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Conserved domains on  [gi|1198283366|gb|OUM50900|]
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ribonuclease J [Bacillus pseudomycoides]

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];
7-556 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 939.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   7 DSVKVFALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYV 86
Cdd:COG0595     4 DKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  87 LRKLSIPVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFK 166
Cdd:COG0595    84 LKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDFK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 167 FDQTPIGNSGADLGKMAQIGNEGVLCLLSDSTNAERPGYTGSEKEVGIEISKVFYNAEGRIIVASFASNVHRIQQVFDAA 246
Cdd:COG0595   164 FDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDAA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 247 AETGRKVAVVGRSMVKVVDIARRLGYLDVPDGMVISLQEVDNFPEKKVAILTTGSQGEPMAALSRMAKQAHKQISIRKGD 326
Cdd:COG0595   244 KKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKPGD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 327 TVIIAASPIPGNEISVSKIIDLLFRAGAEVVYYGERKVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLAED 406
Cdd:COG0595   324 TVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLAEE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 407 VGVLKENIFIVEKGDVIAFEGEEAKQAGKVQAGNVLIDGLGVGDVGNIVLRDRKMLSQDGILVVVVTLGKDEKKIISGPE 486
Cdd:COG0595   404 MGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGGPD 483

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 487 IISRGFVYVRESEALIERSTDIVRTIVEQSIKEYSIEWSMLKQNIRELLGQFLYEETKRKPMILPIIMEV 556
Cdd:COG0595   484 IVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
7-556 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 939.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   7 DSVKVFALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYV 86
Cdd:COG0595     4 DKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  87 LRKLSIPVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFK 166
Cdd:COG0595    84 LKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDFK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 167 FDQTPIGNSGADLGKMAQIGNEGVLCLLSDSTNAERPGYTGSEKEVGIEISKVFYNAEGRIIVASFASNVHRIQQVFDAA 246
Cdd:COG0595   164 FDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDAA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 247 AETGRKVAVVGRSMVKVVDIARRLGYLDVPDGMVISLQEVDNFPEKKVAILTTGSQGEPMAALSRMAKQAHKQISIRKGD 326
Cdd:COG0595   244 KKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKPGD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 327 TVIIAASPIPGNEISVSKIIDLLFRAGAEVVYYGERKVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLAED 406
Cdd:COG0595   324 TVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLAEE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 407 VGVLKENIFIVEKGDVIAFEGEEAKQAGKVQAGNVLIDGLGVGDVGNIVLRDRKMLSQDGILVVVVTLGKDEKKIISGPE 486
Cdd:COG0595   404 MGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGGPD 483

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 487 IISRGFVYVRESEALIERSTDIVRTIVEQSIKEYSIEWSMLKQNIRELLGQFLYEETKRKPMILPIIMEV 556
Cdd:COG0595   484 IVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 9-430 0e+00

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 563.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   9 VKVFALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLR 88
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  89 KLSI-PVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFN-TTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFK 166
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 167 FDQTPIGNSGADLGKMAQIGNEGVLCLLSDSTNAERPGYTGSEKEVGIEISKVFYNAEGRIIVASFASNVHRIQQVFDAA 246
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 247 AETGRKVAVVGRSMVKVVDIARRLGYLDVPDGMVISLQEVDNFPEKKVAILTTGSQGEPMAALSRMAKQAHKQISIRKGD 326
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 327 TVIIAASPIPGNE-ISVSKIID-LLFRAGAEVVYygerKVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLA 404
Cdd:TIGR00649 321 TVVFSAPPIPGNEnIAVSITLDiRLNRAGARVIK----GIHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....*.
gi 1198283366 405 EDVGVLKENIFIVEKGDVIAFEGEEA 430
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 12-425 1.31e-118

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: 350.17  E-value: 1.31e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  12 FALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLS 91
Cdd:cd07714     1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  92 IPVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFKFDQTP 171
Cdd:cd07714    81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 172 IGNSGADLGKMAQIGNEGVLCLLSDStnaerpgytgsekevgieiskvfynaegriivasfasnvhriqqvfdaaaetgr 251
Cdd:cd07714   161 VDGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 252 kvavvgrsmvkvvdiarrlgyldvpdgmvislqevdnfpekkvailttgsqgepmaalsrmakqahkqisirkgdtviia 331
Cdd:cd07714       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 332 aspipgneisvskiidllfragaevvyygerkVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLAEDVGVLK 411
Cdd:cd07714   187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                         410
                  ....*....|....
gi 1198283366 412 ENIFIVEKGDVIAF 425
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 ...
 455-556 5.71e-44

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: 151.11  E-value: 5.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 455 VLRDRKMLSQDGILVVVVTLGKDEKKIISGPEIISRGFVYVRESEALIERSTDIVRTIVEQSIKEYSIEWSMLKQNIREL 534
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 1198283366 535 LGQFLYEETKRKPMILPIIMEV 556
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-168 2.44e-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: 91.46  E-value: 2.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   23 NMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPditylvenqERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKLTVG 102
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGP---------KKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198283366  103 LIQEKLGEAGMLGR-----VDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSvgVCFHTSQGAIVYTGDFKFD 168
Cdd:smart00849  72 LLKDLLALLGELGAeaepaPPDRTLKDGDELDLGGGELEVIHTPGHTPGS--IVLYLPEGKILFTGDLLFA 140
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
7-556 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 939.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   7 DSVKVFALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYV 86
Cdd:COG0595     4 DKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  87 LRKLSIPVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFK 166
Cdd:COG0595    84 LKELNVPVYGTPLTLALLEAKLKEHGLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGDFK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 167 FDQTPIGNSGADLGKMAQIGNEGVLCLLSDSTNAERPGYTGSEKEVGIEISKVFYNAEGRIIVASFASNVHRIQQVFDAA 246
Cdd:COG0595   164 FDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIIDAA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 247 AETGRKVAVVGRSMVKVVDIARRLGYLDVPDGMVISLQEVDNFPEKKVAILTTGSQGEPMAALSRMAKQAHKQISIRKGD 326
Cdd:COG0595   244 KKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKPGD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 327 TVIIAASPIPGNEISVSKIIDLLFRAGAEVVYYGERKVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLAED 406
Cdd:COG0595   324 TVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLAEE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 407 VGVLKENIFIVEKGDVIAFEGEEAKQAGKVQAGNVLIDGLGVGDVGNIVLRDRKMLSQDGILVVVVTLGKDEKKIISGPE 486
Cdd:COG0595   404 MGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGGPD 483

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 487 IISRGFVYVRESEALIERSTDIVRTIVEQSIKEYSIEWSMLKQNIRELLGQFLYEETKRKPMILPIIMEV 556
Cdd:COG0595   484 IVSRGFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 9-430 0e+00

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 563.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   9 VKVFALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLR 88
Cdd:TIGR00649   1 IKIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  89 KLSI-PVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFN-TTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFK 166
Cdd:TIGR00649  81 QVGFfPIYGTPLTIALIKSKIKEHGLNVRTDLLEIHEGEPVEFGeNTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 167 FDQTPIGNSGADLGKMAQIGNEGVLCLLSDSTNAERPGYTGSEKEVGIEISKVFYNAEGRIIVASFASNVHRIQQVFDAA 246
Cdd:TIGR00649 161 FDNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 247 AETGRKVAVVGRSMVKVVDIARRLGYLDVPDGMVISLQEVDNFPEKKVAILTTGSQGEPMAALSRMAKQAHKQISIRKGD 326
Cdd:TIGR00649 241 RKNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 327 TVIIAASPIPGNE-ISVSKIID-LLFRAGAEVVYygerKVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLA 404
Cdd:TIGR00649 321 TVVFSAPPIPGNEnIAVSITLDiRLNRAGARVIK----GIHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLA 396

                         410       420
                  ....*....|....*....|....*.
gi 1198283366 405 EDVGVLKENIFIVEKGDVIAFEGEEA 430
Cdd:TIGR00649 397 EEEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 12-425 1.31e-118

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: 350.17  E-value: 1.31e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  12 FALGGVGEIGKNMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLS 91
Cdd:cd07714     1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  92 IPVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFKFDQTP 171
Cdd:cd07714    81 VPIYATPLTLALIKKKLEEFKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQTP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 172 IGNSGADLGKMAQIGNEGVLCLLSDStnaerpgytgsekevgieiskvfynaegriivasfasnvhriqqvfdaaaetgr 251
Cdd:cd07714   161 VDGKPTDLEKLAELGKEGVLLLLSDS------------------------------------------------------ 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 252 kvavvgrsmvkvvdiarrlgyldvpdgmvislqevdnfpekkvailttgsqgepmaalsrmakqahkqisirkgdtviia 331
Cdd:cd07714       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 332 aspipgneisvskiidllfragaevvyygerkVHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHAYLAEDVGVLK 411
Cdd:cd07714   187 --------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIPE 234

                         410
                  ....*....|....
gi 1198283366 412 ENIFIVEKGDVIAF 425
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 ...
 455-556 5.71e-44

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: 151.11  E-value: 5.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 455 VLRDRKMLSQDGILVVVVTLGKDEKKIISGPEIISRGFVYVRESEALIERSTDIVRTIVEQSIKEYSIEWSMLKQNIREL 534
Cdd:pfam17770   1 VLRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRGFVYVRESEDLIEEAEEVVREALERADEKGIADWGALKEKIRRA 80

                          90       100
                  ....*....|....*....|..
gi 1198283366 535 LGQFLYEETKRKPMILPIIMEV 556
Cdd:pfam17770  81 LRRFLYEKTKRRPMILPIIMEV 102
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-168 2.44e-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: 91.46  E-value: 2.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   23 NMYCVEIDSEIFIVDAGLMFPGDEMFGIDIVIPditylvenqERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKLTVG 102
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGP---------KKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198283366  103 LIQEKLGEAGMLGR-----VDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSvgVCFHTSQGAIVYTGDFKFD 168
Cdd:smart00849  72 LLKDLLALLGELGAeaepaPPDRTLKDGDELDLGGGELEVIHTPGHTPGS--IVLYLPEGKILFTGDLLFA 140
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-167 3.61e-20

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: 88.82  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  15 GGVGEIGKNmyCVEI---DSEIFIvDAGLMFPGDEMFGIDI----------------VIPDITYLVENQER--VKGLFIT 73
Cdd:cd07732     6 RGTNEIGGN--CIEVetgGTRILL-DFGLPLDPESKYFDEVldflelgllpdivglyRDPLLLGGLRSEEDpsVDAVLLS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  74 HGHEDHIGGIVYVLRklSIPVYATKLTVGLIQEKLGEAGMLGRV--DLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVC 151
Cdd:cd07732    83 HAHLDHYGLLNYLRP--DIPVYMGEATKRILKALLPFFGEGDPVprNIRVFESGKSFTIGDFTVTPYLVDHSAPGAYAFL 160

                         170
                  ....*....|....*.
gi 1198283366 152 FHTSQGAIVYTGDFKF 167
Cdd:cd07732   161 IEAPGKRIFYTGDFRF 176
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 27-164 7.15e-19

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 86.49  E-value: 7.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  27 VEIDSEIFIVDAGlmfpgdemfgidiviPDITY----LVENQERVKGLFITHGHEDHIGGIVYVLRKL---SIPVYATKL 99
Cdd:COG1235    40 VEADGTRLLIDAG---------------PDLREqllrLGLDPSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPG 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1198283366 100 TVGLIQEKLG--EAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGD 164
Cdd:COG1235   105 TLEALERRFPylFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATD 171
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 9-393 8.44e-18

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 85.62  E-value: 8.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366   9 VKVFALGGVGEIGKNMYCVEIDSEIFIVDAGlMFPGDEM-----FGIDIvipditylvenqERVKGLFITHGHEDHIGGI 83
Cdd:COG1236     1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCG-LFQGGKErnwppFPFRP------------SDVDAVVLTHAHLDHSGAL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  84 -VYVLRKLSIPVYATKLTVGL----------IQEKLGEAGMLGRVD--------LKTIDSNSAVEFNTTTVSFFGTTHsI 144
Cdd:COG1236    68 pLLVKEGFRGPIYATPATADLarillgdsakIQEEEAEAEPLYTEEdaeralelFQTVDYGEPFEIGGVRVTFHPAGH-I 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 145 PDSVGVCFHTSQGAIVYTGDFKFDQTPIgNSGADLGKMAQIgnegvlcLLSDST--NAERPGYTGSEKEVGIEISKVFyN 222
Cdd:COG1236   147 LGSAQVELEVGGKRIVFSGDYGREDDPL-LAPPEPVPPADV-------LITESTygDRLHPPREEVEAELAEWVRETL-A 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 223 AEGRIIVASFAsnvhriqqvfdaaaetgrkvavVGRS--MVKVVDIARRLGYL-DVP---DGMVISLQEV-DNFPEK--- 292
Cdd:COG1236   218 RGGTVLIPAFA----------------------LGRAqeLLYLLRELKKEGRLpDIPiyvSGMAIRATEIyRRHGEYlrd 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 293 --------KVAILTTGSQgEPMAALsrmakqahkqisiRKGDTVIIAAS------PI----------PGNEISVS----- 343
Cdd:COG1236   276 eaqdpfalPNLRFVTSVE-ESKALN-------------RKGPAIIIAPSgmltggRIlhhlkrflwdPRNTILFVgyqae 341

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1198283366 344 -----KIIDllfraGAEVVYYGERKVHV----------SGHGSQEELKLMLNLMK-PKYFIPVHGE 393
Cdd:COG1236   342 gtlgrRLLR-----GAKEVKIFGEEVPVrarverlfglSAHADWDELLEWIKATGkPERVFLVHGE 402
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 14-172 1.26e-15

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 75.57  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  14 LGGVGEIGKNMYCVEIDSEIFIVDAGlMFPG--------DEMFGIDIvipditylvenqERVKGLFITHGHEDHIGGIVY 85
Cdd:cd16295     4 LGAAREVTGSCYLLETGGKRILLDCG-LFQGgkeleelnNEPFPFDP------------KEIDAVILTHAHLDHSGRLPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  86 VLRK-LSIPVYATKLTVGL----------IQEKlgEAGMLGRVDLKTIDSNSAVEFNTTTVSfFGTTHSIPDSVGVCFH- 153
Cdd:cd16295    71 LVKEgFRGPIYATPATKDLaelllldsakIQEE--EAEHPPAEPLYTEEDVEKALKHFRPVE-YGEPFEIGPGVKVTFYd 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1198283366 154 --------------TSQGAIVYTGDFKFDQTPI 172
Cdd:cd16295   148 aghilgsasveleiGGGKRILFSGDLGRKNTPL 180
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 16-167 7.35e-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: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  16 GVGEIGKNMYCVEIDS-EIFIVDAGlmfpgdeMFGIDIVIpdiTYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPV 94
Cdd:cd06262     4 PVGPLQTNCYLVSDEEgEAILIDPG-------AGALEKIL---EAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  95 YATKLTVGLIQEKLGEAGMLGRVDLK------TIDSNSAVEFNTTTVSFFGTT-HSiPDSvgVCFHTSQGAIVYTGDFKF 167
Cdd:cd06262    74 YIHEADAELLEDPELNLAFFGGGPLPppepdiLLEDGDTIELGGLELEVIHTPgHT-PGS--VCFYIEEEGVLFTGDTLF 150
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
25-164 1.74e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 70.22  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  25 YCVEIDSEIFIVDAG------LMFPGDEMFGIDIVipditylvenqervkglFITHGHEDHIGGIVYVL-------RKLS 91
Cdd:COG1234    22 YLLEAGGERLLIDCGegtqrqLLRAGLDPRDIDAI-----------------FITHLHGDHIAGLPGLLstrslagREKP 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198283366  92 IPVYATKLTVGLIQE--KLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPdSVGVCFHTSQGAIVYTGD 164
Cdd:COG1234    85 LTIYGPPGTKEFLEAllKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEEPGRSLVYSGD 158
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-182 1.28e-12

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: 67.02  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  23 NMYCVEIDSEIFIVDAGLMFPGDEMFgidivipdITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKLTVG 102
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 103 LIQEKlGEAGMLGRVDLK---TIDSNSAVEFNTTTVSFFGTT-HSiPDSvgVCFHTSQGAIVYTGD--FKFDQTPIGNSG 176
Cdd:COG0491    88 ALEAP-AAGALFGREPVPpdrTLEDGDTLELGGPGLEVIHTPgHT-PGH--VSFYVPDEKVLFTGDalFSGGVGRPDLPD 163


                  ....*.
gi 1198283366 177 ADLGKM 182
Cdd:COG0491   164 GDLAQW 169
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 30-164 5.59e-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: 66.08  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  30 DSEIFI-VDAG-----LMFpgDEMFGiDIVIPDITYLVENQERVKGLFITHGHEDHIGGIV------YVLRKLSIPVYAT 97
Cdd:cd07735    26 GSDGDIlLDAGtgvgaLSL--EEMFN-DILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPllspndGGQRGSPKTIYGL 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198283366  98 KLTVGLIQEKL-----------GEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGD 164
Cdd:cd07735   103 PETIDALKKHIfnwviwpdftsIPSGKYPYLRLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGD 180
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 354-417 3.29e-11

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: 58.79  E-value: 3.29e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198283366 354 AEVVYYGerkvHVSGHGSQEELKLMLNLMKPKYFIPVHGEFRMQKAHA-YLAEDVGVlkeNIFIV 417
Cdd:pfam07521   6 ARIETID----GFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAeLLKEELGI---EVFVP 63
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 27-167 3.34e-11

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: 62.49  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  27 VEIDSEIFIVDAGlmfpgdemfgidiviPDITY--LVENQERVKGLFITHGHEDHIGGI-----VYVLRKLSIPVYATKL 99
Cdd:cd16279    40 IETGGKNILIDTG---------------PDFRQqaLRAGIRKLDAVLLTHAHADHIHGLddlrpFNRLQQRPIPVYASEE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1198283366 100 TVGLIQEKLGEA------GMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFhtsqGAIVYTGDFKF 167
Cdd:cd16279   105 TLDDLKRRFPYFfaatggGGVPKLDLHIIEPDEPFTIGGLEITPLPVLHGKLPSLGFRF----GDFAYLTDVSE 174
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 11-166 3.77e-11

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: 61.51  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  11 VFALGGVGeigkNMYCVEIDSEIFIVDAGlmFPGDEMFG----IDIvipditylveNQERVKGLFITHGHEDHIGGIVYV 86
Cdd:cd07733     2 VLASGSKG----NCTYLETEDGKLLIDAG--LSGRKITGrlaeIGR----------DPEDIDAILVTHEHADHIKGLGVL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  87 LRKLSIPVYATKLTVGLIQEKLGEagmlgrVDLKTIDS---NSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTG 163
Cdd:cd07733    66 ARKYNVPIYATAGTLRAMERKVGL------IDVDQKQIfepGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLT 139


                  ...
gi 1198283366 164 DFK 166
Cdd:cd07733   140 DLK 142
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
10-164 5.99e-11

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 63.44  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  10 KVFALGGVGEIGKNM----YCVEIDSEIFI-VDAGLMFPG---DEMFGIDIVIPDitylvENQERVKGLFITHGHEDHIG 81
Cdd:COG5212    13 EVRVLGCSGGISDGNlttyLLRPLGSDDYVlLDAGTVVSGlelAEQKGAFKGRQG-----YVLEHIKGYLISHAHLDHIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  82 GIVYVLRKLS-IPVYATKLTVGLIQE------------KLGEAGMLGRVDLKTIDSNSAVEFNTT--TVSFFGTTHSIPd 146
Cdd:COG5212    88 GLPILSPDDSpKTIYALPETIDALRNhyfnwviwpdftDIGSAPHLPKYRYVPLKPGQTFPLGGTglRVTAFPLSHSVP- 166

                         170
                  ....*....|....*...
gi 1198283366 147 SVGVCFHTSQGAIVYTGD 164
Cdd:COG5212   167 SSAFLIESGGGAFLYSGD 184
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-167 5.69e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.92  E-value: 5.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  23 NMYCVEIDSEIFIVDAGlmfpgdeMFGIDIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYA------ 96
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTG-------GSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVvaeear 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198283366  97 --TKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIPDSVGVCFHTSQGAIVYTGDFKF 167
Cdd:pfam00753  80 elLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLF 152
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 14-170 3.99e-09

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 56.57  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  14 LGGVGEIGKNMYCVEIDSEIFIVDAGlMFPGDEMFGIDI-----VIPDITYLVenqervkglfITHGHEDHIGGIVYVLR 88
Cdd:cd07734     3 LGGGQEVGRSCFLVEFKGRTVLLDCG-MNPGKEDPEACLpqfelLPPEIDAIL----------ISHFHLDHCGALPYLFR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  89 --KLSIPVYATKLTVGL-----------IQEKLGEAGMLGRVDL-KTIDSNSAVEFNTT-------TVSFFGTTHsIPDS 147
Cdd:cd07734    72 gfIFRGPIYATHPTVALgrllledyvksAERIGQDQSLYTPEDIeEALKHIVPLGYGQSidlfpalSLTAYNAGH-VLGA 150

                         170       180
                  ....*....|....*....|...
gi 1198283366 148 VGVCFHTSQGAIVYTGDFKFDQT 170
Cdd:cd07734   151 AMWEIQIYGEKLVYTGDFSNTED 173
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 23-105 3.82e-08

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: 53.76  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  23 NMYCVEIDSEIFIVDAGLMFPGDEMfgidivipdITYLVE---NQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKL 99
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGLPGSAKRI---------LKALRElglSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHER 82


                  ....*.
gi 1198283366 100 TVGLIQ 105
Cdd:cd07721    83 EAPYLE 88
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 65-164 6.04e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 52.44  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  65 ERVKGLFITHGHEDHI---GGIVYVLR-------KLSIPVYATKLTvgliQEKLGEA-GMLGRVDLKTIDSNSAVEFNTT 133
Cdd:cd07716    49 EDLDAVVLSHLHPDHCadlGVLQYARRyhprgarKPPLPLYGPAGP----AERLAALyGLEDVFDFHPIEPGEPLEIGPF 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1198283366 134 TVSFFGTTHSIPdSVGVCFHTSQGAIVYTGD 164
Cdd:cd07716   125 TITFFRTVHPVP-CYAMRIEDGGKVLVYTGD 154
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 25-179 6.62e-08

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: 52.65  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  25 YCVEIDSEIFIVDAGlmfPG--DEMFGIDIVIPDITYLvenqervkglFITHGHEDHIGGIVYVLRKLSIPVYATKLTV- 101
Cdd:cd16272    20 YLLETGGTRILLDCG---EGtvYRLLKAGVDPDKLDAI----------FLSHFHLDHIGGLPTLLFARRYGGRKKPLTIy 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366 102 ----------GLIQEKLGEAGMLGRVDLKTIDSNSAV-EFNTTTVSFFGTTHSIPdSVGVCFHTSQGAIVYTGDFKFDQT 170
Cdd:cd16272    87 gpkgikefleKLLNFPVEILPLGFPLEIEELEEGGEVlELGDLKVEAFPVKHSVE-SLGYRIEAEGKSIVYSGDTGPCEN 165

                         170
                  ....*....|
gi 1198283366 171 PI-GNSGADL 179
Cdd:cd16272   166 LVeLAKGADL 175
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 65-170 1.06e-06

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: 48.67  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  65 ERVKGLFITHGHEDHIGGIVyvlRKLSIPVYATKLTVGLIQEKLgeagmlgRVDLKTIDS---NSAVEFNTTTVSFFGTT 141
Cdd:cd16298    35 EGCTAYFLTHFHSDHYCGLT---KKFKFPIYCSKITGNLVKSKL-------KVEEQYINVlpmNTECIVNGVKVVLLDAN 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 1198283366 142 HSiPDSVGVCFHTSQG-AIVYTGDFKFDQT 170
Cdd:cd16298   105 HC-PGAVMILFRLPSGtLVLHTGDFRADPS 133
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 35-92 1.20e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 49.05  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1198283366  35 IVDAGlmfpGDEMFGIDIVIPditYLVE-NQERVKGLFITHGHEDHIGGIVYVLRKLSI 92
Cdd:cd07731    23 LIDTG----PRDSFGEDVVVP---YLKArGIKKLDYLILTHPDADHIGGLDAVLKNFPV 74
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 30-164 1.89e-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: 49.47  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  30 DSEIFIVDAGLMFPGDemFGIDIVIPditYLVENQ-ERVKGLFITHGHEDHIGGIVYVLRKLSI------PVYATKLTVG 102
Cdd:COG2333    20 DGKTILIDTGPRPSFD--AGERVVLP---YLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVgrvlvsGPPDTSETYE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198283366 103 LIQEKLGEAGmlgrVDLKTIDSNSAVEFNTTTVSFFGTTHSIP-------DSVGVCFHTSQGAIVYTGD 164
Cdd:COG2333    95 RLLEALKEKG----IPVRPCRAGDTWQLGGVRFEVLWPPEDLLegsdennNSLVLRLTYGGFSFLLTGD 159
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-115 1.92e-06

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 48.68  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  30 DSEIFIVDAGLmfpgDEMFGIDIvipdITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKLTVGLIQEKLG 109
Cdd:cd07743    17 DKEALLIDSGL----DEDAGRKI----RKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPLL 88


                  ....*.
gi 1198283366 110 EAGMLG 115
Cdd:cd07743    89 EPSYLG 94
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 24-164 3.01e-06

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: 47.45  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  24 MYCV--EIDSEIFIVDaglmfPGDEmfgiDIVIpdiTYLVENQERVKGLFITHGHEDHIGGIVYVLRKL-SIPVYAtklt 100
Cdd:cd07723    11 IYLIvdEATGEAAVVD-----PGEA----EPVL---AALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYG---- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1198283366 101 vgliqeklGEAGMLGRVDlKTIDSNSAVEFNTTTVSFFGT---ThsiPDSvgVCFHTSQGAIVYTGD 164
Cdd:cd07723    75 --------PAEDRIPGLD-HPVKDGDEIKLGGLEVKVLHTpghT---LGH--ICYYVPDEPALFTGD 127
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 17-185 8.71e-06

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 46.96  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  17 VGEIGKNMYCV--EIDSEIFIVDaglmfPGDEMFGIdivipdITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPV 94
Cdd:cd16322     6 LGPLQENTYLVadEGGGEAVLVD-----PGDESEKL------LARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  95 YATKLTVGLI-----QEKLGEAGM--LGRVDLKtIDSNSAVEFNTTTVSFFGTT-HSiPDSvgVCFHTSQGAIVYTGDFK 166
Cdd:cd16322    75 YLHPDDLPLYeaadlGAKAFGLGIepLPPPDRL-LEDGQTLTLGGLEFKVLHTPgHS-PGH--VCFYVEEEGLLFSGDLL 150

                         170       180
                  ....*....|....*....|..
gi 1198283366 167 FdQTPIGNS---GADLGKMAQI 185
Cdd:cd16322   151 F-QGSIGRTdlpGGDPKAMAAS 171
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 66-179 1.11e-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: 46.51  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  66 RVKGLFITHGHEDHIGGIVYvLRKLSIPVYATKLTVGLIQEKLGEagmlgrVDLKTIDSNSAVEFNTTTVSFFGTTHSiP 145
Cdd:cd16285    63 PVTAAISTHSHDDRTGGIKA-LNARGIPTYATALTNELAKKEGKP------VPTHSLKGALTLGFGPLEVFYPGPGHT-P 134

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1198283366 146 DSVGVCFHTSQ----GAIVYTGdfkfDQTPIGN-SGADL 179
Cdd:cd16285   135 DNIVVWLPKSKilfgGCLVKSA----SATSLGNvGDADV 169
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 64-106 3.81e-05

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 44.97  E-value: 3.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1198283366  64 QERVKGLFITHGHEDHIGGIVyVLRKLSIPVYATKLTVGLIQE 106
Cdd:cd16304    61 KKPVTLAIVTHAHDDRIGGIK-ALQKRGIPVYSTKLTAQLAKK 102
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 54-168 4.85e-05

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293831  Cd Length: 160  Bit Score: 43.68  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  54 IPDITYLV-----ENQERVKGLFITHGHEDHIGGivyvLRK--LSIPVYATKLTVGLIQEKLGeagmlgrVD---LKTID 123
Cdd:cd16273    19 IPGTSFVVdafkyGKIPGISAYFLSHFHSDHYGG----LTKswSHGPIYCSEITANLVKLKLK-------VDeeyIVVLP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1198283366 124 SNSAVEF-NTTTVSFFGTTHSiPDSVGVCFHTSQGA-IVYTGDFKFD 168
Cdd:cd16273    88 MNTPVEIdGDVSVTLLDANHC-PGAVMFLFELPDGRrILHTGDFRAN 133
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 58-168 9.32e-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: 43.44  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  58 TYLVEN---QERVKGLFITHGHEDHIGGIVY-VLRKLSIPVYATKLTVGLIQEKLG-----EAGMLGR-VDLKTIDSNSA 127
Cdd:cd07738    37 SYLRQNgisPRLVDHVILTHCHADHDAGTFQkILEEEKITLYTTRTINESFLRKYAaltglPPDFLEElFDFRPVIIGEK 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1198283366 128 VEFNTTTVSFFGTTHSIPdSVGVCFHTSQGAIVYTGDFKFD 168
Cdd:cd07738   117 TKINGAEFEFDYSFHSIP-TIRFKVSYGGKSIAYSGDTRYD 156
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 57-98 9.35e-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: 43.29  E-value: 9.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1198283366  57 ITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATK 98
Cdd:cd16275    38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSK 79
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 27-164 1.04e-04

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: 43.27  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  27 VEIDSEIFIVDAGlmfPG-----DEMfGIDIvipditylvenqERVKGLFITHGHEDHIGGIVYVL-------RKLSIPV 94
Cdd:cd07719    23 VVVGGRVYLVDAG---SGvvrrlAQA-GLPL------------GDLDAVFLTHLHSDHVADLPALLltawlagRKTPLPV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  95 Y----ATKLTVGL---------IQEKLGEAGMLG---RVDLKTIDSNSAV-EFNTTTVSFFGTTHS-IPDSVGVCFHTSQ 156
Cdd:cd07719    87 YgppgTRALVDGLlaayaldidYRARIGDEGRPDpgaLVEVHEIAAGGVVyEDDGVKVTAFLVDHGpVPPALAYRFDTPG 166


                  ....*...
gi 1198283366 157 GAIVYTGD 164
Cdd:cd07719   167 RSVVFSGD 174
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 65-164 1.50e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 43.07  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  65 ERVKGLFITHGHEDHIGGIVyVLRKLSI-PVYATKLTVGLIQEKLGEAGML--GRVDLKTIDSNSAVEFNTTTVSFFGTT 141
Cdd:pfam12706  27 DPIDAVLLTHDHYDHLAGLL-DLREGRPrPLYAPLGVLAHLRRNFPYLFLLehYGVRVHEIDWGESFTVGDGGLTVTATP 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1198283366 142 --HSIP--------DSVGVCFHTSQGAIVYTGD 164
Cdd:pfam12706 106 arHGSPrgldpnpgDTLGFRIEGPGKRVYYAGD 138
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
30-96 1.67e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 43.72  E-value: 1.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198283366  30 DSEIFIVDAGLMfpgdemfGIDIvipditylvenqERVKGLFITHGHEDHIGGIVYVLRKLS-IPVYA 96
Cdd:COG1237    40 QSDVLLKNAEKL-------GIDL------------SDIDAVVLSHGHYDHTGGLPALLELNPkAPVYA 88
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 12-123 2.81e-04

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: 41.90  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  12 FALGGVgeigkNMYCVEIDSEIFIVDAGLMFPGD------EMFGIDIVIPDITYLvenqervkglFITHGHEDHIGGIVY 85
Cdd:cd07725    10 GPLGHV-----NVYLLRDGDETTLIDTGLATEEDaealweGLKELGLKPSDIDRV----------LLTHHHPDHIGLAGK 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1198283366  86 VLRKLSIPVYAtkLTVGLIqeKLGEAGMLGRVDLKTID 123
Cdd:cd07725    75 LQEKSGATVYI--LDVTPV--KDGDKIDLGGLRLKVIE 108
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 57-107 2.87e-04

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 42.27  E-value: 2.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1198283366  57 ITYLVENQERVKGLFITHGHEDHIGGIVYvLRKLSIPVYATKLTVGLIQEK 107
Cdd:cd16301    56 VEWIKAQGLTLKASISTHFHEDRTGGIGY-LNSHSIPTYASELTNQLLKKN 105
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 26-164 5.21e-04

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


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 41.71  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  26 CVEI--DSEIFIVDAG---------LMfpgDEMFGIDIVIpditylvenqervkglFITHGHEDHIGGI-----VYVlRK 89
Cdd:cd07715    25 CVEVraGGELLILDAGtgirelgneLM---KEGPPGEAHL----------------LLSHTHWDHIQGFpffapAYD-PG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  90 LSIPVYATKLTVGLIQEKLGE-----------AGMLGRVDLKTIDSNSAVEFNTTTVSFFGTTHsiPD-SVGVCFHTSQG 157
Cdd:cd07715    85 NRIHIYGPHKDGGSLEEVLRRqmsppyfpvplEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNH--PGgALGYRIEEDGK 162


                  ....*..
gi 1198283366 158 AIVYTGD 164
Cdd:cd07715   163 SVVYATD 169
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-98 6.21e-04

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 41.80  E-value: 6.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1198283366  51 DIVIPDITYLVENQERVKGLFITHGHEDHIGGIVYVLRKLSIPVYATK 98
Cdd:cd16280    46 DLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSE 93
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 65-96 6.82e-04

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 41.84  E-value: 6.82e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1198283366  65 ERVKGLFITHGHEDHIGGIVYVLRKLS-IPVYA 96
Cdd:cd07713    54 SDIDAVVLSHGHYDHTGGLKALLELNPkAPVYA 86
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 27-164 1.55e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.29  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  27 VEIDSEIFIVDAGLMFPGDEMFGIDIVIPDItylvenqERVKGLFITHGHEDHIGG-IVYVLRKLSIPVYATKLTVGLIQ 105
Cdd:COG2220    16 IETGGKRILIDPVFSGRASPVNPLPLDPEDL-------PKIDAVLVTHDHYDHLDDaTLRALKRTGATVVAPLGVAAWLR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1198283366 106 EKlgeagmlGRVDLKTIDSNSAVEFNTTTVSFFGTTHSIP-------DSVGVCFHTSQGAIVYTGD 164
Cdd:COG2220    89 AW-------GFPRVTELDWGESVELGGLTVTAVPARHSSGrpdrnggLWVGFVIETDGKTIYHAGD 147
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 66-107 2.28e-03

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 39.54  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1198283366  66 RVKGLFITHGHEDHIGGIVYvLRKLSIPVYATKLTVGLIQEK 107
Cdd:cd16302    64 KVKAVVPTHFHDDCLGGLKA-FHRRGIPSYANQKTIALAKEK 104
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 62-95 2.37e-03

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.44  E-value: 2.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1198283366  62 ENQERVKGLFITHGHEDHIGGIVYVLRKL---SIPVY 95
Cdd:cd07722    52 EGNATISDILLTHWHHDHVGGLPDVLDLLrgpSPRVY 88
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 35-95 3.00e-03

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 39.07  E-value: 3.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198283366  35 IVDAGlmfpGDemfgidivIPDITYLVENQE-RVKGLFITHGHEDHIGGIVYVLRKLSIPVY 95
Cdd:cd07737    26 VIDPG----GD--------ADKILQAIEDLGlTLKKILLTHGHLDHVGGAAELAEHYGVPII 75
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 63-152 3.79e-03

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: 38.96  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  63 NQErVKGLFITHGHEDHIGGIVYvLRKLSIPVYATKLTVGLIQEKlGEAgmlgrVDLKTIDSNSAVEFNTT--TVSFFGT 140
Cdd:cd16299    61 NLP-VIAVIATHSHEDRAGGLGY-FNKIGIPTYATAMTNSILKKE-NKP-----QATYLIETDKTYKIGGEkfVVYFFGE 132

                          90
                  ....*....|..
gi 1198283366 141 THSIpDSVGVCF 152
Cdd:cd16299   133 GHTA-DNVVVWF 143
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 66-164 4.26e-03

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 38.97  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  66 RVKGLFITHGHEDHIGGIVYVLRKLSIPVYATKLTV----GLIQ-----EKLGEAGMLGRVDLKTIDSNSAVEFNTT--T 134
Cdd:cd07717    50 KIDRIFITHLHGDHILGLPGLLSTMSLLGRTEPLTIygpkGLKEfletlLRLSASRLPYPIEVHELEPDPGLVFEDDgfT 129

                          90       100       110
                  ....*....|....*....|....*....|
gi 1198283366 135 VSFFGTTHSIPdSVGVCFHTSQgAIVYTGD 164
Cdd:cd07717   130 VTAFPLDHRVP-CFGYRFEEGR-KIAYLGD 157
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 28-152 4.34e-03

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: 39.06  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  28 EIDSEIFIVDAGLMFPGDEMFGID---IVIPDITY-------LVENQERVKGL-----FITHGHEDHIGGIVYvLRKLSI 92
Cdd:cd07707     5 QINGPVWVVTDLGSVPSNGLVYNGskgLVLVDSTWtpkttkeLIKEIEKVSQKpvtevINTHFHTDRAGGNAY-LKERGA 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198283366  93 PVYATKLTVGLIQEKLGEAGMLGRVDLKTIDSNSAVE------------FNTTTVSFFGTTHSiPDSVGVCF 152
Cdd:cd07707    84 KTVSTALTRDLAKSEWAEIVAFTRKGLPEYPDLGYELpdgvldgdfnlqFGKVEAFYPGPAHT-PDNIVVYF 154
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 27-164 6.94e-03

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 37.99  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198283366  27 VEIDSEIFIVDAGLMFPGDEMFGIDIvipditylvenqervKGLFITHGHEDHIGGIvYVLRK---LSIPVYATKltvgl 103
Cdd:cd07736    42 IEVDGERILLDAGLTDLAERFPPGSI---------------DAILLTHFHMDHVQGL-FHLRWgvgDPIPVYGPP----- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198283366 104 iqEKLGEAGML---GRVDLKTI----DSNSAVEFNTTTVSFFgttHSIPdSVGVCFHTSQGAIVYTGD 164
Cdd:cd07736   101 --DPQGCADLFkhpGILDFQPLvapfQSFELGGLKITPLPLN---HSKP-TFGYLLESGGKRLAYLTD 162
 
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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