NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515407687|ref|WP_016896743|]
View 

MULTISPECIES: ribonuclease J [Aerococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-551 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 714.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   1 MSDINIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPY 80
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  81 LLKDIQVPVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDF 160
Cdd:COG0595   83 LLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 161 KFDMTVSDAYKTDFSRIVEIGRDGVFALLSDSNAAENMKPNATEIEIEQGLLKEVRNAKGRVIVAAVASNLMRIQQVLDV 240
Cdd:COG0595  163 KFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 241 ASKLGRRVFLDDTELEEIIDVAIRLGKLSIPSKDLItNLKDLGRFEDNEIIFLETGKSGEPLTTLQKMASSRHTTVSIKD 320
Cdd:COG0595  243 AKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLI-DLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 321 GDKVIIVTTPSYDMEKVVAETKNDVYRAGGEVVELAQA-YASSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLA 399
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAkVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 400 TEVGIPEENVFLLDKGDILTYKDGNIHIGGAVPASNVLIDGSGVGDIGNIVLRDRRILSEDGIFLVVLTISRRLGKILSG 479
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515407687 480 PEIISRGFIYMKASETLLDESKDVVVEVTEENLKDKNFEWSKLKGDIRDALSKKLYSETQRRPMILPVIMEA 551
Cdd:COG0595  482 PDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-551 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 714.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   1 MSDINIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPY 80
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  81 LLKDIQVPVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDF 160
Cdd:COG0595   83 LLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 161 KFDMTVSDAYKTDFSRIVEIGRDGVFALLSDSNAAENMKPNATEIEIEQGLLKEVRNAKGRVIVAAVASNLMRIQQVLDV 240
Cdd:COG0595  163 KFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 241 ASKLGRRVFLDDTELEEIIDVAIRLGKLSIPSKDLItNLKDLGRFEDNEIIFLETGKSGEPLTTLQKMASSRHTTVSIKD 320
Cdd:COG0595  243 AKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLI-DLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 321 GDKVIIVTTPSYDMEKVVAETKNDVYRAGGEVVELAQA-YASSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLA 399
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAkVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 400 TEVGIPEENVFLLDKGDILTYKDGNIHIGGAVPASNVLIDGSGVGDIGNIVLRDRRILSEDGIFLVVLTISRRLGKILSG 479
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515407687 480 PEIISRGFIYMKASETLLDESKDVVVEVTEENLKDKNFEWSKLKGDIRDALSKKLYSETQRRPMILPVIMEA 551
Cdd:COG0595  482 PDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 4-425 1.19e-125

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: 375.15  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687    4 INIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPYLLK 83
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   84 DIQV-PVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFG-NVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDFK 161
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  162 FDMTVSDAYKTDFSRIVEIGRDGVFALLSDSNAAENMKPNATEIEIEQGLLKEVRNAKGRVIVAAVASNLMRIQQVLDVA 241
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  242 SKLGRRVFLDDTELEEIIDVAIRLGKLSIPSKDLITnLKDLGRFEDNEIIFLETGKSGEPLTTLQKMASSRHTTVSIKDG 321
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFIS-LKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  322 DKVIIVTTPSYDMEKVVAETKNDVYRAGGEVVELAQAYAsSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLATE 401
Cdd:TIGR00649 320 DTVVFSAPPIPGNENIAVSITLDIRLNRAGARVIKGIHV-SGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAEE 398

                         410       420
                  ....*....|....*....|....
gi 515407687  402 VGIPEENVFLLDKGDILTYKDGNI 425
Cdd:TIGR00649 399 EGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-420 1.70e-92

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: 283.53  E-value: 1.70e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   7 IALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQ 86
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  87 VPVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDFKFDMTV 166
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 167 SDAYKTDFSRIVEIGRDGVFALLSDSNaaenmkpnateieieqgllkevrnakgrvivaavasnlmriqqvldvasklgr 246
Cdd:cd07714  161 VDGKPTDLEKLAELGKEGVLLLLSDSV----------------------------------------------------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 247 rvflddteleeiidvairlgklsipskdlitnlkdlgrfedneiifletgksgeplttlqkmassrHTtvsikdgdkvii 326
Cdd:cd07714  188 ------------------------------------------------------------------HV------------ 189

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 327 vttpsydmekvvaetkndvyraggevvelaqayasSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLATEVGIPE 406
Cdd:cd07714  190 -----------------------------------SGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 515407687 407 ENVFLLDKGDILTY 420
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 ...
 450-550 2.49e-40

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: 141.48  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  450 VLRDRRILSEDGIFLVVLTISRRLGKILSGPEIISRGFIYMKASETLLDESKDVVVEVTEENLKDKNFEWSKLKGDIRDA 529
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|.
gi 515407687  530 LSKKLYSETQRRPMILPVIME 550
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIME 101
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-163 4.54e-21

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: 90.69  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687    18 NMYLVEVDEAIYVLDCGLVYPPDELLGIDmmipdftylKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515407687    98 LAKIQTKKIG-----LKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVstPEGSIVYTGDFKFD 163
Cdd:smart00849  72 LLKDLLALLGelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFA 140
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-551 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 714.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   1 MSDINIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPY 80
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  81 LLKDIQVPVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDF 160
Cdd:COG0595   83 LLKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 161 KFDMTVSDAYKTDFSRIVEIGRDGVFALLSDSNAAENMKPNATEIEIEQGLLKEVRNAKGRVIVAAVASNLMRIQQVLDV 240
Cdd:COG0595  163 KFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 241 ASKLGRRVFLDDTELEEIIDVAIRLGKLSIPSKDLItNLKDLGRFEDNEIIFLETGKSGEPLTTLQKMASSRHTTVSIKD 320
Cdd:COG0595  243 AKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLI-DLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 321 GDKVIIVTTPSYDMEKVVAETKNDVYRAGGEVVELAQA-YASSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLA 399
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAkVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 400 TEVGIPEENVFLLDKGDILTYKDGNIHIGGAVPASNVLIDGSGVGDIGNIVLRDRRILSEDGIFLVVLTISRRLGKILSG 479
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515407687 480 PEIISRGFIYMKASETLLDESKDVVVEVTEENLKDKNFEWSKLKGDIRDALSKKLYSETQRRPMILPVIMEA 551
Cdd:COG0595  482 PDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 4-425 1.19e-125

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: 375.15  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687    4 INIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPYLLK 83
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   84 DIQV-PVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFG-NVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDFK 161
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  162 FDMTVSDAYKTDFSRIVEIGRDGVFALLSDSNAAENMKPNATEIEIEQGLLKEVRNAKGRVIVAAVASNLMRIQQVLDVA 241
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  242 SKLGRRVFLDDTELEEIIDVAIRLGKLSIPSKDLITnLKDLGRFEDNEIIFLETGKSGEPLTTLQKMASSRHTTVSIKDG 321
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFIS-LKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  322 DKVIIVTTPSYDMEKVVAETKNDVYRAGGEVVELAQAYAsSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLATE 401
Cdd:TIGR00649 320 DTVVFSAPPIPGNENIAVSITLDIRLNRAGARVIKGIHV-SGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAEE 398

                         410       420
                  ....*....|....*....|....
gi 515407687  402 VGIPEENVFLLDKGDILTYKDGNI 425
Cdd:TIGR00649 399 EGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-420 1.70e-92

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: 283.53  E-value: 1.70e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   7 IALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQ 86
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  87 VPVFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDFKFDMTV 166
Cdd:cd07714   81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 167 SDAYKTDFSRIVEIGRDGVFALLSDSNaaenmkpnateieieqgllkevrnakgrvivaavasnlmriqqvldvasklgr 246
Cdd:cd07714  161 VDGKPTDLEKLAELGKEGVLLLLSDSV----------------------------------------------------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 247 rvflddteleeiidvairlgklsipskdlitnlkdlgrfedneiifletgksgeplttlqkmassrHTtvsikdgdkvii 326
Cdd:cd07714  188 ------------------------------------------------------------------HV------------ 189

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687 327 vttpsydmekvvaetkndvyraggevvelaqayasSGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHKHLATEVGIPE 406
Cdd:cd07714  190 -----------------------------------SGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                        410
                 ....*....|....
gi 515407687 407 ENVFLLDKGDILTY 420
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 ...
 450-550 2.49e-40

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: 141.48  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  450 VLRDRRILSEDGIFLVVLTISRRLGKILSGPEIISRGFIYMKASETLLDESKDVVVEVTEENLKDKNFEWSKLKGDIRDA 529
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|.
gi 515407687  530 LSKKLYSETQRRPMILPVIME 550
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIME 101
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-162 2.42e-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: 92.29  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   5 NIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYP------------------PDELLGIDMMIPDFTYLKENQDRVAGVF 66
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDpeskyfdevldflelgllPDIVGLYRDPLLLGGLRSEEDPSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  67 LTHGHADAIGALPYLLKDIqvPVFGTELTIELAKIQTK--KIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVG 144
Cdd:cd07732   81 LSHAHLDHYGLLNYLRPDI--PVYMGEATKRILKALLPffGEGDPVPRNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYA 158

                        170
                 ....*....|....*...
gi 515407687 145 IEVSTPEGSIVYTGDFKF 162
Cdd:cd07732  159 FLIEAPGKRIFYTGDFRF 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-163 4.54e-21

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: 90.69  E-value: 4.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687    18 NMYLVEVDEAIYVLDCGLVYPPDELLGIDmmipdftylKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515407687    98 LAKIQTKKIG-----LKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVstPEGSIVYTGDFKFD 163
Cdd:smart00849  72 LLKDLLALLGelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFA 140
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-163 9.28e-17

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 82.54  E-value: 9.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   5 NIIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGidmmiPDFTYlkeNQDRVAGVFLTHGHADAIGALPYLLKD 84
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNW-----PPFPF---RPSDVDAVVLTHAHLDHSGALPLLVKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  85 -IQVPVFGTELTIELAKI-----------QTKKIGLKNYQD-------FHIISEDNEIDFGNVVIKFFKTTHsVPESVGI 145
Cdd:COG1236   74 gFRGPIYATPATADLARIllgdsakiqeeEAEAEPLYTEEDaeralelFQTVDYGEPFEIGGVRVTFHPAGH-ILGSAQV 152

                        170
                 ....*....|....*...
gi 515407687 146 EVSTPEGSIVYTGDFKFD 163
Cdd:COG1236  153 ELEVGGKRIVFSGDYGRE 170
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 6-163 9.98e-17

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: 78.65  E-value: 9.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   6 IIALGGVRENGKNMYLVEVDEAIYVLDCGLVYPPDELLGIDMMIPDFtylkeNQDRVAGVFLTHGHADAIGALPYLLKD- 84
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPF-----DPKEIDAVILTHAHLDHSGRLPLLVKEg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  85 IQVPVFGTELTIEL--------AKIQTKKIGLKN------YQD-------FHIISEDNEIDFG-NVVIKFFKTTHsVPES 142
Cdd:cd16295   76 FRGPIYATPATKDLaelllldsAKIQEEEAEHPPaeplytEEDvekalkhFRPVEYGEPFEIGpGVKVTFYDAGH-ILGS 154

                        170       180
                 ....*....|....*....|..
gi 515407687 143 VGIEVSTPEG-SIVYTGDFKFD 163
Cdd:cd16295  155 ASVELEIGGGkRILFSGDLGRK 176
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
20-159 3.56e-16

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 78.31  E-value: 3.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAIYVLDCG------LVYppdelLGIDMMipdftylkenqdRVAGVFLTHGHADAIGALPYLLKDIQ------- 86
Cdd:COG1234   22 YLLEAGGERLLIDCGegtqrqLLR-----AGLDPR------------DIDAIFITHLHGDHIAGLPGLLSTRSlagrekp 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515407687  87 VPVFGTELTIELAKIQTKKIGLK-NYQ-DFHIISEDNEIDFGNVVIKFFKTTHSVPeSVGIEVSTPEGSIVYTGD 159
Cdd:COG1234   85 LTIYGPPGTKEFLEALLKASGTDlDFPlEFHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGD 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 20-159 1.89e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 76.47  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAIYVLDCGlvyppdellgidmmiPDFTY----LKENQDRVAGVFLTHGHADAIGALPYL---LKDIQVPVFGT 92
Cdd:COG1235   38 ILVEADGTRLLIDAG---------------PDLREqllrLGLDPSKIDAILLTHEHADHIAGLDDLrprYGPNPIPVYAT 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515407687  93 ELTIE--LAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGD 159
Cdd:COG1235  103 PGTLEalERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 18-179 7.91e-15

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: 73.09  E-value: 7.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  18 NMYLV--EVDEAIyVLDCGLvYPPDELLgidmmipdfTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELT 95
Cdd:cd06262   11 NCYLVsdEEGEAI-LIDPGA-GALEKIL---------EAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  96 IELAK------IQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTT-HSvPESVGIEVstPEGSIVYTGDFKFDMTV-- 166
Cdd:cd06262   80 AELLEdpelnlAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPgHT-PGSVCFYI--EEEGVLFTGDTLFAGSIgr 156

                        170
                 ....*....|...
gi 515407687 167 SDAYKTDFSRIVE 179
Cdd:cd06262  157 TDLPGGDPEQLIE 169
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 20-159 9.70e-15

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: 72.47  E-value: 9.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAIYVLDCG------L--VYPPDELlgidmmipdftylkenqdrvAGVFLTHGHAD--A-IGALPYLLKDIQ-- 86
Cdd:cd07716   21 YLLEADGFRILLDCGsgvlsrLqrYIDPEDL--------------------DAVVLSHLHPDhcAdLGVLQYARRYHPrg 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515407687  87 -----VPVFGTELTIE-LAKIQtkkiGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPeSVGIEVSTPEGSIVYTGD 159
Cdd:cd07716   81 arkppLPLYGPAGPAErLAALY----GLEDVFDFHPIEPGEPLEIGPFTITFFRTVHPVP-CYAMRIEDGGKVLVYTGD 154
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 18-159 4.73e-13

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: 68.56  E-value: 4.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  18 NMYLVEVDEAIYVLDCGLVYPPDELLgidmmipdFTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE 97
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515407687  98 LAK--IQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTT-HSvPESVGIEVstPEGSIVYTGD 159
Cdd:COG0491   88 ALEapAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPgHT-PGHVSFYV--PDEKVLFTGD 149
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 20-159 2.38e-12

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: 65.75  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAIYVLDCGlVYPPDELLGIDMMIPDFTYlkenqdrvagVFLTHGHADAIGALPYLLKDIQVPVFGTELTI--- 96
Cdd:cd16272   20 YLLETGGTRILLDCG-EGTVYRLLKAGVDPDKLDA----------IFLSHFHLDHIGGLPTLLFARRYGGRKKPLTIygp 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515407687  97 -------ELAKIQTKKIGLKNYQ-DFHIISEDNEI-DFGNVVIKFFKTTHSvPESVGIEVSTPEGSIVYTGD 159
Cdd:cd16272   89 kgikeflEKLLNFPVEILPLGFPlEIEELEEGGEVlELGDLKVEAFPVKHS-VESLGYRIEAEGKSIVYSGD 159
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 60-159 7.47e-11

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: 62.61  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  60 DRVAGVFLTHGHADAIGALP------YLLKDIQVPVFGTELTIE--------------LAKIQTKKIglkNYQDFHIISE 119
Cdd:cd07735   64 QRIRHYLITHAHLDHIAGLPllspndGGQRGSPKTIYGLPETIDalkkhifnwviwpdFTSIPSGKY---PYLRLEPIEP 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515407687 120 DNEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGD 159
Cdd:cd07735  141 EYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGD 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-162 1.29e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   18 NMYLVEVDEAIYVLDCGLVYPPDELLGIdmmipdfTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLL-------AALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515407687   98 LAK-------IQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTH-SVPESVGIEVSTPEGSIVYTGDFKF 162
Cdd:pfam00753  80 ELLdeelglaASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHgPGHGPGHVVVYYGGGKVLFTGDLLF 152
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 21-162 1.45e-10

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 60.57  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  21 LVEVDEAIYVLDCGlvyppdellgidmmiPDFTY--LKENQDRVAGVFLTHGHADAIGALP-----YLLKDIQVPVFGTE 93
Cdd:cd16279   39 LIETGGKNILIDTG---------------PDFRQqaLRAGIRKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASE 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515407687  94 LTIE------LAKIQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPESVGIEVstpeGSIVYTGDFKF 162
Cdd:cd16279  104 ETLDdlkrrfPYFFAATGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLHGKLPSLGFRF----GDFAYLTDVSE 174
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 20-159 7.90e-09

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: 55.60  E-value: 7.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAIYVLDCG------LVyppdeLLGIDMmipdftylkenqDRVAGVFLTHGHADAIGALPYLLK-------DIQ 86
Cdd:cd07719   21 TLVVVGGRVYLVDAGsgvvrrLA-----QAGLPL------------GDLDAVFLTHLHSDHVADLPALLLtawlagrKTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  87 VPVFG----TELTIELAKIQTKKIGLKNYQDFHIISEDN------EIDFGNVVIKF-------FKTTHS-VPESVGIEVS 148
Cdd:cd07719   84 LPVYGppgtRALVDGLLAAYALDIDYRARIGDEGRPDPGalvevhEIAAGGVVYEDdgvkvtaFLVDHGpVPPALAYRFD 163

                        170
                 ....*....|.
gi 515407687 149 TPEGSIVYTGD 159
Cdd:cd07719  164 TPGRSVVFSGD 174
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 9-162 2.89e-08

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: 53.87  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   9 LGGVRENGKNMYLVEVDEAIYVLDCGLvYPPDELLGIDmmIPDFTYLkenQDRVAGVFLTHGHADAIGALPYLLKDI--Q 86
Cdd:cd07734    3 LGGGQEVGRSCFLVEFKGRTVLLDCGM-NPGKEDPEAC--LPQFELL---PPEIDAILISHFHLDHCGALPYLFRGFifR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  87 VPVFGTE--------LTIELAKIQTKKIGLKNY---QDF-----HII----SEDNEIdFGNVVIKFFKTTHsVPESVGIE 146
Cdd:cd07734   77 GPIYATHptvalgrlLLEDYVKSAERIGQDQSLytpEDIeealkHIVplgyGQSIDL-FPALSLTAYNAGH-VLGAAMWE 154

                        170
                 ....*....|....*.
gi 515407687 147 VSTPEGSIVYTGDFKF 162
Cdd:cd07734  155 IQIYGEKLVYTGDFSN 170
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 18-132 4.41e-08

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: 52.92  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  18 NMYLVeVDEAIYvlDCGLVYPPDELLGIdmmipdFTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE 97
Cdd:cd16275   13 YSYII-IDKATR--EAAVVDPAWDIEKI------LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEID 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515407687  98 LAKIQtkkiglknYQDFHIISEDNEIDFGNVVIKF 132
Cdd:cd16275   84 YYGFR--------CPNLIPLEDGDTIKIGDTEITC 110
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 362-405 9.11e-07

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 46.07  E-value: 9.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 515407687  362 SGHASPKDLQLMISLLKPKYVVPISGEYRLMSAHK-HLATEVGIP 405
Cdd:pfam07521  15 SGHADRRELLELIKGLKPKPIVLVHGEPRALLALAeLLKEELGIE 59
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-160 2.67e-06

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: 48.29  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   7 IALGGVRENGKNMYLVEVDEAIYVLDCGLvyppDELLgiDMMIPDftYLKENQDRVAGVFLTHGHADAIGALPYLLK--D 84
Cdd:cd16293    2 TPLSGAGDESPLCYLLEIDDVTILLDCGW----DESF--DMEYLE--SLKRIAPTIDAVLLSHPDLEHLGALPYLVGklG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  85 IQVPVFGTELTIELAKIQTKK--IGLKNYQDFHIIS-EDNEIDFGNVV-IKFFKTTHSVPESVGIEV------------- 147
Cdd:cd16293   74 LTCPVYATLPVHKMGRMFMYDlyQSRGLEEDFNLFTlDDVDEAFDRITqLKYSQPVNLRGKGDGLTItaynaghtlggti 153

                        170
                 ....*....|....*.
gi 515407687 148 ---STPEGSIVYTGDF 160
Cdd:cd16293  154 wkiTKDSEDIVYAVDW 169
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 60-159 3.98e-06

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: 47.69  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   60 DRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIE-LAK-IQTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTT- 136
Cdd:pfam12706  27 DPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAhLRRnFPYLFLLEHYGVRVHEIDWGESFTVGDGGLTVTATPa 106

                          90       100       110
                  ....*....|....*....|....*....|..
gi 515407687  137 -HSVP--------ESVGIEVSTPEGSIVYTGD 159
Cdd:pfam12706 107 rHGSPrgldpnpgDTLGFRIEGPGKRVYYAGD 138
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 21-159 4.42e-06

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 48.32  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  21 LVEVDEAIYVL-DCGLVYPPDelLGIDMMIPdftYLKENQ-DRVAGVFLTHGHADAIGALPYLLKDIQV------PVFGT 92
Cdd:COG2333   15 LIRTPDGKTILiDTGPRPSFD--AGERVVLP---YLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVgrvlvsGPPDT 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515407687  93 ELTIE--LAKIQTKKIglknyqDFHIISEDNEIDFGNVVIKFFKTTHSVPE-------SVGIEVSTPEGSIVYTGD 159
Cdd:COG2333   90 SETYErlLEALKEKGI------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEgsdennnSLVLRLTYGGFSFLLTGD 159
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 18-90 1.18e-05

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: 46.45  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515407687  18 NMYLVEVDEAIYVLDCGLVYPPDELLgidmmipdfTYLKE---NQDRVAGVFLTHGHADAIGALPYLLKDIQVPVF 90
Cdd:cd07721   12 NAYLIEDDDGLTLIDTGLPGSAKRIL---------KALRElglSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVY 78
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 62-163 2.16e-05

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


Pssm-ID: 293824  Cd Length: 189  Bit Score: 45.36  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  62 VAGVFLTHGHADAI-GALPYLLKDIQVPVFGTELTIE--LAKIQT----KKIGLKNYQDFHIISEDNEIDFGNVVIKFFK 134
Cdd:cd07738   49 VDHVILTHCHADHDaGTFQKILEEEKITLYTTRTINEsfLRKYAAltglPPDFLEELFDFRPVIIGEKTKINGAEFEFDY 128

                         90       100
                 ....*....|....*....|....*....
gi 515407687 135 TTHSVPeSVGIEVSTPEGSIVYTGDFKFD 163
Cdd:cd07738  129 SFHSIP-TIRFKVSYGGKSIAYSGDTRYD 156
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 6-165 2.31e-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: 45.33  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   6 IIALGGVRENGKNMYLVEVDEAIYVLDCG--LVYPPDELLgidmmiPDFTYLKENQ---DRVAGVFLTHGHADAIGALPY 80
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGmhMGYNDERRF------PDFSYISQNGpftEHIDCVIISHFHLDHCGALPY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  81 LLKDIQV--PVFGTELTIELA--------KIQTKKIGLKN-YQDFHI-----------ISEDNEIDfGNVVIKFFKTTHs 138
Cdd:cd16291   75 FTEVVGYdgPIYMTHPTKAICpilledyrKIAVERKGETNfFTSQMIkdcmkkviavnLHETVQVD-DELEIKAYYAGH- 152

                        170       180
                 ....*....|....*....|....*..
gi 515407687 139 VPESVGIEVSTPEGSIVYTGDfkFDMT 165
Cdd:cd16291  153 VLGAAMFYVRVGDESVVYTGD--YNMT 177
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-171 3.63e-05

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: 45.26  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  55 LKENQDRVAGVFLTHGHADAIGalpyllkDIQVPV----------FGTELTIELAKIQTKKIGLKNYQDF----HIISED 120
Cdd:cd07741   47 PKLDPTKLDAIILSHRHLDHSN-------DANVLIeamteggfkkRGTLLAPEDALNGEPVVLLYYHRRKleeiEILEEG 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515407687 121 NEIDFGNVVIKFFKTTHSVPESVGIEVSTPEGSIVYTGDFKFDMTVSDAYK 171
Cdd:cd07741  120 DEYELGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISDTRYFEELIEYYS 170
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 54-160 4.05e-05

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: 44.31  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  54 YLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTEltielakiqtkkiGLKNYQDFHIISEDNEIDFGNVVIKFF 133
Cdd:cd07724   41 LAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE-------------GAPASFFDRLLKDGDVLELGNLTLEVL 107

                         90       100
                 ....*....|....*....|....*...
gi 515407687 134 KTT-HSvPESVGIEVSTPEGsiVYTGDF 160
Cdd:cd07724  108 HTPgHT-PESVSYLVGDPDA--VFTGDT 132
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 8-158 5.10e-05

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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: 293857  Cd Length: 212  Bit Score: 44.74  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687   8 ALGGVRENGKNMYLVeVDEAIYVLDCglvyPPDEllgiDMMIPDFTYLKENQDR-VAGVFLTHGHADAIGALPYLLKdIQ 86
Cdd:cd16299   18 EFNGVKYSANAMYLV-TKKGVILFDT----PWDK----DQYQPLLDSIRKKHNLpVIAVIATHSHEDRAGGLGYFNK-IG 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515407687  87 VPVFGTELTIELAKIQTKKiglknyQDFHIISEDNEIDFGN--VVIKFFKTTHSVPESVgieVSTPEGSIVYTG 158
Cdd:cd16299   88 IPTYATAMTNSILKKENKP------QATYLIETDKTYKIGGekFVVYFFGEGHTADNVV---VWFPKEKVLDGG 152
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 10-116 6.66e-05

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 44.20  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  10 GGVRENGknMYLVEVDEAiYVLDCGLVYPPDELLgIDMMIPDFTYlkenqdRVAGVFLTHGHADAIGALPYlLKDIQVPV 89
Cdd:cd16285   22 GAVPSNG--LIVIDGKGL-VLIDTPWTEAQTATL-LDWIEKKLGK------PVTAAISTHSHDDRTGGIKA-LNARGIPT 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 515407687  90 FGTELTIELAKIQTKKI---GLKNYQDFHI 116
Cdd:cd16285   91 YATALTNELAKKEGKPVpthSLKGALTLGF 120
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 54-159 3.47e-04

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: 41.74  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  54 YLKE-NQDRVAGVFLTHGHADAIGALPYLLKDIQV------PVFGTELTIELAKIQTKKIGLKnyqdFHIISEDNEIDFG 126
Cdd:cd07731   40 YLKArGIKKLDYLILTHPDADHIGGLDAVLKNFPVkevympGVTHTTKTYEDLLDAIKEKGIP----VTPCKAGDRWQLG 115

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515407687 127 NVVIKFFKTTHSVPE-----SVGIEVSTPEGSIVYTGD 159
Cdd:cd07731  116 GVSFEVLSPPKDDYDdlnnnSCVLRLTYGGTSFLLTGD 153
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 56-179 4.94e-04

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 41.76  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  56 KENQDRVAGVFLTHGHADAIGALPYlLKDIQVPVFGTELTIELAKIQTKKI------GLKNYQDFHIISEDNEIDfGNVV 129
Cdd:cd07707   53 KVSQKPVTEVINTHFHTDRAGGNAY-LKERGAKTVSTALTRDLAKSEWAEIvaftrkGLPEYPDLGYELPDGVLD-GDFN 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515407687 130 IKFFKTTHSVPESV----GIEVSTPEGSIVYTGDFKFDMT---VSDAYKTDFSRIVE 179
Cdd:cd07707  131 LQFGKVEAFYPGPAhtpdNIVVYFPQENVLYGGCIIKETDlgnVADADVKEWPTSIE 187
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 52-133 6.18e-04

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 41.50  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  52 FTYLKEN-QDRVAGVFLTHGHADAIGALPyLLKDIQVPVFGTELTIELAKIQTKkiGLKNYqdfhIISEDNEIDFGNVVI 130
Cdd:cd16304   53 LDWIKKKlKKPVTLAIVTHAHDDRIGGIK-ALQKRGIPVYSTKLTAQLAKKQGY--PSPDG----ILKDDTTLKFGNTKI 125


                 ...
gi 515407687 131 KFF 133
Cdd:cd16304  126 ETF 128
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 60-161 6.53e-04

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: 40.32  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  60 DRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTELTIELAkiqTKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSV 139
Cdd:cd07733   44 EDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRAM---ERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDA 120

                         90       100
                 ....*....|....*....|..
gi 515407687 140 PESVGIEVSTPEGSIVYTGDFK 161
Cdd:cd07733  121 ADPVGYRFEEGGRRFGMLTDLK 142
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-159 1.38e-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: 39.93  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  19 MYLVEVDEAIYVLDCGlvypPDELLGIdmmipdftyLKENQDRVA--GVFLTHGHADAIGALPYLLKDIQV--------P 88
Cdd:cd07740   18 CFHVASEAGRFLIDCG----ASSLIAL---------KRAGIDPNAidAIFITHLHGDHFGGLPFFLLDAQFvakrtrplT 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515407687  89 VFGTELTIELAK--IQTKKIGL-KNYQDFHI----ISEDNEIDFGNVVIKFFKTTHSVPE-SVGIEVSTPEGSIVYTGD 159
Cdd:cd07740   85 IAGPPGLRERLRraMEALFPGSsKVPRRFDLevieLEPGEPTTLGGVTVTAFPVVHPSGAlPLALRLEAAGRVLAYSGD 163
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 54-135 1.40e-03

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: 39.75  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  54 YLKENQDRVAGVFLTHGHADAIGALPYLLKDI-QVPVFGTELTielakiqtkKIGLKNyqdfHIISEDNEIDFGNVVIKF 132
Cdd:cd07723   36 ALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAED---------RIPGLD----HPVKDGDEIKLGGLEVKV 102


                 ...
gi 515407687 133 FKT 135
Cdd:cd07723  103 LHT 105
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 66-177 1.90e-03

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: 39.04  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  66 FLTHGHADAIGALPyllKDIQVPVFGTELTIELAKiqtKKIGLKNyQDFHIISEDNEIDFGNVVIKFFKTTHsVPESVGI 145
Cdd:cd16298   41 FLTHFHSDHYCGLT---KKFKFPIYCSKITGNLVK---SKLKVEE-QYINVLPMNTECIVNGVKVVLLDANH-CPGAVMI 112

                         90       100       110
                 ....*....|....*....|....*....|...
gi 515407687 146 EVSTPEG-SIVYTGDFKFDMTVSDAYKTDFSRI 177
Cdd:cd16298  113 LFRLPSGtLVLHTGDFRADPSMERYPELIGQKI 145
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 65-159 3.04e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.52  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  65 VFLTHGHADAIG--ALPYLLKDiQVPVFGTEltiELAkiqtKKIGLKNYQDFHIISEDNEIDFGNVVIKFFKTTHSVPES 142
Cdd:COG2220   52 VLVTHDHYDHLDdaTLRALKRT-GATVVAPL---GVA----AWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRP 123

                         90       100
                 ....*....|....*....|....
gi 515407687 143 -------VGIEVSTPEGSIVYTGD 159
Cdd:COG2220  124 drngglwVGFVIETDGKTIYHAGD 147
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 10-144 4.07e-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: 38.77  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  10 GGVRENGknMYLVEVDEAIyVLDCglvyPPDELLGIDMMipdfTYLKEN-QDRVAGVFLTHGHADAIGALPYlLKDIQVP 88
Cdd:cd16302   23 GKVPCNG--MIVINGGEAV-VFDT----PTNDSQSEELI----DWIENSlKAKVKAVVPTHFHDDCLGGLKA-FHRRGIP 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515407687  89 VFGTELTIELAKIQTKKIGLKNYQDFHIISEDNEidfgNVVIKFFKTTHSVPESVG 144
Cdd:cd16302   91 SYANQKTIALAKEKGLPVPQHGFSDSLTLKLGGK----KIVCRYFGEGHTKDNIVV 142
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-102 4.95e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 38.67  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515407687  20 YLVEVDEAiYVLDCGLvyppDELLGIDMmipdFTYLKENQDRVAGVFLTHGHADAIGALPYLLKDIQVPVFGTEltIELA 99
Cdd:cd07743   13 YVFGDKEA-LLIDSGL----DEDAGRKI----RKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPK--IEKA 81


                 ...
gi 515407687 100 KIQ 102
Cdd:cd07743   82 FIE 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH