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Conserved domains on  [gi|489471876|ref|WP_003376966|]
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MULTISPECIES: ribonuclease J [Clostridium]

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];
3-555 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 956.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   3 KEKDKIKIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGAL 82
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  83 PYVLKDLNVPVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTG 162
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 163 DFKIDYTPIDGQVADLARFVELGKKGVIAMLADSTNVERQGYTMSERTVGKTFENIFSKAEGRIIVATFASNIHRIQQII 242
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 243 TASEKIGRKVAVSGRSMENIVAVASELGYLKFEDGTLISVDDIKKYPNNRISIITTGSQGEPMSALSRMASSDHKKVSIV 322
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 323 PGDMVIISATPIPGNEKLVSKVINQLFKQGANVIYEALADVHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAEL 402
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 403 AVKLGMPEKNAIISENGDVIEVTRDTIRKSGSVMSGQVFVDGLGVGDVGNIVLRDRRHLSQDGILTVVVTIGKDTGKVIA 482
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876 483 GPDIISRGFVYVRESEDLMEGARLIVRDALKECEEKHITEWAVIKSKVKEVLRMFLYEKTKRKPMILPIIMEV 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
3-555 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 956.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   3 KEKDKIKIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGAL 82
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  83 PYVLKDLNVPVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTG 162
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 163 DFKIDYTPIDGQVADLARFVELGKKGVIAMLADSTNVERQGYTMSERTVGKTFENIFSKAEGRIIVATFASNIHRIQQII 242
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 243 TASEKIGRKVAVSGRSMENIVAVASELGYLKFEDGTLISVDDIKKYPNNRISIITTGSQGEPMSALSRMASSDHKKVSIV 322
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 323 PGDMVIISATPIPGNEKLVSKVINQLFKQGANVIYEALADVHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAEL 402
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 403 AVKLGMPEKNAIISENGDVIEVTRDTIRKSGSVMSGQVFVDGLGVGDVGNIVLRDRRHLSQDGILTVVVTIGKDTGKVIA 482
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876 483 GPDIISRGFVYVRESEDLMEGARLIVRDALKECEEKHITEWAVIKSKVKEVLRMFLYEKTKRKPMILPIIMEV 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 8-429 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: 525.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876    8 IKIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLK 87
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   88 DLNV-PVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLN-NISIEFIRTSHSIADSAAIAIHTPLGVILHTGDFK 165
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  166 IDYTPIDGQVADLARFVELGKKGVIAMLADSTNVERQGYTMSERTVGKTFENIFSKAEGRIIVATFASNIHRIQQIITAS 245
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  246 EKIGRKVAVSGRSMENIVAVASELGYLKFEDGTLISVDDIKKYPNNRISIITTGSQGEPMSALSRMASSDHKKVSIVPGD 325
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  326 MVIISATPIPGNEKL-VSKVIN-QLFKQGANVIYEAladvHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAELA 403
Cdd:TIGR00649 321 TVVFSAPPIPGNENIaVSITLDiRLNRAGARVIKGI----HVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....*.
gi 489471876  404 VKLGMPEKNAIISENGDVIEVTRDTI 429
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 11-424 5.38e-122

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: 359.03  E-value: 5.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  11 IPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLN 90
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  91 VPVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTGDFKIDYTP 170
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 171 IDGQVADLARFVELGKKGVIAMLADStnverqgytmsertvgktfenifskaegriivatfasnihriqqiitasekigr 250
Cdd:cd07714  161 VDGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 251 kvavsgrsmenivavaselgylkfedgtlisvddikkypnnrisiittgsqgepmsalsrmassdhkkvsivpgdmviis 330
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 331 atpipgneklvskvinqlfkqganviyealadVHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAELAVKLGMPE 410
Cdd:cd07714  187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 489471876 411 KNAIISENGDVIEV 424
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 ...
 454-555 2.08e-47

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: 160.36  E-value: 2.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  454 VLRDRRHLSQDGILTVVVTIGKDTGKVIAGPDIISRGFVYVRESEDLMEGARLIVRDALKECEEKHITEWAVIKSKVKEV 533
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 489471876  534 LRMFLYEKTKRKPMILPIIMEV 555
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-170 2.90e-22

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: 94.16  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876    22 NLTAFEYKNEIVVIDCGLKFPDDEMLGIDvvipdigylLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIG 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489471876   102 IVENRLKESGILSS-----SNLKRVQPRDIIKLNNISIEFIRTSHSIADSaaIAIHTPLGVILHTGDFKIDYTP 170
Cdd:smart00849  72 LLKDLLALLGELGAeaepaPPDRTLKDGDELDLGGGELEVIHTPGHTPGS--IVLYLPEGKILFTGDLLFAGGD 143
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
3-555 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 956.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   3 KEKDKIKIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGAL 82
Cdd:COG0595    1 LKKDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  83 PYVLKDLNVPVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTG 162
Cdd:COG0595   81 PYLLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 163 DFKIDYTPIDGQVADLARFVELGKKGVIAMLADSTNVERQGYTMSERTVGKTFENIFSKAEGRIIVATFASNIHRIQQII 242
Cdd:COG0595  161 DFKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 243 TASEKIGRKVAVSGRSMENIVAVASELGYLKFEDGTLISVDDIKKYPNNRISIITTGSQGEPMSALSRMASSDHKKVSIV 322
Cdd:COG0595  241 DAAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 323 PGDMVIISATPIPGNEKLVSKVINQLFKQGANVIYEALADVHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAEL 402
Cdd:COG0595  321 PGDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKL 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 403 AVKLGMPEKNAIISENGDVIEVTRDTIRKSGSVMSGQVFVDGLGVGDVGNIVLRDRRHLSQDGILTVVVTIGKDTGKVIA 482
Cdd:COG0595  401 AEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVG 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876 483 GPDIISRGFVYVRESEDLMEGARLIVRDALKECEEKHITEWAVIKSKVKEVLRMFLYEKTKRKPMILPIIMEV 555
Cdd:COG0595  481 GPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 8-429 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: 525.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876    8 IKIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLK 87
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   88 DLNV-PVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLN-NISIEFIRTSHSIADSAAIAIHTPLGVILHTGDFK 165
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  166 IDYTPIDGQVADLARFVELGKKGVIAMLADSTNVERQGYTMSERTVGKTFENIFSKAEGRIIVATFASNIHRIQQIITAS 245
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  246 EKIGRKVAVSGRSMENIVAVASELGYLKFEDGTLISVDDIKKYPNNRISIITTGSQGEPMSALSRMASSDHKKVSIVPGD 325
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  326 MVIISATPIPGNEKL-VSKVIN-QLFKQGANVIYEAladvHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAELA 403
Cdd:TIGR00649 321 TVVFSAPPIPGNENIaVSITLDiRLNRAGARVIKGI----HVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....*.
gi 489471876  404 VKLGMPEKNAIISENGDVIEVTRDTI 429
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 11-424 5.38e-122

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: 359.03  E-value: 5.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  11 IPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLN 90
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  91 VPVYGTKLTIGIVENRLKESGILSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTGDFKIDYTP 170
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 171 IDGQVADLARFVELGKKGVIAMLADStnverqgytmsertvgktfenifskaegriivatfasnihriqqiitasekigr 250
Cdd:cd07714  161 VDGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 251 kvavsgrsmenivavaselgylkfedgtlisvddikkypnnrisiittgsqgepmsalsrmassdhkkvsivpgdmviis 330
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 331 atpipgneklvskvinqlfkqganviyealadVHVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAELAVKLGMPE 410
Cdd:cd07714  187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 489471876 411 KNAIISENGDVIEV 424
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 ...
 454-555 2.08e-47

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: 160.36  E-value: 2.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  454 VLRDRRHLSQDGILTVVVTIGKDTGKVIAGPDIISRGFVYVRESEDLMEGARLIVRDALKECEEKHITEWAVIKSKVKEV 533
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 489471876  534 LRMFLYEKTKRKPMILPIIMEV 555
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-170 2.90e-22

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: 94.16  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876    22 NLTAFEYKNEIVVIDCGLKFPDDEMLGIDvvipdigylLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIG 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489471876   102 IVENRLKESGILSS-----SNLKRVQPRDIIKLNNISIEFIRTSHSIADSaaIAIHTPLGVILHTGDFKIDYTP 170
Cdd:smart00849  72 LLKDLLALLGELGAeaepaPPDRTLKDGDELDLGGGELEVIHTPGHTPGS--IVLYLPEGKILFTGDLLFAGGD 143
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-164 4.24e-21

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: 91.52  E-value: 4.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   9 KIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFPDDEMLGIDV-------VIPDI-----------GYLLKNKEKVKGIF 70
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDPESKYFDEVldflelgLLPDIvglyrdplllgGLRSEEDPSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  71 LTHGHEDHIGALPYVLKDlnVPVYGTKLTIGIVENRLKESGILSSS--NLKRVQPRDIIKLNNISIEFIRTSHSIADSAA 148
Cdd:cd07732   81 LSHAHLDHYGLLNYLRPD--IPVYMGEATKRILKALLPFFGEGDPVprNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYA 158

                        170
                 ....*....|....*.
gi 489471876 149 IAIHTPLGVILHTGDF 164
Cdd:cd07732  159 FLIEAPGKRIFYTGDF 174
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 9-171 1.29e-17

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 84.85  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   9 KIIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKFpddemlgidvvipdiGYLLKNKE-------KVKGIFLTHGHEDHIGA 81
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQ---------------GGKERNWPpfpfrpsDVDAVVLTHAHLDHSGA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  82 LPYVLKD-LNVPVYGTKLTIGIVENRLKESGILSSSN---------------LKRVQPRDI---IKLNNISIEFIRTSHs 142
Cdd:COG1236   67 LPLLVKEgFRGPIYATPATADLARILLGDSAKIQEEEaeaeplyteedaeraLELFQTVDYgepFEIGGVRVTFHPAGH- 145

                        170       180
                 ....*....|....*....|....*....
gi 489471876 143 IADSAAIAIHTPLGVILHTGDFKIDYTPI 171
Cdd:COG1236  146 ILGSAQVELEVGGKRIVFSGDYGREDDPL 174
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 29-164 1.26e-16

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: 78.10  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  29 KNEIVVIDCGlkfpDDEMLGIdvvipdIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIGIVENRLK 108
Cdd:cd06262   19 EGEAILIDPG----AGALEKI------LEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876 109 ESGILSSSNLKRVQP------RDIIKLNNISIEFIRT-SHSiADSaaIAIHTPLGVILHTGDF 164
Cdd:cd06262   89 NLAFFGGGPLPPPEPdilledGDTIELGGLELEVIHTpGHT-PGS--VCFYIEEEGVLFTGDT 148
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 10-171 2.01e-15

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 74.80  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  10 IIPLGGLEEVGKNLTAFEYKNEIVVIDCGLKF-------PDDEMLGIDVvipdigyllknkEKVKGIFLTHGHEDHIGAL 82
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQggkeleeLNNEPFPFDP------------KEIDAVILTHAHLDHSGRL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  83 PYVLKD-LNVPVYGTKLTIGIVENRLKESGILSSSN------------------LKRVQP---RDIIKLN-NISIEFIRT 139
Cdd:cd16295   69 PLLVKEgFRGPIYATPATKDLAELLLLDSAKIQEEEaehppaeplyteedvekaLKHFRPveyGEPFEIGpGVKVTFYDA 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489471876 140 SHsIADSAAIAIHTPLGV-ILHTGDFKIDYTPI 171
Cdd:cd16295  149 GH-ILGSASVELEIGGGKrILFSGDLGRKNTPL 180
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 22-183 1.70e-14

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: 72.80  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  22 NLTAFEYKNEIVVIDCGLKFPDDEMLgidvvipdIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIG 101
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 102 IVENRLKESGILSSSNL--KRVQPRDIIKLNNISIEFIRTS-HSIADsaaIAIHTPLGVILHTGD--FKIDYTPIDGQVA 176
Cdd:COG0491   88 ALEAPAAGALFGREPVPpdRTLEDGDTLELGGPGLEVIHTPgHTPGH---VSFYVPDEKVLFTGDalFSGGVGRPDLPDG 164


                 ....*..
gi 489471876 177 DLARFVE 183
Cdd:COG0491  165 DLAQWLA 171
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 9-167 2.85e-13

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: 69.93  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   9 KIIPLG---GLEEvgKNLTAF----EYKNEIVVIDCG---LKFPDDEMLGIDVVIP-DIGYLLKNKekVKGIFLTHGHED 77
Cdd:cd07735    2 ELVVLGcsgGPDE--GNTSSFlldpAGSDGDILLDAGtgvGALSLEEMFNDILFPSqKAAYELYQR--IRHYLITHAHLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  78 HIGALP------YVLKDLNVPVYGTKLTIGIVEN--------------RLKESGILSSSNLKRVQPrdiIKLNNISIEFI 137
Cdd:cd07735   78 HIAGLPllspndGGQRGSPKTIYGLPETIDALKKhifnwviwpdftsiPSGKYPYLRLEPIEPEYP---IALTGLSVTAF 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 489471876 138 RTSHSIADSAAIAIHTPLGVILHTGDFKID 167
Cdd:cd07735  155 PVSHGVPVSTAFLIRDGGDSFLFFGDTGPD 184
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 24-163 7.70e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 65.69  E-value: 7.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  24 TAFEYKNEIVVIDCGlkfpddemlgidvviPDIGYLLK----NKEKVKGIFLTHGHEDHIGALPYV---LKDLNVPVYGT 96
Cdd:COG1235   38 ILVEADGTRLLIDAG---------------PDLREQLLrlglDPSKIDAILLTHEHADHIAGLDDLrprYGPNPIPVYAT 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489471876  97 KLTIGIVENRLkesGILSSSNLKRVQPRDI-----IKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTGD 163
Cdd:COG1235  103 PGTLEALERRF---PYLFAPYPGKLEFHEIepgepFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 56-139 3.26e-11

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: 62.17  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  56 IGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIgivenrlKESGIlSSSNLKRVQPRDIIKLNNISIE 135
Cdd:cd16275   38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEI-------DYYGF-RCPNLIPLEDGDTIKIGDTEIT 109


                 ....
gi 489471876 136 FIRT 139
Cdd:cd16275  110 CLLT 113
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
9-163 4.26e-11

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 64.21  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   9 KIIPLG---GLEEvgKNLTAF----EYKNEIVVIDCGLKFPD---DEMLGidVVIPDIGYLLknkEKVKGIFLTHGHEDH 78
Cdd:COG5212   13 EVRVLGcsgGISD--GNLTTYllrpLGSDDYVLLDAGTVVSGlelAEQKG--AFKGRQGYVL---EHIKGYLISHAHLDH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  79 IGALPY-VLKDLNVPVYGTKLTIGIVEN------------RLKESGILSSSNLKRVQPRDIIKLNN--ISIEFIRTSHSI 143
Cdd:COG5212   86 IAGLPIlSPDDSPKTIYALPETIDALRNhyfnwviwpdftDIGSAPHLPKYRYVPLKPGQTFPLGGtgLRVTAFPLSHSV 165

                        170       180
                 ....*....|....*....|
gi 489471876 144 AdSAAIAIHTPLGVILHTGD 163
Cdd:COG5212  166 P-SSAFLIESGGGAFLYSGD 184
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-163 5.48e-11

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: 62.16  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  30 NEIVVIDCGLkfpdDEmlgiDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIGIVENRLKE 109
Cdd:cd07743   18 KEALLIDSGL----DE----DAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPLLE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489471876 110 SGILS----------------SSNLKRVQPRDIIKLNNISIEFIRTS-HSIADsaaIAIHTPLGViLHTGD 163
Cdd:cd07743   90 PSYLGgayppkelrnkflmakPSKVDDIIEEGELELGGVGLEIIPLPgHSFGQ---IGILTPDGV-LFAGD 156
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 29-163 6.16e-11

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: 62.95  E-value: 6.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  29 KNEIVVIDCGLKFPDDemLGIDVVIPdigYLLKNK-EKVKGIFLTHGHEDHIGALPYVLKDLNV------PVYGTKLTIG 101
Cdd:COG2333   20 DGKTILIDTGPRPSFD--AGERVVLP---YLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVgrvlvsGPPDTSETYE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489471876 102 IVENRLKESGIlsssNLKRVQPRDIIKLNNISIEFIRTSHSI-------ADSAAIAIHTPLGVILHTGD 163
Cdd:COG2333   95 RLLEALKEKGI----PVRPCRAGDTWQLGGVRFEVLWPPEDLlegsdenNNSLVLRLTYGGFSFLLTGD 159
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
20-180 1.00e-10

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 62.13  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  20 GKNLTAF--EYKNEIVVIDCG-------LKFpddemlGIDVvipdigyllknkEKVKGIFLTHGHEDHIGALPYVLKDLN 90
Cdd:COG1234   16 GRATSSYllEAGGERLLIDCGegtqrqlLRA------GLDP------------RDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  91 -------VPVYGTKLTIGIVENRLKESGILSSSNLK--RVQPRDIIKLNNISIEFIRTSHSIaDSAAIAIHTPLGVILHT 161
Cdd:COG1234   78 lagrekpLTIYGPPGTKEFLEALLKASGTDLDFPLEfhEIEPGEVFEIGGFTVTAFPLDHPV-PAYGYRFEEPGRSLVYS 156

                        170
                 ....*....|....*....
gi 489471876 162 GDfkidyTPIDGQVADLAR 180
Cdd:COG1234  157 GD-----TRPCEALVELAK 170
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 22-161 1.61e-10

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: 60.70  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  22 NLTAFEYKNEIVVIDCGLKFPDDEMLGidvVIPDIGYLLKnkeKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIG 101
Cdd:cd07721   12 NAYLIEDDDGLTLIDTGLPGSAKRILK---ALRELGLSPK---DIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAP 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 102 IVENRLKESGILSSSNLKRVQPRdiiklnnISIEFIRTSHSIADSAAIAIHTPLGVIlHT 161
Cdd:cd07721   86 YLEGEKPYPPPVRLGLLGLLSPL-------LPVKPVPVDRTLEDGDTLDLAGGLRVI-HT 137
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 12-169 1.60e-09

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: 57.73  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  12 PLGGLEEVGKNLTAFEYKNEIVVIDCGLkfpDDEMLGIDVVIPDIGYLLKnkeKVKGIFLTHGHEDHIGALPYVLK--DL 89
Cdd:cd07734    2 PLGGGQEVGRSCFLVEFKGRTVLLDCGM---NPGKEDPEACLPQFELLPP---EIDAILISHFHLDHCGALPYLFRgfIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  90 NVPVYGTKLTIGIVENRLKESGILSSSNLK---RVQPRDI-IKLNNISI----EFIRTSHSIADSAAIAIHTPLGVI--L 159
Cdd:cd07734   76 RGPIYATHPTVALGRLLLEDYVKSAERIGQdqsLYTPEDIeEALKHIVPlgygQSIDLFPALSLTAYNAGHVLGAAMweI 155

                        170
                 ....*....|
gi 489471876 160 HTGDFKIDYT 169
Cdd:cd07734  156 QIYGEKLVYT 165
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 27-137 3.89e-09

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: 55.99  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  27 EYKNEIVVIDCGLKFPDDEmlgiDVVIPdigYLL-KNKEKVKGIFLTHGHEDHIGALPYVLKDLNV------PVYGTKLT 99
Cdd:cd07731   16 QTPGKTILIDTGPRDSFGE----DVVVP---YLKaRGIKKLDYLILTHPDADHIGGLDAVLKNFPVkevympGVTHTTKT 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489471876 100 IGIVENRLKESGIlsssNLKRVQPRDIIKLNNISIEFI 137
Cdd:cd07731   89 YEDLLDAIKEKGI----PVTPCKAGDRWQLGGVSFEVL 122
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
22-164 8.64e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.45  E-value: 8.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   22 NLTAFEYKNEIVVIDCGLkfpdDEMLGIDVVIPDIGYLLKnkeKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIG 101
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG----SAEAALLLLLAALGLGPK---DIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876  102 IVENRLKESGILSSSNLKR----------VQPRDIIKLNNISIEFIRTSHSiaDSAAIAIHTPLGVILHTGDF 164
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGPpvvplppdvvLEEGDGILGGGLGLLVTHGPGH--GPGHVVVYYGGGKVLFTGDL 150
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 27-163 6.05e-08

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: 52.46  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  27 EYKNEIVVIDCGlkfpDDEMLgidvvipdIGYLLKNKEKVKGIFLTHGHEDHIGALPYvLKDL--NVPVYGTKL-TIGIV 103
Cdd:cd07723   17 EATGEAAVVDPG----EAEPV--------LAALEKNGLTLTAILTTHHHWDHTGGNAE-LKALfpDAPVYGPAEdRIPGL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489471876 104 ENRLKESgilsssnlkrvqprDIIKLNNISIEFIRTS-HSiADSaaIAIHTPLGVILHTGD 163
Cdd:cd07723   84 DHPVKDG--------------DEIKLGGLEVKVLHTPgHT-LGH--ICYYVPDEPALFTGD 127
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 364-405 6.84e-08

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: 49.54  E-value: 6.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 489471876  364 HVSGHACQEELKLIHTLVKPKFFIPVHGEYRMLKQHAELAVK 405
Cdd:pfam07521  13 GFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKE 54
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 33-168 1.38e-07

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: 51.11  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  33 VVIDCGLKFPDdemlgIDVVIPDIGyllKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIGIVENRLKESgi 112
Cdd:cd07733   21 LLIDAGLSGRK-----ITGRLAEIG---RDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRAMERKVGLI-- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489471876 113 lSSSNLKRVQPRDIIKLNNISIEFIRTSHSIADsaaiaihtPLGVILHTGDFKIDY 168
Cdd:cd07733   91 -DVDQKQIFEPGETFSIGDFDVESFGVSHDAAD--------PVGYRFEEGGRRFGM 137
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 8-86 2.49e-07

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: 51.05  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   8 IKIIPLGGLEEVGKNLTAFEYKNEIVVIDCG----------LKFPDDemlgIDVvipdigyllknkEKVKGIFLTHGHED 77
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGihpgysglasLPFFDE----IDL------------SEIDLLLITHFHLD 64


                 ....*....
gi 489471876  78 HIGALPYVL 86
Cdd:cd16292   65 HCGALPYFL 73
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 64-180 3.39e-07

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 50.52  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  64 EKVKGIFLTHGHEDHI---GALPYVLKDLN-------VPVYGTKLTigivENRLKE-SGILSSSNLKRVQPRDIIKLNNI 132
Cdd:cd07716   49 EDLDAVVLSHLHPDHCadlGVLQYARRYHPrgarkppLPLYGPAGP----AERLAAlYGLEDVFDFHPIEPGEPLEIGPF 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489471876 133 SIEFIRTSHSIaDSAAIAIHTPLGVILHTGDfkIDYTPidgQVADLAR 180
Cdd:cd07716  125 TITFFRTVHPV-PCYAMRIEDGGKVLVYTGD--TGYCD---ELVEFAR 166
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 64-174 8.67e-07

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: 49.05  E-value: 8.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  64 EKVKGIFLTHGHEDHIGALPyvlKDLNVPVYGTKLTIGIVENRLKesgiLSSSNLKRVQPRDIIKLNNISIEFIRTSHSi 143
Cdd:cd16298   35 EGCTAYFLTHFHSDHYCGLT---KKFKFPIYCSKITGNLVKSKLK----VEEQYINVLPMNTECIVNGVKVVLLDANHC- 106

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489471876 144 ADSAAIAIHTPLG-VILHTGDFKID-----YTPIDGQ 174
Cdd:cd16298  107 PGAVMILFRLPSGtLVLHTGDFRADpsmerYPELIGQ 143
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 64-192 3.93e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.99  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  64 EKVKGIFLTHGHEDHIG--ALPYVLKDlNVPVYGTKLtigiVENRLKESGIlssSNLKRVQPRDIIKLNNISIEFIRTSH 141
Cdd:COG2220   47 PKIDAVLVTHDHYDHLDdaTLRALKRT-GATVVAPLG----VAAWLRAWGF---PRVTELDWGESVELGGLTVTAVPARH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876 142 SIA-------DSAAIAIHTPLGVILHTGD-------------FKIDYT--PIDG--------QVADLARFVELGKkgVIA 191
Cdd:COG2220  119 SSGrpdrnggLWVGFVIETDGKTIYHAGDtgyfpemkeigerFPIDVAllPIGAypftmgpeEAAEAARDLKPKV--VIP 196


                 .
gi 489471876 192 M 192
Cdd:COG2220  197 I 197
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 10-96 1.03e-05

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293849  Cd Length: 199  Bit Score: 46.49  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  10 IIPLGGLEEVGKNLTAFEYKNEIVVIDCG--LKFPDDEMLgidvviPDIGYLLKNK---EKVKGIFLTHGHEDHIGALPY 84
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGmhMGYNDERRF------PDFSYISQNGpftEHIDCVIISHFHLDHCGALPY 74

                         90
                 ....*....|....
gi 489471876  85 VLKDLNV--PVYGT 96
Cdd:cd16291   75 FTEVVGYdgPIYMT 88
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 27-141 1.86e-05

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: 45.54  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  27 EYKNEIVVIDCGlkfpddemlgidvviPDIGY-LLKNK-EKVKGIFLTHGHEDHIG------ALPYVLKDlNVPVYGTKL 98
Cdd:cd16279   41 ETGGKNILIDTG---------------PDFRQqALRAGiRKLDAVLLTHAHADHIHglddlrPFNRLQQR-PIPVYASEE 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489471876  99 TIGIVENRL------KESGILSSSNLKRVQPRDIIKLNNISIEFIRTSH 141
Cdd:cd16279  105 TLDDLKRRFpyffaaTGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLH 153
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 8-142 2.01e-05

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: 45.80  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   8 IKIIPLGGLEEvgkN--LTAFEYKNEIVVIDcglkfPDDEMLGIDVVIPDIGYllknkeKVKGIFLTHGHEDHIGALPYV 85
Cdd:cd16322    1 VRPFTLGPLQE---NtyLVADEGGGEAVLVD-----PGDESEKLLARFGTTGL------TLLYILLTHAHFDHVGGVADL 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489471876  86 LKDLNVPVYGTKLTIGIVENrLKESGILSSSNLKRVQPRDI-------IKLNNISIEFIRT-SHS 142
Cdd:cd16322   67 RRHPGAPVYLHPDDLPLYEA-ADLGAKAFGLGIEPLPPPDRlledgqtLTLGGLEFKVLHTpGHS 130
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 33-163 2.48e-05

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: 45.22  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  33 VVIDCGlkfpddEmlGIDVVIPDIGYLLKNKEK--VKGIFLTHGHEDHIGALPYVLKDL---NVPVYgtKLtigiVENRL 107
Cdd:cd07722   30 ILIDTG------E--GRPSYIPLLKSVLDSEGNatISDILLTHWHHDHVGGLPDVLDLLrgpSPRVY--KF----PRPEE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489471876 108 KESGILSSSNLKRVQPRDIIKLNNISIEfirtshsiadsaaiAIHTPlGvilHTGD 163
Cdd:cd07722   96 DEDPDEDGGDIHDLQDGQVFKVEGATLR--------------VIHTP-G---HTTD 133
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 63-170 6.08e-05

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 44.22  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876   63 KEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTIGIvenrLKESGILSSSNLKRVQPRDIIKLN--------NISI 134
Cdd:pfam12706  26 DDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAH----LRRNFPYLFLLEHYGVRVHEIDWGesftvgdgGLTV 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489471876  135 EFIRTSHSIADSAAIAIHTPLGVILHTGDFKIDYTP 170
Cdd:pfam12706 102 TATPARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAG 137
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
45-145 1.17e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 44.10  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  45 EMLGIDVvipdigyllknkEKVKGIFLTHGHEDHIGALPYVLK-DLNVPVYGTKltiGIVENRLKESGILSSSNLKrvQP 123
Cdd:COG1237   49 EKLGIDL------------SDIDAVVLSHGHYDHTGGLPALLElNPKAPVYAHP---DAFEKRYSKRPGGKYIGIP--FS 111

                         90       100
                 ....*....|....*....|..
gi 489471876 124 RDIIKLNNISIEFIRTSHSIAD 145
Cdd:COG1237  112 REELEKLGARLILVKEPTEIAP 133
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 31-164 1.34e-04

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: 42.77  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  31 EIVVIDcglkfPddemlGIDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYgtkltIGivenrlkeS 110
Cdd:cd07724   24 EAAVID-----P-----VRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIV-----IG--------E 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489471876 111 GILSSSNLKRVQPRDIIKLNNISIEFIRT-SHSiADSAAIAIHTPLGVIlhTGDF 164
Cdd:cd07724   81 GAPASFFDRLLKDGDVLELGNLTLEVLHTpGHT-PESVSYLVGDPDAVF--TGDT 132
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 22-192 1.35e-04

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 43.59  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  22 NLTA--FEYKNEIVVIDCG-----------LKFPddemlgidvvipdigyllknkeKVKGIFLTHGHEDHIGALPyvlkd 88
Cdd:cd07717   16 NLSSiaLRLEGELWLFDCGegtqrqllragLSPS----------------------KIDRIFITHLHGDHILGLP----- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  89 lnvpvygtkltigivenrlkesGILSS-SNLKRVQPRDII---KLnnisIEFIRTSHSIADSAA------IAIHTPLGVI 158
Cdd:cd07717   69 ----------------------GLLSTmSLLGRTEPLTIYgpkGL----KEFLETLLRLSASRLpypievHELEPDPGLV 122

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489471876 159 LHTGDFKIDYTPIDGQVADLARFVELGKKGVIAM 192
Cdd:cd07717  123 FEDDGFTVTAFPLDHRVPCFGYRFEEGRKIAYLG 156
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 45-145 1.41e-04

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 43.76  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  45 EMLGIDVvipdigyllknkEKVKGIFLTHGHEDHIGALPYVLKDL-NVPVYGTKltiGIVENRLKESGILSSSNLkrvQP 123
Cdd:cd07713   47 KKLGIDL------------SDIDAVVLSHGHYDHTGGLKALLELNpKAPVYAHP---DAFEPRYSKRGGGKKGIG---IG 108

                         90       100
                 ....*....|....*....|..
gi 489471876 124 RDIIKLNNISIEFIRTSHSIAD 145
Cdd:cd07713  109 REELEKAGARLVLVEEPTEIAP 130
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 59-95 1.46e-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: 42.93  E-value: 1.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489471876  59 LLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYG 95
Cdd:cd07737   40 IEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIG 76
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 35-96 3.19e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component 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. This subgroup includes Ydh1p, the yeast homolog of CPSF2. 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. 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: 293851  Cd Length: 199  Bit Score: 42.12  E-value: 3.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489471876  35 IDCGL--KFPDDEMLGIDVVIPDIGyllknkekvkGIFLTHGHEDHIGALPYVLK--DLNVPVYGT 96
Cdd:cd16293   26 LDCGWdeSFDMEYLESLKRIAPTID----------AVLLSHPDLEHLGALPYLVGklGLTCPVYAT 81
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-163 6.19e-04

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: 41.09  E-value: 6.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  24 TAFEYKNEIVVIDCGlkfpddemlgiDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYGTKLTI--- 100
Cdd:cd16272   20 YLLETGGTRILLDCG-----------EGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKPLTIygp 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489471876 101 -GIVE--NRLKESGILSSSNLKRVQPRDI------IKLNNISIEFIRTSHSIAdSAAIAIHTPLGVILHTGD 163
Cdd:cd16272   89 kGIKEflEKLLNFPVEILPLGFPLEIEELeeggevLELGDLKVEAFPVKHSVE-SLGYRIEAEGKSIVYSGD 159
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-139 9.13e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 41.03  E-value: 9.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  32 IVVIDcGLKFPDDEmlgiDVVIPDIGYLLKNKEKVKGIFLTHGHEDHIGALPYvLKDLnvpvYGTKLTIGIVENRLKESG 111
Cdd:cd16280   33 LILID-ALNNNEAA----DLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY-LKDL----YGAKVVMSEADWDMMEEP 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489471876 112 ILSSSNLKRVQP--RDI-------IKLNNISIEFIRT 139
Cdd:cd16280  103 PEEGDNPRWGPPpeRDIvikdgdtLTLGDTTITVYLT 139
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 64-139 9.47e-04

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: 40.93  E-value: 9.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489471876  64 EKVKGIFLTHGHEDHIGALPYVLKDL-NVPVYGTKLTIGIvenrLKESGILSSSNLKRVQPRDIIKLNNISIEFIRT 139
Cdd:cd07709   67 RKIDYIVVNHQEPDHSGSLPELLELApNAKIVCSKKAARF----LKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPA 139
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 24-180 1.01e-03

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: 40.58  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  24 TAFEYKNEIVVIDCG----LKFpddEMLGIDVvipdigyllknkEKVKGIFLTHGHEDHIGALPYVLK-------DLNVP 92
Cdd:cd07719   21 TLVVVGGRVYLVDAGsgvvRRL---AQAGLPL------------GDLDAVFLTHLHSDHVADLPALLLtawlagrKTPLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  93 VYG----TKLTIGIVE-------NRLKESGILSSSNLKRVQPRDI------IKLNNISIEFIRTSHSIADSA-AIAIHTP 154
Cdd:cd07719   86 VYGppgtRALVDGLLAayaldidYRARIGDEGRPDPGALVEVHEIaaggvvYEDDGVKVTAFLVDHGPVPPAlAYRFDTP 165

                        170       180
                 ....*....|....*....|....*.
gi 489471876 155 LGVILHTGDfkidyTPIDGQVADLAR 180
Cdd:cd07719  166 GRSVVFSGD-----TGPSENLIELAK 186
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 63-135 1.32e-03

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: 40.35  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489471876  63 KEKVKGIFLTHGHEDHIGALPyVLKDLNVPVYGTKLTIgiveNRLKESGIlsSSNLKRVQPRDIIKLNNISIE 135
Cdd:cd16304   61 KKPVTLAIVTHAHDDRIGGIK-ALQKRGIPVYSTKLTA----QLAKKQGY--PSPDGILKDDTTLKFGNTKIE 126
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 63-112 2.78e-03

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: 39.54  E-value: 2.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489471876  63 KEKVKGIFLTHGHEDHIGALPYvLKDLNVPVYGTKLTIGIvenrLKESGI 112
Cdd:cd16302   62 KAKVKAVVPTHFHDDCLGGLKA-FHRRGIPSYANQKTIAL----AKEKGL 106
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-163 4.54e-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) 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: 38.39  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  69 IFLTHGHEDHIGALPYVLKDLNVpVYG--TKLTI----GIVE--NRLKESGILSSSNLKR--------VQPRDIIKLNNI 132
Cdd:cd07740   53 IFITHLHGDHFGGLPFFLLDAQF-VAKrtRPLTIagppGLRErlRRAMEALFPGSSKVPRrfdlevieLEPGEPTTLGGV 131

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489471876 133 SIEFIRTSHSIADSAAIAIHTPLG-VILHTGD 163
Cdd:cd07740  132 TVTAFPVVHPSGALPLALRLEAAGrVLAYSGD 163
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 30-143 5.67e-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: 38.05  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  30 NEIVVIDCGLKFPDD--------EMLGIDVVipDIGYllknkekvkgIFLTHGHEDHIGALPYVLKDLNVPVYgtkltig 101
Cdd:cd07725   24 DETTLIDTGLATEEDaealweglKELGLKPS--DIDR----------VLLTHHHPDHIGLAGKLQEKSGATVY------- 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489471876 102 ivenrlkesgilsSSNLKRVQPRDIIKLNNISIEFIRTS-HSI 143
Cdd:cd07725   85 -------------ILDVTPVKDGDKIDLGGLRLKVIETPgHTP 114
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-95 5.69e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 38.24  E-value: 5.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489471876  30 NEIVVIDCGlkfPDDE--MLGIDVVIPDigyllknkEKVKGIFLTHGHEDHIGALPYVLKDLNVPVYG 95
Cdd:cd16278   27 DGVVVIDPG---PDDPahLDALLAALGG--------GRVSAILVTHTHRDHSPGAARLAERTGAPVRA 83
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 18-87 6.19e-03

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 39.50  E-value: 6.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489471876   18 EVGKNLTAFEYKN-EIVVIDCGLKFPDDEMlGIDVVIPdigYLLKNKEKVKGIFLTHGHEDHIGALPYVLK 87
Cdd:TIGR00361 446 DVGQGLAMFIGANgKGILYDTGEPWREGSL-GEKVIIP---FLTAKGIKLEALILSHADQDHIGGAEIILK 512
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-163 9.03e-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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 37.94  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489471876  62 NKEKVKGIFLTHGHEDHIGalpyvlkDLNVPVYGtkLTIGIVENR---------LKESGILSSSNLKR-------VQPRD 125
Cdd:cd07741   50 DPTKLDAIILSHRHLDHSN-------DANVLIEA--MTEGGFKKRgtllapedaLNGEPVVLLYYHRRkleeieiLEEGD 120

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489471876 126 IIKLNNISIEFIRTSHSIADSAAIAIHTPLGVILHTGD 163
Cdd:cd07741  121 EYELGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISD 158
 
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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