEIIIVDAGIKFPED-----------------DLLGIdYVIPDYSYIVDNLDR--VKALVITHG 77
Cdd:cd07732    6 RGTNEIGGNCIEVETGGTRILLDFGLPLDPEskyfdevldflelgllpDIVGL-YRDPLLLGGLRSEEDpsVDAVLLSHA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  78 HEDHIGGIPFLLKqaNIPIYAGPLALALIR--GKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIH 155
Cdd:cd07732   85 HLDHYGLLNYLRP--DIPVYMGEATKRILKalLPFFGEGDPVPRNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYAFLIE 162

                        170
                 ....*....|....
gi 489146959 156 TPQGKIICTGDFKF 169
Cdd:cd07732  163 APGKRIFYTGDFRF 176
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 29-166 1.39e-17

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 82.64  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGIkfpedDL--LGIDYVIpdysyivdNLDRVKALVITHGHEDHIGGIPFL---LKQANIPIYAGPLAL 103
Cdd:COG1235   40 VEADGTRLLIDAGP-----DLreQLLRLGL--------DPSKIDAILLTHEHADHIAGLDDLrprYGPNPIPVYATPGTL 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489146959 104 ALIRGKLE--EHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGD 166
Cdd:COG1235  107 EALERRFPylFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 18-182 1.73e-17

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: 80.79  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  18 GLGEIGKNTYGIEY-QDEIIIVDAGIkFPEDDLLgidyvipdySYIVDNLDRVKALVITHGHEDHIGGIPFLLKQANIPI 96
Cdd:cd06262    4 PVGPLQTNCYLVSDeEGEAILIDPGA-GALEKIL---------EAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  97 YAGPLALALIRGKLEEHGLW------RDATVHEINHNTELTFKNMSVTFFRTT-HSipePLGIVIHTPQGKIICTGDFKF 169
Cdd:cd06262   74 YIHEADAELLEDPELNLAFFgggplpPPEPDILLEDGDTIELGGLELEVIHTPgHT---PGSVCFYIEEEGVLFTGDTLF 150

                        170       180
                 ....*....|....*....|
gi 489146959 170 -------DFtPVGDPADLHR 182
Cdd:cd06262  151 agsigrtDL-PGGDPEQLIE 169
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 25-193 5.54e-16

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: 77.04  E-value: 5.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  25 NTYGIEYQDEIIIVDAGIKFPEDDLLgidyvipdYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALA 104
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 105 LIRGKLEEHGLWRDATV--HEINHNTELTFKNMSVTFFRTT-HSipePLGIVIHTPQGKIICTGD------FKFDFTPVG 175
Cdd:COG0491   88 ALEAPAAGALFGREPVPpdRTLEDGDTLELGGPGLEVIHTPgHT---PGHVSFYVPDEKVLFTGDalfsggVGRPDLPDG 164

                        170       180
                 ....*....|....*....|..
gi 489146959 176 DPAD----LHRMAALGEEGVLC 193
Cdd:COG0491  165 DLAQwlasLERLLALPPDLVIP 186
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 12-157 5.55e-15

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: 73.79  E-value: 5.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  12 GVFAIGGLGEIgkNTYGIEYQDEIIIVDAGIKFPEDDL------LGIDyvipdysyivdnLDRVKALVITHGHEDHIGGI 85
Cdd:cd07721    1 GVYQLPLLPPV--NAYLIEDDDGLTLIDTGLPGSAKRIlkalreLGLS------------PKDIRRILLTHGHIDHIGSL 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489146959  86 PFLLKQANIPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTELTFKNMSVTfFRTTHSIPEPLGI-VIHTP 157
Cdd:cd07721   67 AALKEAPGAPVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRT-LEDGDTLDLAGGLrVIHTP 138
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
29-166 7.70e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 74.46  E-value: 7.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGikfpeddlLGIDYVIPDYSYivdNLDRVKALVITHGHEDHIGGIPFLLK-------QANIPIYAGPL 101
Cdd:COG1234   24 LEAGGERLLIDCG--------EGTQRQLLRAGL---DPRDIDAIFITHLHGDHIAGLPGLLStrslagrEKPLTIYGPPG 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489146959 102 ALALIRGKLEEHGLWRDAT--VHEINHNTELTFKNMSVTFFRTTHSIPePLGIVIHTPQGKIICTGD 166
Cdd:COG1234   93 TKEFLEALLKASGTDLDFPleFHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGD 158
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 17-234 2.44e-13

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 71.76  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  17 GGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLlgidyvipDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQ-ANIP 95
Cdd:COG1236    7 GAAGEVTGSCYLLETGGTRILIDCGLFQGGKER--------NWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEgFRGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  96 IYAGPLALALIR------GKLEEHGL-------WRDA-----TVHEINHNTELTFKNMSVTFFRTTHsIpepLG---IVI 154
Cdd:COG1236   79 IYATPATADLARillgdsAKIQEEEAeaeplytEEDAeraleLFQTVDYGEPFEIGGVRVTFHPAGH-I---LGsaqVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 155 HTPQGKIICTGDFKF-------DFTPVgDPADLhrmaalgeegvlcLLSDST--NAEVPTFTNSEKVVGQSILKIIEGiH 225
Cdd:COG1236  155 EVGGKRIVFSGDYGReddpllaPPEPV-PPADV-------------LITESTygDRLHPPREEVEAELAEWVRETLAR-G 219


                 ....*....
gi 489146959 226 GRIIFASFA 234
Cdd:COG1236  220 GTVLIPAFA 228
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 17-180 3.74e-13

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: 68.25  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  17 GGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDLLGIDYviPDYSYIVDNLDrvkALVITHGHEDHIGGIPFLLKQA-NIP 95
Cdd:cd16295    5 GAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNN--EPFPFDPKEID---AVILTHAHLDHSGRLPLLVKEGfRGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  96 IYAGPLALALIR------GKLEEHGL----------WRDAT-----VHEINHNTELTF-KNMSVTFFRTTHsIpepLG-- 151
Cdd:cd16295   80 IYATPATKDLAElllldsAKIQEEEAehppaeplytEEDVEkalkhFRPVEYGEPFEIgPGVKVTFYDAGH-I---LGsa 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489146959 152 -IVIHTPQGKIIC-TGDFKFDFTP-VGDPADL 180
Cdd:cd16295  156 sVELEIGGGKRILfSGDLGRKNTPlLRDPAPP 187
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
25-169 1.52e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 66.62  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   25 NTYGIEYQDEIIIVDAGIKFPEDDLLgidyvipDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALA 104
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLL-------LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489146959  105 LIRGKLEEHGLWR--------DATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFKF 169
Cdd:pfam00753  80 ELLDEELGLAASRlglpgppvVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLF 152
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 22-177 4.83e-12

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 65.71  E-value: 4.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  22 IGKNTYGIEYQDEIIIVDAGikfpeddLLGIDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPF-LLKQANIPIYAgP 100
Cdd:COG2220    9 LGHATFLIETGGKRILIDPV-------FSGRASPVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLrALKRTGATVVA-P 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 101 LALAlirGKLEEHGLWRdatVHEINHNTELTFKNMSVTFFRTTHSIP-------EPLGIVIHTPQGKIICTGD------- 166
Cdd:COG2220   81 LGVA---AWLRAWGFPR---VTELDWGESVELGGLTVTAVPARHSSGrpdrnggLWVGFVIETDGKTIYHAGDtgyfpem 154

                        170
                 ....*....|....*....
gi 489146959 167 ------FKFD--FTPVGDP 177
Cdd:COG2220  155 keigerFPIDvaLLPIGAY 173
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
17-166 1.23e-10

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 62.67  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  17 GGLGEIGKNTYGI--EYQDEIIIVDAGIKFPE---DDLLGIDYVIPDYSyivdnLDRVKALVITHGHEDHIGGIPFLL-K 90
Cdd:COG5212   21 GGISDGNLTTYLLrpLGSDDYVLLDAGTVVSGlelAEQKGAFKGRQGYV-----LEHIKGYLISHAHLDHIAGLPILSpD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  91 QANIPIYAGPLALALIRGKLEEHGLWRDATV------------HEINHNTELTFKN--MSVTFFRTTHSIPEpLGIVIHT 156
Cdd:COG5212   96 DSPKTIYALPETIDALRNHYFNWVIWPDFTDigsaphlpkyryVPLKPGQTFPLGGtgLRVTAFPLSHSVPS-SAFLIES 174

                        170
                 ....*....|
gi 489146959 157 PQGKIICTGD 166
Cdd:COG5212  175 GGGAFLYSGD 184
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 65-166 1.80e-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: 59.97  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  65 NLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLAL-----------ALIRGKLEEHGLWRDATVHEINHNTE-LTF 132
Cdd:cd16272   47 DPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKPLTIygpkgikefleKLLNFPVEILPLGFPLEIEELEEGGEvLEL 126

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489146959 133 KNMSVTFFRTTHSIPEpLGIVIHTpQGKIIC-TGD 166
Cdd:cd16272  127 GDLKVEAFPVKHSVES-LGYRIEA-EGKSIVySGD 159
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
29-165 3.23e-10

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 61.05  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGikfPED------DLLGIDyvipdysyivdnLDRVKALVITHGHEDHIGGIPFLLKQA-NIPIYAGPL 101
Cdd:COG1237   27 IETEGKRILFDTG---QSDvllknaEKLGID------------LSDIDAVVLSHGHYDHTGGLPALLELNpKAPVYAHPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 102 ALA---------------LIRGKLEEHGlwrdATVHEINHNTELT--------------FKNMSVTFFRTTHSIPEP--- 149
Cdd:COG1237   92 AFEkryskrpggkyigipFSREELEKLG----ARLILVKEPTEIApgvyltgeiprvtdFEKGDPGLYVKEDGGLVPdpf 167

                        170
                 ....*....|....*....
gi 489146959 150 ---LGIVIHTPQGKIICTG 165
Cdd:COG1237  168 ldeQALVIKTDKGLVVITG 186
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 25-168 3.35e-10

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: 58.43  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  25 NTYGIEYQDEIIIVDAGIKFPEDD----LLGIDyvipdysyivdnLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGP 100
Cdd:cd07733   10 NCTYLETEDGKLLIDAGLSGRKITgrlaEIGRD------------PEDIDAILVTHEHADHIKGLGVLARKYNVPIYATA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489146959 101 LALALIRGKLeehGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGDFK 168
Cdd:cd07733   78 GTLRAMERKV---GLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTDLK 142
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 29-170 4.55e-10

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: 59.02  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGikfpeddllgidyviPD--YSYIVDNLDRVKALVITHGHEDHIGGI----PF-LLKQANIPIYAGPL 101
Cdd:cd16279   40 IETGGKNILIDTG---------------PDfrQQALRAGIRKLDAVLLTHAHADHIHGLddlrPFnRLQQRPIPVYASEE 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489146959 102 ALALIRGKL------EEHGLWRDATVHEINHNTELTFKNMSVTFFRtthsipeplgiVIHtpqGKIICTGdFKFD 170
Cdd:cd16279  105 TLDDLKRRFpyffaaTGGGGVPKLDLHIIEPDEPFTIGGLEITPLP-----------VLH---GKLPSLG-FRFG 164
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 354-418 1.32e-09

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: 54.16  E-value: 1.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489146959  354 GVEVIHGKVNNIHTSGHGGQQEQKLMLRLIKPKYFMPVHGEYRMQKVHAGLAMDTGipKENIFIM 418
Cdd:pfam07521   1 GIPVRARIETIDGFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL--GIEVFVP 63
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 29-165 4.52e-09

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: 57.63  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGikfPED------DLLGIDyvipdysyivdnLDRVKALVITHGHEDHIGGIPFLLKQ-ANIPIYAGPL 101
Cdd:cd07713   25 IETEGKKILFDTG---QSGvllhnaKKLGID------------LSDIDAVVLSHGHYDHTGGLKALLELnPKAPVYAHPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 102 AL----ALIRGKLEEHGLWRD------ATVHEINHNTELT----------------FKNMSVTFFRTTHSIPEP----LG 151
Cdd:cd07713   90 AFeprySKRGGGKKGIGIGREelekagARLVLVEEPTEIApgvyltgeiprvtdfeKGNPGLFVKEDGGLVPDDfedeQA 169

                        170
                 ....*....|....
gi 489146959 152 IVIHTPQGKIICTG 165
Cdd:cd07713  170 LVIDTKKGLVVITG 183
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 19-182 2.85e-08

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: 54.28  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  19 LGEIGKNTYGI--EYQDEIIIVDAGikFPEDDLLgidyvipdySYIVDNLDRVKALVITHGHEDHIGGIPFLLKQANIPI 96
Cdd:cd16322    6 LGPLQENTYLVadEGGGEAVLVDPG--DESEKLL---------ARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  97 YAGPLALALIR-----GKLEEHGLWR-DATVHEINHNTELTFKNMSVTFFRTT-HSipePLGIVIHTPQGKIICTGDFKF 169
Cdd:cd16322   75 YLHPDDLPLYEaadlgAKAFGLGIEPlPPPDRLLEDGQTLTLGGLEFKVLHTPgHS---PGHVCFYVEEEGLLFSGDLLF 151

                        170       180
                 ....*....|....*....|
gi 489146959 170 -------DFtPVGDPADLHR 182
Cdd:cd16322  152 qgsigrtDL-PGGDPKAMAA 170
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-166 3.36e-08

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: 54.86  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  32 QDEIIIVDAGIKFPEDdlLGIDYVIPdysYIVD-NLDRVKALVITHGHEDHIGGIPFLLKqaNIPI----YAGPLALALI 106
Cdd:COG2333   20 DGKTILIDTGPRPSFD--AGERVVLP---YLRAlGIRRLDLLVLTHPDADHIGGLAAVLE--AFPVgrvlVSGPPDTSET 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489146959 107 RGKLEEHGLWRDATVHEINHNTELTFKNMSVTFFRTTHSIPEP-------LGIVIHTPQGKIICTGD 166
Cdd:COG2333   93 YERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnsLVLRLTYGGFSFLLTGD 159
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-107 4.57e-08

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 53.30  E-value: 4.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489146959  33 DEIIIVDAGIkfpeDDllgiDYVIPDYSYIVDNLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALALIR 107
Cdd:cd07743   18 KEALLIDSGL----DE----DAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIE 84
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 65-166 5.49e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 52.83  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  65 NLDRVKALVITHGHEDHIGGIPFLL----------KQANIPIYAGPLALALIRGKLEEHGLwrdATVHEINHNTELTFKN 134
Cdd:cd07716   47 DPEDLDAVVLSHLHPDHCADLGVLQyarryhprgaRKPPLPLYGPAGPAERLAALYGLEDV---FDFHPIEPGEPLEIGP 123

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489146959 135 MSVTFFRTTHSIPEpLGIVIHTPQGKIICTGD 166
Cdd:cd07716  124 FTITFFRTVHPVPC-YAMRIEDGGKVLVYTGD 154
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 33-166 1.07e-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: 53.37  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  33 DEIIIVDAG---IKFPEDDLLGIDYVIPDY-SYIVDNldRVKALVITHGHEDHIGGIPFL------LKQANIPIYAGPLA 102
Cdd:cd07735   28 DGDILLDAGtgvGALSLEEMFNDILFPSQKaAYELYQ--RIRHYLITHAHLDHIAGLPLLspndggQRGSPKTIYGLPET 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489146959 103 LALIRgkleEH----------GLWRDA-----TVHEINHNTELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIICTGD 166
Cdd:cd07735  106 IDALK----KHifnwviwpdfTSIPSGkypylRLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGD 180
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 27-166 3.62e-07

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 51.45  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  27 YGIEYQDEIIIVDAGI-----KFPEDDLLGIDYVIPDYSYIVDNLDR-------VKALVITHGHEDHIGGIPFLlkqANI 94
Cdd:cd07729   35 YLIEHPEGTILVDTGFhpdaaDDPGGLELAFPPGVTEEQTLEEQLARlgldpedIDYVILSHLHFDHAGGLDLF---PNA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  95 PIY---------AGPLALA--LIRGKLEEHGLWRDATVHEINHNTELtFKnmSVTFFRT-THSipeP--LGIVIHTPQGK 160
Cdd:cd07729  112 TIIvqraeleyaTGPDPLAagYYEDVLALDDDLPGGRVRLVDGDYDL-FP--GVTLIPTpGHT---PghQSVLVRLPEGT 185


                 ....*.
gi 489146959 161 IICTGD 166
Cdd:cd07729  186 VLLAGD 191
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 29-96 4.19e-07

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: 50.21  E-value: 4.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  29 IEYQDEIIIVDAGIKFPEddllGIDYVIPdY--SYIVDNLDrvkALVITHGHEDHIGGIPFLLKqaNIPI 96
Cdd:cd07731   15 IQTPGKTILIDTGPRDSF----GEDVVVP-YlkARGIKKLD---YLILTHPDADHIGGLDAVLK--NFPV 74
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 67-173 4.85e-07

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: 50.39  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959   67 DRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALALIRG-----KLEEHGLWRdATVHEINHNTELTFKNMSVTFFR 141
Cdd:pfam12706  27 DPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRnfpylFLLEHYGVR-VHEIDWGESFTVGDGGLTVTATP 105

                          90       100       110
                  ....*....|....*....|....*....|..
gi 489146959  142 TTHSIPEPLGIVIHTPQGKIICTGDFKFDFTP 173
Cdd:pfam12706 106 ARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAG 137
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 68-182 9.31e-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: 49.07  E-value: 9.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  68 RVKALVITHGHEDHIGGIPFLLKQANIPIYAGPlalalirgklEEHGLWRDAT--VHEINHNTELTFKNMSVTFfrtths 145
Cdd:cd16275   47 TLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSK----------EEIDYYGFRCpnLIPLEDGDTIKIGDTEITC------ 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489146959 146 ipeplgivIHTP-----------QGKIIcTGDFKF-------DFtPVGDPADLHR 182
Cdd:cd16275  111 --------LLTPghtpgsmcyllGDSLF-TGDTLFiegcgrcDL-PGGDPEEMYE 155
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 66-166 1.22e-06

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: 49.05  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  66 LDRVKALVITHGHEDHIGGIPFLLKQA-------NIPIYaGP-----------LALAL---IRGKLEEHGL---WRDATV 121
Cdd:cd07719   49 LGDLDAVFLTHLHSDHVADLPALLLTAwlagrktPLPVY-GPpgtralvdgllAAYALdidYRARIGDEGRpdpGALVEV 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489146959 122 HEIN-HNTELTFKNMSVTFFRTTHSIPEP-LGIVIHTPQGKIICTGD 166
Cdd:cd07719  128 HEIAaGGVVYEDDGVKVTAFLVDHGPVPPaLAYRFDTPGRSVVFSGD 174
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 17-169 3.05e-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: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  17 GGLGEIGKNTYGIEYQDEIIIVDAGIkFPEDDLLGIDyvIPDYSYIVDNLDrvkALVITHGHEDHIGGIPFLLKQA--NI 94
Cdd:cd07734    4 GGGQEVGRSCFLVEFKGRTVLLDCGM-NPGKEDPEAC--LPQFELLPPEID---AILISHFHLDHCGALPYLFRGFifRG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  95 PIYAGPLALALIRGKLEE-----------HGLWRDATVHE-INHNTELTF-------KNMSVTFFRTTHsIPEPLGIVIH 155
Cdd:cd07734   78 PIYATHPTVALGRLLLEDyvksaerigqdQSLYTPEDIEEaLKHIVPLGYgqsidlfPALSLTAYNAGH-VLGAAMWEIQ 156

                        170
                 ....*....|....
gi 489146959 156 TPQGKIICTGDFKF 169
Cdd:cd07734  157 IYGEKLVYTGDFSN 170
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-186 5.49e-06

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 47.96  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  33 DEIIIVDAGikfpeddllgidYVIPDYSYIVDNLDR-------VKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALAL 105
Cdd:cd16280   31 DGLILIDAL------------NNNEAADLIVDGLEKlgldpadIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959 106 IRGKLEEHGLWRDATVHE----INHNTELTFKNMSVTFFRTthsiPeplGiviHTPqgkiictGDFKFDFtPVGDPADLH 181
Cdd:cd16280   99 MEEPPEEGDNPRWGPPPErdivIKDGDTLTLGDTTITVYLT----P---G---HTP-------GTLSLIF-PVKDGGKTH 160


                 ....*
gi 489146959 182 RmAAL 186
Cdd:cd16280  161 R-AGL 164
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 65-166 9.37e-06

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: 46.48  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  65 NLDR--VKALVITHGHEDHIGGIPFLL--------KQANIPIYAGPLALALIRGKLE------EHGLWR-DATVHEINHN 127
Cdd:cd07740   44 GIDPnaIDAIFITHLHGDHFGGLPFFLldaqfvakRTRPLTIAGPPGLRERLRRAMEalfpgsSKVPRRfDLEVIELEPG 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489146959 128 TELTFKNMSVTFFRTTHSIPEPLGIVIHTPQGKIIC-TGD 166
Cdd:cd07740  124 EPTTLGGVTVTAFPVVHPSGALPLALRLEAAGRVLAySGD 163
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 68-166 1.05e-05

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: 47.06  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  68 RVKALVITHGHEDHIGGIPFLLKQAN-------IPIYAGPLALALIRGKLEEHGLWRDA--TVHEINHNTELTF--KNMS 136
Cdd:cd07717   50 KIDRIFITHLHGDHILGLPGLLSTMSllgrtepLTIYGPKGLKEFLETLLRLSASRLPYpiEVHELEPDPGLVFedDGFT 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 489146959 137 VTFFRTTHSIPEpLGIVIHTPQgKIICTGD 166
Cdd:cd07717  130 VTAFPLDHRVPC-FGYRFEEGR-KIAYLGD 157
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 33-167 1.15e-05

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 46.71  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  33 DEIIIVDAG-IKFPEDDLLGIDYVIPdysyivdnLDRVKALVITHGHEDHIGGIPFLLKQA-NIPIYAGPLALALirgkL 110
Cdd:cd07709   40 EKTALIDTVkEPFFDEFLENLEEVID--------PRKIDYIVVNHQEPDHSGSLPELLELApNAKIVCSKKAARF----L 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489146959 111 EEHGLWRDATVHEINHNTELTFKNMSVTFFRTT--HSiPEplgiVIHT--PQGKIICTGDF 167
Cdd:cd07709  108 KHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPmlHW-PD----TMVTydPEDKILFSGDA 163
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 56-170 1.67e-05

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: 45.20  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  56 IPDYSYIVD-----NLDRVKALVITHGHEDHIGGipfLLKQANIPIYAGPLALALIRGKLEEhglwRDATVHEINHNTEL 130
Cdd:cd16298   19 IPGTGFTVDafqygVIEGCTAYFLTHFHSDHYCG---LTKKFKFPIYCSKITGNLVKSKLKV----EEQYINVLPMNTEC 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489146959 131 TFKNMSVTFFRTTHSiPEPLGIVIHTPQGKIIC-TGDFKFD 170
Cdd:cd16298   92 IVNGVKVVLLDANHC-PGAVMILFRLPSGTLVLhTGDFRAD 131
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 68-162 2.07e-05

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: 45.74  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  68 RVKALVITHGHEDHIGGIPFLLKQaNIPIYAGPLALALirgkLEEHGLWRDATVHEinHNTELTFKNMSV-TFFR-TTHS 145
Cdd:cd16304   63 PVTLAIVTHAHDDRIGGIKALQKR-GIPVYSTKLTAQL----AKKQGYPSPDGILK--DDTTLKFGNTKIeTFYPgEGHT 135

                         90
                 ....*....|....*..
gi 489146959 146 ipePLGIVIHTPQGKII 162
Cdd:cd16304  136 ---ADNIVVWLPQSKIL 149
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 68-157 8.86e-05

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: 43.22  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  68 RVKALVITHGHEDHIGGIPFLLKQ-ANIPIYAGplalalirgklEEHGLwrDATVHEINHNTELTFKNMSVTffrtthsi 146
Cdd:cd07723   43 TLTAILTTHHHWDHTGGNAELKALfPDAPVYGP-----------AEDRI--PGLDHPVKDGDEIKLGGLEVK-------- 101

                         90
                 ....*....|.
gi 489146959 147 peplgiVIHTP 157
Cdd:cd07723  102 ------VLHTP 106
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 68-133 1.00e-04

Bacteroides fragilis CcrA and related 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. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 43.77  E-value: 1.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489146959  68 RVKALVITHGHEDHIGGIPFlLKQANIPIYAGPLALALIRgkleEHGLwrdaTVHEINHNTELTFK 133
Cdd:cd16302   64 KVKAVVPTHFHDDCLGGLKA-FHRRGIPSYANQKTIALAK----EKGL----PVPQHGFSDSLTLK 120
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 60-161 1.29e-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: 43.43  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  60 SYIVDNLDR-VKALVITHGHEDHIGGIPFLLKQAnIPIYAGPLALALirgkLEEHGlwRDATVHEINHNTELTFKNMSVT 138
Cdd:cd16285   54 DWIEKKLGKpVTAAISTHSHDDRTGGIKALNARG-IPTYATALTNEL----AKKEG--KPVPTHSLKGALTLGFGPLEVF 126

                         90       100
                 ....*....|....*....|...
gi 489146959 139 FFRTTHSipePLGIVIHTPQGKI 161
Cdd:cd16285  127 YPGPGHT---PDNIVVWLPKSKI 146
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-104 1.76e-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) 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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 42.48  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  23 GKNTYGIEYQDEIIIVDAGikfPEDDllgidyvipdysyivDNLD---------RVKALVITHGHEDHIGGIPFLLKQAN 93
Cdd:cd16278   17 GTNTYLLGAPDGVVVIDPG---PDDP---------------AHLDallaalgggRVSAILVTHTHRDHSPGAARLAERTG 78

                         90
                 ....*....|.
gi 489146959  94 IPIYAGPLALA 104
Cdd:cd16278   79 APVRAFGPHRA 89
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 16-120 2.91e-04

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 42.50  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  16 IGGLGEIGKNTYGIEYQDEIIIVDAGIKFPEDDllgidyVIPDYSYIVDNLDrVKALVITHGHEDHIGGIPfLLKQANIP 95
Cdd:cd16300   19 MPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTA------QILNWAKQELNLP-VRLAVVTHAHQDKMGGMD-ALHAAGIA 90

                         90       100
                 ....*....|....*....|....*...
gi 489146959  96 IYAGPLA--LALIRGKL-EEHGLWRDAT 120
Cdd:cd16300   91 TYANALSnqLAPQEGLVpAQHSLTFAAE 118
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 69-100 3.62e-04

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 41.77  E-value: 3.62e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489146959  69 VKALVITHGHEDHIGGIPFLLKQANIPIYaGP 100
Cdd:cd07737   47 LKKILLTHGHLDHVGGAAELAEHYGVPII-GP 77
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 23-97 4.65e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 41.36  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  23 GKNTYGIEYQDEIIIVDAGikfpEddllGIDYVIPDYSYIVDNLD--RVKALVITHGHEDHIGGIPFLLK---QANIPIY 97
Cdd:cd07722   17 GTNTYLVGTGKRRILIDTG----E----GRPSYIPLLKSVLDSEGnaTISDILLTHWHHDHVGGLPDVLDllrGPSPRVY 88
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 73-166 5.42e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 41.72  E-value: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  73 VITHGHEDHIGGIPFLLKQANIPIyagpLALALIRGKLEEHGLWRdatVHEINHNTELTFKNMSVTFFRTTHS--IPE-- 148
Cdd:PRK00685  45 LLTHGHGDHLGDTVEIAKRTGATV----IANAELANYLSEKGVEK---THPMNIGGTVEFDGGKVKLTPALHSssFIDed 117

                         90       100
                 ....*....|....*....|....*
gi 489146959 149 -------PLGIVIHTPQGKIICTGD 166
Cdd:PRK00685 118 gitylgnPTGFVITFEGKTIYHAGD 142
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 20-144 5.98e-04

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 41.33  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  20 GEIGKNT--YGIEYQDEIIIVDAG--IKfpeddLLGidyvipdySYIVDNLDRVKA-LVITHGHEDHIGGIPF----LLK 90
Cdd:cd07715   17 VRYGGNTscVEVRAGGELLILDAGtgIR-----ELG--------NELMKEGPPGEAhLLLSHTHWDHIQGFPFfapaYDP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489146959  91 QANIPIYAGPLALALIRGKLEE-----------HGLWRDATVHEINHNTELTFKNMSVTFFRTTH 144
Cdd:cd07715   84 GNRIHIYGPHKDGGSLEEVLRRqmsppyfpvplEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNH 148
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 68-182 1.20e-03

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes 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: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 40.08  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  68 RVKALVITHGHEDHIGGIPFLLKQANIPIYAGPLALAlirgkleehglwrDATVHEINHNTELTFKNMSVTFFRTT-HSi 146
Cdd:cd07724   48 KITYVLETHVHADHVSGARELAERTGAPIVIGEGAPA-------------SFFDRLLKDGDVLELGNLTLEVLHTPgHT- 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489146959 147 PEPLGIVIHTPQGkiICTGDFKF-------DF--TPVGDPADLHR 182
Cdd:cd07724  114 PESVSYLVGDPDA--VFTGDTLFvgdvgrpDLpgEAEGLARQLYD 156
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 69-98 1.40e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 40.56  E-value: 1.40e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489146959  69 VKALVITHGHEDHIGGIPFLLKQA---NIPIYA 98
Cdd:cd07710   57 VKAIIYTHSHPDHFGGAGGFVEEEdsgKVPIIA 89
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 25-85 2.66e-03

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 39.84  E-value: 2.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489146959  25 NTYGIEYQDEIIIVDAGikfpeddlLGiDYVIPDYSYIVDNL-------DRVKALVITHGHEDHIGGI 85
Cdd:cd07720   50 NAFLVRTGGRLILVDTG--------AG-GLFGPTAGKLLANLaaagidpEDIDDVLLTHLHPDHIGGL 108
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-189 2.74e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 39.47  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  69 VKALVITHGHEDHIGGIPfLLKQANIPIYAGPLALALIRGKLEEHGLWRDATVHEINHNTEL-----TFKN-MSVTF--- 139
Cdd:cd16282   53 VRYVVNTHYHGDHTLGNA-AFADAGAPIIAHENTREELAARGEAYLELMRRLGGDAMAGTELvlpdrTFDDgLTLDLggr 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489146959 140 -FRTTHsipepLG-------IVIHTPQGKIICTGDFKF----DFTPVGDPAD----LHRMAALGEE 189
Cdd:cd16282  132 tVELIH-----LGpahtpgdLVVWLPEEGVLFAGDLVFngriPFLPDGSLAGwiaaLDRLLALDAT 192
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-109 3.17e-03

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 39.64  E-value: 3.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489146959  65 NLDRVKALVITHGHEDHIGGIPFLLKQANIPIYAGPL-ALALIRGK 109
Cdd:cd16290   57 RLEDVKLILNSHAHFDHAGGIAALQRDSGATVAASPAgAAALRSGG 102
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 16-93 3.91e-03

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 38.72  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  16 IGGLGEIGKNTYGIEYQDEIIIVDAGI---KFPEDDLLGIDYVipdysyivdNLDRVKALVITHGHEDHIGGIPFLLKQA 92
Cdd:cd16292    6 LGAGQEVGRSCVILEFKGKTIMLDCGIhpgYSGLASLPFFDEI---------DLSEIDLLLITHFHLDHCGALPYFLQKT 76


                 .
gi 489146959  93 N 93
Cdd:cd16292   77 N 77
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 25-98 4.03e-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: 38.43  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  25 NTYGIEYQDEIIIVDAGIKFPED--------DLLGIDYVIPDYsyivdnldrvkaLVITHGHEDHIGGIPFLLKQANIPI 96
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLATEEDaealweglKELGLKPSDIDR------------VLLTHHHPDHIGLAGKLQEKSGATV 83


                 ..
gi 489146959  97 YA 98
Cdd:cd07725   84 YI 85
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 10-166 4.05e-03

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 38.72  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  10 EVGVFAIGGLGEIGKNTYG-------IEYQDEIIIVDAGIKFPEDDLLG-----------IDYVipdysyivdnldrvka 71
Cdd:cd07711    1 EVKVLVEGYARRDSDGGFRasstvtlIKDGGKNILVDTGTPWDRDLLLKalaehglspedIDYV---------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  72 lVITHGHEDHIGGIPfLLKQAniPIYAGPlalALIRGKLEEHGlWRDATVHEINHNteltfknmsVTFFRTT-HSiPEPL 150
Cdd:cd07711   65 -VLTHGHPDHIGNLN-LFPNA--TVIVGW---DICGDSYDDHS-LEEGDGYEIDEN---------VEVIPTPgHT-PEDV 126

                        170
                 ....*....|....*..
gi 489146959 151 GIVIHT-PQGKIICTGD 166
Cdd:cd07711  127 SVLVETeKKGTVAVAGD 143
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-85 6.34e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 38.63  E-value: 6.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489146959  29 IEYQDEIIIVDAGI--KFPeDDLLGIdYVIPDYSYIVDNLDR-------VKALVITHGHEDHIGGI 85
Cdd:cd16281   48 IETGGRNILIDTGIgdKQD-PKFRSI-YVQHSEHSLLKSLARlglspedITDVILTHLHFDHCGGA 111
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 69-134 7.03e-03

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. 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. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 38.03  E-value: 7.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489146959  69 VKALVITHGHEDHIGGIPFLLKQaNIPIYAGPLALALirgkLEEHGlwRDATVHEINHNTELTFKN 134
Cdd:cd16301   66 LKASISTHFHEDRTGGIGYLNSH-SIPTYASELTNQL----LKKNG--KELATHSFSGDEFWLLKG 124
NorV COG0426
Flavorubredoxin [Energy production and conversion];
33-167 7.66e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 38.66  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  33 DEIIIVDA-GIKFPEDDLLGIDYVIpdysyivdNLDRVKALVITHGHEDHIGGIPFLLKQA-NIPIYAGPLALALirgkL 110
Cdd:COG0426   42 EKTALIDTvGESFFEEFLENLSKVI--------DPKKIDYIIVNHQEPDHSGSLPELLELApNAKIVCSKKAARF----L 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489146959 111 EEHGLWRDATVHEINHNTELTFKNMSVTFFRT--THSiPEplgiVIHT--PQGKIICTGDF 167
Cdd:COG0426  110 PHFYGIPDFRFIVVKEGDTLDLGGHTLQFIPApmLHW-PD----TMFTydPEDKILFSGDA 165
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 56-170 8.58e-03

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. 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: 293831  Cd Length: 160  Bit Score: 37.13  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489146959  56 IPDYSYIVD-----NLDRVKALVITHGHEDHIGGI--PFLLKqaniPIYAGPLALALIRGKLeehGLWRDaTVHEINHNT 128
Cdd:cd16273   19 IPGTSFVVDafkygKIPGISAYFLSHFHSDHYGGLtkSWSHG----PIYCSEITANLVKLKL---KVDEE-YIVVLPMNT 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489146959 129 ELTFKNM-SVTFFRTTHSiPEPLGIVIHTPQGKIIC-TGDFKFD 170
Cdd:cd16273   91 PVEIDGDvSVTLLDANHC-PGAVMFLFELPDGRRILhTGDFRAN 133
 
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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