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Conserved domains on  [gi|1080618509|gb|OFN94235|]
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ribonuclease J [Streptococcus sp. HMSC074F05]

Protein Classification

ribonuclease J( domain architecture ID 11426779)

ribonuclease J plays a key part in RNA processing and in RNA degradation; it can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end

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

Graphical summary

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List of domain hits

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

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 728.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   1 MSSIKLVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPY 80
Cdd:COG0595     3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  81 LLAEAKVPVFGTELTIELAKLFVKSNDsVKKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGD 160
Cdd:COG0595    83 LLKELNVPVYGTPLTLALLEAKLKEHG-LLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 161 FKFDQTASESYATDFARLAEIGREGVLALLSDSANADSKMQVASEQEVGDEILDTIADWDGRVIVAAVASNLSRIQQVFD 240
Cdd:COG0595   162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 241 AAAGTGRRVVLTGFDVENIVRTAIRLNKLSLAnEKLLIKPKEMSRFEDHELIILETGRMGEPINGLRKMSIGRHRYVEIK 320
Cdd:COG0595   242 AAKKHGRKVALVGRSMERNVEIARELGYLKIP-DGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 321 DGDLVYIVTTPSIAKEAVVARVENMVYQAGgvVKLITSSLR---VSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHA 397
Cdd:COG0595   321 PGDTVIFSSSPIPGNEKAVARVINELYRLG--AEVIYDSDAkvhVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 398 RVAMEVGILPENIFIPKRGTVMEYEKGDFVPAGSVSAGDVMIDGNAIGDVGNIVLRDRKVLSEDGIFIVAITVNRKEKKI 477
Cdd:COG0595   399 KLAEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKL 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080618509 478 ISKARVHTRGFVYVKKSRDILRESCELVNQSVEDYLNQDSFDWGELKGLVRDNLSKFLFEQTKRRPAILPVVMEV 552
Cdd:COG0595   479 VGGPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-552 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 728.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   1 MSSIKLVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPY 80
Cdd:COG0595     3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  81 LLAEAKVPVFGTELTIELAKLFVKSNDsVKKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGD 160
Cdd:COG0595    83 LLKELNVPVYGTPLTLALLEAKLKEHG-LLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 161 FKFDQTASESYATDFARLAEIGREGVLALLSDSANADSKMQVASEQEVGDEILDTIADWDGRVIVAAVASNLSRIQQVFD 240
Cdd:COG0595   162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 241 AAAGTGRRVVLTGFDVENIVRTAIRLNKLSLAnEKLLIKPKEMSRFEDHELIILETGRMGEPINGLRKMSIGRHRYVEIK 320
Cdd:COG0595   242 AAKKHGRKVALVGRSMERNVEIARELGYLKIP-DGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 321 DGDLVYIVTTPSIAKEAVVARVENMVYQAGgvVKLITSSLR---VSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHA 397
Cdd:COG0595   321 PGDTVIFSSSPIPGNEKAVARVINELYRLG--AEVIYDSDAkvhVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 398 RVAMEVGILPENIFIPKRGTVMEYEKGDFVPAGSVSAGDVMIDGNAIGDVGNIVLRDRKVLSEDGIFIVAITVNRKEKKI 477
Cdd:COG0595   399 KLAEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKL 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080618509 478 ISKARVHTRGFVYVKKSRDILRESCELVNQSVEDYLNQDSFDWGELKGLVRDNLSKFLFEQTKRRPAILPVVMEV 552
Cdd:COG0595   479 VGGPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 4-427 1.02e-117

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: 354.35  E-value: 1.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   4 IKLVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLA 83
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  84 EAKV-PVFGTELTIELAKLFVKSNdSVKKFNDFHVIDQNSEIDFGDA-VVSFFQTTHSIPESIGIVIGTPEGNIVYTGDF 161
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEH-GLNVRTDLLEIHEGEPVEFGENtAIEFFRITHSIPDSVGFALHTPLGYIVYTGDF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 162 KFDQTASESYATDFARLAEIGREGVLALLSDSANADSKMQVASEQEVGDEILDTIADWDGRVIVAAVASNLSRIQQVFDA 241
Cdd:TIGR00649 160 KFDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 242 AAGTGRRVVLTGFDVENIVRTAIRLNKLSLANEkLLIKPKEMSRFEDHELIILETGRMGEPINGLRKMSIGRHRYVEIKD 321
Cdd:TIGR00649 240 ARKNGRKVAVYGRSMESLIGIARRLGYIKCPHN-NFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 322 GDLVYIVTTPSIAKEAVVAR--VENMVYQAGgvVKLITsSLRVSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHARV 399
Cdd:TIGR00649 319 GDTVVFSAPPIPGNENIAVSitLDIRLNRAG--ARVIK-GIHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKL 395

                         410       420
                  ....*....|....*....|....*...
gi 1080618509 400 AMEVGILPENIFIPKRGTVMEYEkGDFV 427
Cdd:TIGR00649 396 AEEEGYPGENIFILRNGEVLEIN-GDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-421 3.77e-95

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: 290.08  E-value: 3.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   7 VTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAK 86
Cdd:cd07714     1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  87 VPVFGTELTIELAKLFVKSNDSVKKfNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGDFKFDQT 166
Cdd:cd07714    81 VPIYATPLTLALIKKKLEEFKLIKK-VKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 167 ASESYATDFARLAEIGREGVLALLSDSanadskmqvaseqevgdeildtiadwdgrvivaavasnlsriqqvfdaaagtg 246
Cdd:cd07714   160 PVDGKPTDLEKLAELGKEGVLLLLSDS----------------------------------------------------- 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 247 rrvvltgfdvenivrtairlnklslanekllikpkemsrfeDHeliiletgrmgepinglrkmsigrhryveikdgdlvy 326
Cdd:cd07714   187 -----------------------------------------VH------------------------------------- 188

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 327 ivttpsiakeavvarvenmvyqaggvvklitsslrVSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHARVAMEVGIL 406
Cdd:cd07714   189 -----------------------------------VSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIP 233

                         410
                  ....*....|....*
gi 1080618509 407 PENIFIPKRGTVMEY 421
Cdd:cd07714   234 EENIFLLENGDVLEL 248
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 451-552 2.87e-35

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: 127.62  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 451 VLRDRKVLSEDGIFIVAITVNRKEKKIISKARVHTRGFVYVKKSRDILRESCELVNQSVEDYLNQDSFDWGELKGLVRDN 530
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 1080618509 531 LSKFLFEQTKRRPAILPVVMEV 552
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-194 1.86e-20

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 88.76  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   18 NLYVAEVNDSIFVLDAGLKYPENeqlgvdvVIPNMDYLfeNKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAED-------LLAELKKL--GPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   98 LAKLFVKSN----DSVKKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIgtPEGNIVYTGDFKFDQTASESYAT 173
Cdd:smart00849  72 LLKDLLALLgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|.
gi 1080618509  174 DFARLAEIGREGVLALLSDSA 194
Cdd:smart00849 150 GGDAAASDALESLLKLLKLLP 170
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-552 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 728.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   1 MSSIKLVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPY 80
Cdd:COG0595     3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  81 LLAEAKVPVFGTELTIELAKLFVKSNDsVKKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGD 160
Cdd:COG0595    83 LLKELNVPVYGTPLTLALLEAKLKEHG-LLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 161 FKFDQTASESYATDFARLAEIGREGVLALLSDSANADSKMQVASEQEVGDEILDTIADWDGRVIVAAVASNLSRIQQVFD 240
Cdd:COG0595   162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 241 AAAGTGRRVVLTGFDVENIVRTAIRLNKLSLAnEKLLIKPKEMSRFEDHELIILETGRMGEPINGLRKMSIGRHRYVEIK 320
Cdd:COG0595   242 AAKKHGRKVALVGRSMERNVEIARELGYLKIP-DGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 321 DGDLVYIVTTPSIAKEAVVARVENMVYQAGgvVKLITSSLR---VSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHA 397
Cdd:COG0595   321 PGDTVIFSSSPIPGNEKAVARVINELYRLG--AEVIYDSDAkvhVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 398 RVAMEVGILPENIFIPKRGTVMEYEKGDFVPAGSVSAGDVMIDGNAIGDVGNIVLRDRKVLSEDGIFIVAITVNRKEKKI 477
Cdd:COG0595   399 KLAEEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKL 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080618509 478 ISKARVHTRGFVYVKKSRDILRESCELVNQSVEDYLNQDSFDWGELKGLVRDNLSKFLFEQTKRRPAILPVVMEV 552
Cdd:COG0595   479 VGGPDIVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 4-427 1.02e-117

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: 354.35  E-value: 1.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   4 IKLVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLA 83
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  84 EAKV-PVFGTELTIELAKLFVKSNdSVKKFNDFHVIDQNSEIDFGDA-VVSFFQTTHSIPESIGIVIGTPEGNIVYTGDF 161
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEH-GLNVRTDLLEIHEGEPVEFGENtAIEFFRITHSIPDSVGFALHTPLGYIVYTGDF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 162 KFDQTASESYATDFARLAEIGREGVLALLSDSANADSKMQVASEQEVGDEILDTIADWDGRVIVAAVASNLSRIQQVFDA 241
Cdd:TIGR00649 160 KFDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 242 AAGTGRRVVLTGFDVENIVRTAIRLNKLSLANEkLLIKPKEMSRFEDHELIILETGRMGEPINGLRKMSIGRHRYVEIKD 321
Cdd:TIGR00649 240 ARKNGRKVAVYGRSMESLIGIARRLGYIKCPHN-NFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 322 GDLVYIVTTPSIAKEAVVAR--VENMVYQAGgvVKLITsSLRVSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHARV 399
Cdd:TIGR00649 319 GDTVVFSAPPIPGNENIAVSitLDIRLNRAG--ARVIK-GIHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKL 395

                         410       420
                  ....*....|....*....|....*...
gi 1080618509 400 AMEVGILPENIFIPKRGTVMEYEkGDFV 427
Cdd:TIGR00649 396 AEEEGYPGENIFILRNGEVLEIN-GDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-421 3.77e-95

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: 290.08  E-value: 3.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   7 VTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAK 86
Cdd:cd07714     1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  87 VPVFGTELTIELAKLFVKSNDSVKKfNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGDFKFDQT 166
Cdd:cd07714    81 VPIYATPLTLALIKKKLEEFKLIKK-VKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 167 ASESYATDFARLAEIGREGVLALLSDSanadskmqvaseqevgdeildtiadwdgrvivaavasnlsriqqvfdaaagtg 246
Cdd:cd07714   160 PVDGKPTDLEKLAELGKEGVLLLLSDS----------------------------------------------------- 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 247 rrvvltgfdvenivrtairlnklslanekllikpkemsrfeDHeliiletgrmgepinglrkmsigrhryveikdgdlvy 326
Cdd:cd07714   187 -----------------------------------------VH------------------------------------- 188

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 327 ivttpsiakeavvarvenmvyqaggvvklitsslrVSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHARVAMEVGIL 406
Cdd:cd07714   189 -----------------------------------VSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIP 233

                         410
                  ....*....|....*
gi 1080618509 407 PENIFIPKRGTVMEY 421
Cdd:cd07714   234 EENIFLLENGDVLEL 248
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 451-552 2.87e-35

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: 127.62  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509 451 VLRDRKVLSEDGIFIVAITVNRKEKKIISKARVHTRGFVYVKKSRDILRESCELVNQSVEDYLNQDSFDWGELKGLVRDN 530
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 1080618509 531 LSKFLFEQTKRRPAILPVVMEV 552
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 10-163 9.76e-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: 90.36  E-value: 9.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  10 GGVRENGKNlyVAEV--NDSIFVLDAGLKYP-------ENEQLGVDVVIPNMD-----------YLFENKDRIAGVFLTH 69
Cdd:cd07732     6 RGTNEIGGN--CIEVetGGTRILLDFGLPLDpeskyfdEVLDFLELGLLPDIVglyrdplllggLRSEEDPSVDAVLLSH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  70 GHADAIGALPYLLAEakVPVFGTELTIELAKLFVKSNDSVKKF-NDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVI 148
Cdd:cd07732    84 AHLDHYGLLNYLRPD--IPVYMGEATKRILKALLPFFGEGDPVpRNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYAFLI 161

                         170
                  ....*....|....*
gi 1080618509 149 GTPEGNIVYTGDFKF 163
Cdd:cd07732   162 EAPGKRIFYTGDFRF 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-194 1.86e-20

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 88.76  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   18 NLYVAEVNDSIFVLDAGLKYPENeqlgvdvVIPNMDYLfeNKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAED-------LLAELKKL--GPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   98 LAKLFVKSN----DSVKKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIgtPEGNIVYTGDFKFDQTASESYAT 173
Cdd:smart00849  72 LLKDLLALLgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|.
gi 1080618509  174 DFARLAEIGREGVLALLSDSA 194
Cdd:smart00849 150 GGDAAASDALESLLKLLKLLP 170
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 6-166 2.16e-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: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   6 LVTLGGVRENGKNLYVAEVNDSIFVLDAGLkYPENEQLGVDvviPNMDYLFENKDrIAGVFLTHGHADAIGALPYLLAEA 85
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGL-FQGGKELEEL---NNEPFPFDPKE-IDAVILTHAHLDHSGRLPLLVKEG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  86 -KVPVFGTELTIELAKL----FVK----------------SNDSVKKFNDFHVIDQNSEIDFGDAV-VSFFQTTHsIPES 143
Cdd:cd16295    76 fRGPIYATPATKDLAELllldSAKiqeeeaehppaeplytEEDVEKALKHFRPVEYGEPFEIGPGVkVTFYDAGH-ILGS 154

                         170       180
                  ....*....|....*....|....
gi 1080618509 144 IGIVIGTPEG-NIVYTGDFKFDQT 166
Cdd:cd16295   155 ASVELEIGGGkRILFSGDLGRKNT 178
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-166 3.24e-14

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 74.45  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   5 KLVTLGGVRENGKNLYVAEVNDSIFVLDAGL----KYPENEQLGVDVVipnmdylfenkdRIAGVFLTHGHADAIGALPY 80
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLfqggKERNWPPFPFRPS------------DVDAVVLTHAHLDHSGALPL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  81 LLAE-AKVPVFGTELTIELAKLFVKsnDSVK-------------------KFNDFHVIDQNSEIDFGDAVVSFFQTTHsI 140
Cdd:COG1236    70 LVKEgFRGPIYATPATADLARILLG--DSAKiqeeeaeaeplyteedaerALELFQTVDYGEPFEIGGVRVTFHPAGH-I 146

                         170       180
                  ....*....|....*....|....*.
gi 1080618509 141 PESIGIVIGTPEGNIVYTGDFKFDQT 166
Cdd:COG1236   147 LGSAQVELEVGGKRIVFSGDYGREDD 172
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
20-160 5.49e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 71.76  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  20 YVAEVNDSIFVLDAG------LKypeneQLGVDVvipnmdylfenkDRIAGVFLTHGHADAIGALPYLLA-------EAK 86
Cdd:COG1234    22 YLLEAGGERLLIDCGegtqrqLL-----RAGLDP------------RDIDAIFITHLHGDHIAGLPGLLStrslagrEKP 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080618509  87 VPVFGTELTIELAKLFVKSNDSVKKFN-DFHVIDQNSEIDFGDAVVSFFQTTHSIPeSIGIVIGTPEGNIVYTGD 160
Cdd:COG1234    85 LTIYGPPGTKEFLEALLKASGTDLDFPlEFHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGD 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 23-160 1.08e-13

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 71.08  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  23 EVNDSIFVLDAG--LKypenEQlgvdvvipnMDYLFENKDRIAGVFLTHGHADAIGALPYL---LAEAKVPVFGTELTIE 97
Cdd:COG1235    41 EADGTRLLIDAGpdLR----EQ---------LLRLGLDPSKIDAILLTHEHADHIAGLDDLrprYGPNPIPVYATPGTLE 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080618509  98 -----LAKLFVKSNDSVkkfnDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGD 160
Cdd:COG1235   108 alerrFPYLFAPYPGKL----EFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 5-163 1.70e-12

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: 66.16  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   5 KLVTLGGVRENGknLYVAEVNDSIFVLDAGlkYPENEQLgvdvvipnMDYLFENKDRIAGVFLTHGHADAIGALPYLLAE 84
Cdd:cd06262     1 KRLPVGPLQTNC--YLVSDEEGEAILIDPG--AGALEKI--------LEAIEELGLKIKAILLTHGHFDHIGGLAELKEA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  85 AKVPVFGTELTIELAKLFVKSNDS-----VKKFNDFHVIDQNSEIDFGDAVVSFFQTT-HSiPESIGIVIgtPEGNIVYT 158
Cdd:cd06262    69 PGAPVYIHEADAELLEDPELNLAFfgggpLPPPEPDILLEDGDTIELGGLELEVIHTPgHT-PGSVCFYI--EEEGVLFT 145


                  ....*
gi 1080618509 159 GDFKF 163
Cdd:cd06262   146 GDTLF 150
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 60-180 2.91e-12

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: 65.16  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  60 DRIAGVFLTHGHAD----------AIGALPYLLAEAKVPVFGTELTIELAKLFVKSNDSVkkfnDFHVIDQNSEIDFGDA 129
Cdd:cd07716    49 EDLDAVVLSHLHPDhcadlgvlqyARRYHPRGARKPPLPLYGPAGPAERLAALYGLEDVF----DFHPIEPGEPLEIGPF 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080618509 130 VVSFFQTTHSIPeSIGIVIGTPEGNIVYTGDfkfdqTAsesYATDFARLAE 180
Cdd:cd07716   125 TITFFRTVHPVP-CYAMRIEDGGKVLVYTGD-----TG---YCDELVEFAR 166
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 12-175 9.17e-12

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: 65.31  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  12 VRENGKNLYVAevndsifvLDAG--LKYPENEQLGVDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALP------YLLA 83
Cdd:cd07735    22 LDPAGSDGDIL--------LDAGtgVGALSLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPllspndGGQR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  84 EAKVPVFGTELTIELAK--LFvksNDSV-----------KKFNDFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGT 150
Cdd:cd07735    94 GSPKTIYGLPETIDALKkhIF---NWVIwpdftsipsgkYPYLRLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRD 170

                         170       180
                  ....*....|....*....|....*
gi 1080618509 151 PEGNIVYTGDFKFDQTASESYATDF 175
Cdd:cd07735   171 GGDSFLFFGDTGPDSVSKSPRLDAL 195
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 20-160 1.26e-11

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: 63.44  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  20 YVAEVNDSIFVLDAGlkypENeqlgvdvVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTI--- 96
Cdd:cd16272    20 YLLETGGTRILLDCG----EG-------TVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKPLTIygp 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080618509  97 ----ELAKLFVKSNDSVKKFN---DFHVIDQNSEI-DFGDAVVSFFQTTHSIPeSIGIVIGTPEGNIVYTGD 160
Cdd:cd16272    89 kgikEFLEKLLNFPVEILPLGfplEIEELEEGGEVlELGDLKVEAFPVKHSVE-SLGYRIEAEGKSIVYSGD 159
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 18-160 1.28e-11

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 64.33  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  18 NLYVAEVNDSIFVLDAGLKYPENEQLgvdvvipnMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE 97
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080618509  98 -LAKLFVKSNDSVKKFNDFHVIDQNSEIDFGDAVVSFFQTT-HSiPESIGIVIgtPEGNIVYTGD 160
Cdd:COG0491    88 aLEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPgHT-PGHVSFYV--PDEKVLFTGD 149
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 59-160 9.38e-11

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: 61.17  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  59 KDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE-LAKLFVKSNDSVKKFNDFHVIDQNSEIDFGDAVVSFFQTT 137
Cdd:pfam12706  26 DDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAhLRRNFPYLFLLEHYGVRVHEIDWGESFTVGDGGLTVTATP 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1080618509 138 --HSIP--------ESIGIVIGTPEGNIVYTGD 160
Cdd:pfam12706 106 arHGSPrgldpnpgDTLGFRIEGPGKRVYYAGD 138
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 57-163 3.92e-10

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 59.41  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  57 ENKDRIAGVFLTHGHADAIGALP-----YLLAEAKVPVFGTELTIE-LAKLFVKSNDSVKKFN----DFHVIDQNSEIDF 126
Cdd:cd16279    62 AGIRKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASEETLDdLKRRFPYFFAATGGGGvpklDLHIIEPDEPFTI 141

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1080618509 127 GDAVVSFFQTTHSIPESIGIVIgtpeGNIVYTGDFKF 163
Cdd:cd16279   142 GGLEITPLPVLHGKLPSLGFRF----GDFAYLTDVSE 174
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 362-413 2.91e-09

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 53.39  E-value: 2.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1080618509 362 VSGHGNARDLQLMINLLRPKYLFPIQGEYRELDAHARVAMEvgILPENIFIP 413
Cdd:pfam07521  14 FSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKE--ELGIEVFVP 63
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-163 4.53e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.22  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  18 NLYVAEVNDSIFVLDAGLKYPENEQLgvdvvipNMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLL-------LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080618509  98 LAKLFVKSNDSVKKFN-------DFHVIDQNSEIDFGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGDFKF 163
Cdd:pfam00753  80 ELLDEELGLAASRLGLpgppvvpLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLF 152
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 9-166 2.64e-07

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: 51.18  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   9 LGGVRENGKNLYVAEVNDSIFVLDAGLkypeneqlgvDVVIPNMDYLFENKDRIAG----VFLTHGHADAIGALPYLLAE 84
Cdd:cd07734     3 LGGGQEVGRSCFLVEFKGRTVLLDCGM----------NPGKEDPEACLPQFELLPPeidaILISHFHLDHCGALPYLFRG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  85 A--KVPVFGTELTIELAKL----FVKSNDSVKKFNDFH-------VIDQNSEIDFGDAV-------VSFFQTTHsIPESI 144
Cdd:cd07734    73 FifRGPIYATHPTVALGRLlledYVKSAERIGQDQSLYtpedieeALKHIVPLGYGQSIdlfpalsLTAYNAGH-VLGAA 151

                         170       180
                  ....*....|....*....|..
gi 1080618509 145 GIVIGTPEGNIVYTGDFKFDQT 166
Cdd:cd07734   152 MWEIQIYGEKLVYTGDFSNTED 173
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 62-197 2.92e-06

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: 48.06  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  62 IAGVFLTHGHADAI-GALPYLLAEAKVPVFGTElTI------ELAKLFVKSNDSVKKFNDFHVIDQNSEIDFGDAVVSFF 134
Cdd:cd07738    49 VDHVILTHCHADHDaGTFQKILEEEKITLYTTR-TInesflrKYAALTGLPPDFLEELFDFRPVIIGEKTKINGAEFEFD 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080618509 135 QTTHSIPeSIGIVIGTPEGNIVYTGDFKFDQtasesyatdfARLAEIGREGVLA------LLSDSANAD 197
Cdd:cd07738   128 YSFHSIP-TIRFKVSYGGKSIAYSGDTRYDP----------DGLKSLYEQGILSesrrafLLRFPWDAD 185
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 18-90 5.18e-06

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: 47.60  E-value: 5.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080618509  18 NLYVAEVNDSIFVLDAGLKYPEneqlgvDVVIPNMDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAKVPVF 90
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGLPGSA------KRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVY 78
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 25-160 1.00e-05

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: 47.16  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  25 NDSIFVLDAGLKYPENeqLGVDVVIPNMDYLfeNKDRIAGVFLTHGHADAIGALPYLLAEAKV-------PVFGTELTIE 97
Cdd:COG2333    20 DGKTILIDTGPRPSFD--AGERVVLPYLRAL--GIRRLDLLVLTHPDADHIGGLAAVLEAFPVgrvlvsgPPDTSETYER 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  98 LAKLFVKSNDSVkkfndfHVIDQNSEIDFGDAVVSFFQTTHSIPE-------SIGIVIGTPEGNIVYTGD 160
Cdd:COG2333    96 LLEALKEKGIPV------RPCRAGDTWQLGGVRFEVLWPPEDLLEgsdennnSLVLRLTYGGFSFLLTGD 159
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 23-160 1.74e-05

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: 45.58  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  23 EVNDSIFVLDAGLKYPEN-EQLGVDVvipnmdylfenkDRIAGVFLTHGHADAIGALPYLL-------AEAKVPVFGTEL 94
Cdd:cd07719    24 VVGGRVYLVDAGSGVVRRlAQAGLPL------------GDLDAVFLTHLHSDHVADLPALLltawlagRKTPLPVYGPPG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  95 TIELAKLFVKSND---------SVKKFNDFHVIDQNSEIDFGDAV-------VSFFQTTHS-IPESIGIVIGTPEGNIVY 157
Cdd:cd07719    92 TRALVDGLLAAYAldidyrariGDEGRPDPGALVEVHEIAAGGVVyeddgvkVTAFLVDHGpVPPALAYRFDTPGRSVVF 171


                  ...
gi 1080618509 158 TGD 160
Cdd:cd07719   172 SGD 174
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 45-161 3.05e-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: 44.70  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  45 VDVVIpnmDYLFENKDRIAGVFLTHGHADAIGALPYLLAEAKvpvfgteltielAKLFVKSNDSVKKFndFHVIDQNSEI 124
Cdd:cd07724    35 VDRYL---DLAAELGLKITYVLETHVHADHVSGARELAERTG------------APIVIGEGAPASFF--DRLLKDGDVL 97

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1080618509 125 DFGDAVVSFFQTT-HSiPESIGIVIGTPEGniVYTGDF 161
Cdd:cd07724    98 ELGNLTLEVLHTPgHT-PESVSYLVGDPDA--VFTGDT 132
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 60-180 4.62e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.91  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  60 DRIAGVFLTHGHADAIG-ALPYLLAEAKVPVFGTEltiELAKLFVKsndsvKKFNDFHVIDQNSEIDFGDAVVSFFQTTH 138
Cdd:COG2220    47 PKIDAVLVTHDHYDHLDdATLRALKRTGATVVAPL---GVAAWLRA-----WGFPRVTELDWGESVELGGLTVTAVPARH 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1080618509 139 SIPES-------IGIVIGTPEGNIVYTGDfkfdqTAsesYATDFARLAE 180
Cdd:COG2220   119 SSGRPdrngglwVGFVIETDGKTIYHAGD-----TG---YFPEMKEIGE 159
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 57-133 4.72e-05

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: 44.06  E-value: 4.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080618509  57 ENKDRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIELAKLfvksndsvkKFNDFHVIDQNSEIDFGDAVVSF 133
Cdd:cd16275    43 ELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGF---------RCPNLIPLEDGDTIKIGDTEITC 110
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 61-100 5.08e-04

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 41.50  E-value: 5.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1080618509  61 RIAGVFLTHGHADAIGALPYlLAEAKVPVFGTELTIELAK 100
Cdd:cd16285    63 PVTAAISTHSHDDRTGGIKA-LNARGIPTYATALTNELAK 101
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 60-161 5.94e-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: 41.70  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  60 DRIAGVFLTHGHADAIGALPYLLAEAK-VPVFGTELTIELAKLFVKSNDSvkkfnDFHVIDQNSEIDFGDAVVSFFQTT- 137
Cdd:cd07709    67 RKIDYIVVNHQEPDHSGSLPELLELAPnAKIVCSKKAARFLKHFYPGIDE-----RFVVVKDGDTLDLGKHTLKFIPAPm 141

                          90       100
                  ....*....|....*....|....*
gi 1080618509 138 -HSiPESigIVIGTPEGNIVYTGDF 161
Cdd:cd07709   142 lHW-PDT--MVTYDPEDKILFSGDA 163
NorV COG0426
Flavorubredoxin [Energy production and conversion];
60-161 7.09e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.13  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  60 DRIAGVFLTHGHADAIGALPYLLAEA-KVPVFGTELTIELAKLFVKSNDSvkkfnDFHVIDQNSEIDFGDAVVSFFQT-- 136
Cdd:COG0426    69 KKIDYIIVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLPHFYGIPDF-----RFIVVKEGDTLDLGGHTLQFIPApm 143

                          90       100
                  ....*....|....*....|....*
gi 1080618509 137 THSiPESigIVIGTPEGNIVYTGDF 161
Cdd:COG0426   144 LHW-PDT--MFTYDPEDKILFSGDA 165
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-163 8.12e-04

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 41.02  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  58 NKDRIAGVFLTHGHADAIGALPYLLaEAKvpvfgTELTIELAKLFVKSNDSV------------KKFNDFHVIDQNSEID 125
Cdd:cd07741    50 DPTKLDAIILSHRHLDHSNDANVLI-EAM-----TEGGFKKRGTLLAPEDALngepvvllyyhrRKLEEIEILEEGDEYE 123

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1080618509 126 FGDAVVSFFQTTHSIPESIGIVIGTPEGNIVYTGDFKF 163
Cdd:cd07741   124 LGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISDTRY 161
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 26-87 1.25e-03

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 39.81  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  26 DSIFV--------LDAGlkypENEQLGVDVVIPNMDYLfeNKDRIAGVFLTHGHADAIGALPYLLAEAKV 87
Cdd:cd07731    11 DAILIqtpgktilIDTG----PRDSFGEDVVVPYLKAR--GIKKLDYLILTHPDADHIGGLDAVLKNFPV 74
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 45-119 1.38e-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: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  45 VDVVIPN--MDYLFENKDRIAGVFLTHGHADAIGALPYLLAE-AKVPVFG-TELTIELAKLFVKSNDSVKKFN-DFHVID 119
Cdd:cd07723    25 VDPGEAEpvLAALEKNGLTLTAILTTHHHWDHTGGNAELKALfPDAPVYGpAEDRIPGLDHPVKDGDEIKLGGlEVKVLH 104
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-160 1.81e-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: 39.55  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  29 FVLDAGLK-YPENEQLGVDvviPNmdylfenkdRIAGVFLTHGHADAIGALPYLLAEAKV--------PVFGTELTIELA 99
Cdd:cd07740    28 FLIDCGASsLIALKRAGID---PN---------AIDAIFITHLHGDHFGGLPFFLLDAQFvakrtrplTIAGPPGLRERL 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080618509 100 K-----LFVKSNDSVKKFN-DFHVIDQNSEIDFGDAVVSFFQTTHSIPE-SIGIVIGTPEGNIVYTGD 160
Cdd:cd07740    96 RrameaLFPGSSKVPRRFDlEVIELEPGEPTTLGGVTVTAFPVVHPSGAlPLALRLEAAGRVLAYSGD 163
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 6-161 2.68e-03

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: 39.43  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   6 LVTLGGVRENGKNLYVAEVNDSIFVLDAGLKYPENEQLgvdvvipnMDYLFENKDRIAGVFLTHGHADAIGALPYLLAE- 84
Cdd:cd16293     1 FTPLSGAGDESPLCYLLEIDDVTILLDCGWDESFDMEY--------LESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  85 -AKVPVFGTELTIELAKLF----VKSNDSVKKFNDFHVIDqnseIDF-GDAV--VSFFQTTHSIPESIGIVI-------- 148
Cdd:cd16293    73 gLTCPVYATLPVHKMGRMFmydlYQSRGLEEDFNLFTLDD----VDEaFDRItqLKYSQPVNLRGKGDGLTItaynaght 148

                         170       180
                  ....*....|....*....|.
gi 1080618509 149 --GT------PEGNIVYTGDF 161
Cdd:cd16293   149 lgGTiwkitkDSEDIVYAVDW 169
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 59-100 3.67e-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: 39.19  E-value: 3.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1080618509  59 KDRIAGVFLTHGHADAIGALPYLLaEAKVPVFGTELTIELAK 100
Cdd:cd16304    61 KKPVTLAIVTHAHDDRIGGIKALQ-KRGIPVYSTKLTAQLAK 101
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 4-95 5.91e-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: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509   4 IKLVTLGGVRENgkNLYVAEVNDSIFVLDAGLKYPENEQLGVDvvipnmdYLFENK---DRIAGVFLTHGHADAIGALPY 80
Cdd:cd07725     4 LSLPLPGPLGHV--NVYLLRDGDETTLIDTGLATEEDAEALWE-------GLKELGlkpSDIDRVLLTHHHPDHIGLAGK 74

                          90
                  ....*....|....*
gi 1080618509  81 LLAEAKVPVFGTELT 95
Cdd:cd07725    75 LQEKSGATVYILDVT 89
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 60-162 8.43e-03

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: 37.24  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080618509  60 DRIAGVFLTHGHADAIGALPYLLAEAKVPVFGTELTIE--LAKLFVKSNDSVKKFNDFHVidqnseIDFGDAVVSFFQTT 137
Cdd:cd07733    44 EDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRamERKVGLIDVDQKQIFEPGET------FSIGDFDVESFGVS 117

                          90       100
                  ....*....|....*....|....*
gi 1080618509 138 HSIPESIGIVIGTPEGNIVYTGDFK 162
Cdd:cd07733   118 HDAADPVGYRFEEGGRRFGMLTDLK 142
 
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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