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Conserved domains on  [gi|505262897|ref|WP_015449999|]
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MULTISPECIES: ribonuclease J [Bifidobacterium]

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];
63-609 0e+00

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


:

Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 821.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  63 KGSMRIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPY 142
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 143 LLKlRPDIPLIGSKLTLAFVEAKCKEHHIN--PTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLIDTGD 220
Cdd:COG0595   83 LLK-ELNVPVYGTPLTLALLEAKLKEHGLLkkVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 221 IKLDQLPLDHKITDLVEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGPVLDRVFAEATRKIIVASFSSHVHRVQQVVD 300
Cdd:COG0595  162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 301 AAHKYGRKVVFVGRSMVRNMSIAADLGYLHIPEGTVVDLKKAKDIQDDKIVYMCTGSQGEPMAALGRIADGNHRDITVNE 380
Cdd:COG0595  242 AAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 381 FDTVILASSLIPGNENGVYRVINKLVQLGARVVNKDNAAVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIA 460
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 461 VKTGVAPDNVVLAEDGDVVDLYHGKAAVVGSVPCGYVYVDGDSVGELTDEDLEKRRILGTEGFVSSFVVVNTDTADVLSG 540
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262897 541 PKIY---LNAVAEDESEFEKVRHQIVEQLQDAMMQGTRDTHKLQQIMRRTLGSWVARQLHRKPVIVPVVADI 609
Cdd:COG0595  482 PDIVsrgFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
63-609 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 821.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  63 KGSMRIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPY 142
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 143 LLKlRPDIPLIGSKLTLAFVEAKCKEHHIN--PTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLIDTGD 220
Cdd:COG0595   83 LLK-ELNVPVYGTPLTLALLEAKLKEHGLLkkVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 221 IKLDQLPLDHKITDLVEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGPVLDRVFAEATRKIIVASFSSHVHRVQQVVD 300
Cdd:COG0595  162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 301 AAHKYGRKVVFVGRSMVRNMSIAADLGYLHIPEGTVVDLKKAKDIQDDKIVYMCTGSQGEPMAALGRIADGNHRDITVNE 380
Cdd:COG0595  242 AAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 381 FDTVILASSLIPGNENGVYRVINKLVQLGARVVNKDNAAVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIA 460
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 461 VKTGVAPDNVVLAEDGDVVDLYHGKAAVVGSVPCGYVYVDGDSVGELTDEDLEKRRILGTEGFVSSFVVVNTDTADVLSG 540
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262897 541 PKIY---LNAVAEDESEFEKVRHQIVEQLQDAMMQGTRDTHKLQQIMRRTLGSWVARQLHRKPVIVPVVADI 609
Cdd:COG0595  482 PDIVsrgFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 67-486 3.32e-139

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: 411.75  E-value: 3.32e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   67 RIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKL 146
Cdd:TIGR00649   2 KIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLHQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  147 RPDIPLIGSKLTLAFVEAKCKEHHIN--PTMIEVKGRDKIKAGP-FNLEFVTVTHSIPDALAVCVRTPAGSLIDTGDIKL 223
Cdd:TIGR00649  82 VGFFPIYGTPLTIALIKSKIKEHGLNvrTDLLEIHEGEPVEFGEnTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  224 DQLPLDHKITDLVEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGPVLDRVFAEATRKIIVASFSSHVHRVQQVVDAAH 303
Cdd:TIGR00649 162 DNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIAR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  304 KYGRKVVFVGRSMVRNMSIAADLGYLHIPEGTVVDLKKAKDIQDDKIVYMCTGSQGEPMAALGRIADGNHRDITVNEFDT 383
Cdd:TIGR00649 242 KNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGDT 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  384 VILASSLIPGNENGVYRVI--NKLVQLGARVVNKdnaaVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIAV 461
Cdd:TIGR00649 322 VVFSAPPIPGNENIAVSITldIRLNRAGARVIKG----IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAE 397

                         410       420
                  ....*....|....*....|....*
gi 505262897  462 KTGVAPDNVVLAEDGDVVDLYHGKA 486
Cdd:TIGR00649 398 EEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 69-481 1.65e-95

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 293.16  E-value: 1.65e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  69 VPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRp 148
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPEL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 149 DIPLIGSKLTLAFVEAKCKEHHI--NPTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLIDTGDIKLDQL 226
Cdd:cd07714   80 NVPIYATPLTLALIKKKLEEFKLikKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 227 PLDHKITDLVEFGKLGERGIDLLMMDStnaevpgfvrpettigpvldrvfaeatrkiivasfsshvhrvqqvvdaahkyg 306
Cdd:cd07714  160 PVDGKPTDLEKLAELGKEGVLLLLSDS----------------------------------------------------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 307 rkvvfvgrsmvrnmsiaadlgylhipegtvvdlkkakdiqddkivymctgsqgepmaalgriadgnhrditvnefdtvil 386
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 387 asslipgnengvyrvinklvqlgarvvnkdnaaVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIAVKTGVA 466
Cdd:cd07714  187 ---------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIP 233

                        410
                 ....*....|....*
gi 505262897 467 PDNVVLAEDGDVVDL 481
Cdd:cd07714  234 EENIFLLENGDVLEL 248
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-270 1.01e-19

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: 86.84  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897    80 NMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDfhyikdrldKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTL 159
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---------KIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   160 AFVEAKCKEH-------HINPTMIEVKGRDKIKAGPFNLEFVTVTHSIPDalAVCVRTPAGSLIDTGDIKLDQlpldhki 232
Cdd:smart00849  71 ELLKDLLALLgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPG--SIVLYLPEGKILFTGDLLFAG------- 141

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 505262897   233 tdlvEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGP 270
Cdd:smart00849 142 ----GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 512-609 8.76e-16

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: 73.30  E-value: 8.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  512 LEKRRILGTEGFVSSFVVVNTDTADVLSGPKIYLN-AVAEDESE--FEKVRHQIVEQLQDAMMQGTRDTHKLQQIMRRTL 588
Cdd:pfam17770   2 LRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRgFVYVRESEdlIEEAEEVVREALERADEKGIADWGALKEKIRRAL 81

                          90       100
                  ....*....|....*....|.
gi 505262897  589 GSWVARQLHRKPVIVPVVADI 609
Cdd:pfam17770  82 RRFLYEKTKRRPMILPIIMEV 102
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
121-194 3.61e-05

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 46.61  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262897 121 LDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKLTLAFVEakcKEHHINPTMIEVKGRDKIKAGPFNLEFV 194
Cdd:PRK11921  67 LDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCTKNGAKSLK---GHYHQDWNFVVVKTGDRLEIGSNELIFI 137
 
Name Accession Description Interval E-value
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
63-609 0e+00

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 821.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  63 KGSMRIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPY 142
Cdd:COG0595    3 KDKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLKFPEDEMPGVDLVIPDISYLEENKDKIKGIVLTHGHEDHIGALPY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 143 LLKlRPDIPLIGSKLTLAFVEAKCKEHHIN--PTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLIDTGD 220
Cdd:COG0595   83 LLK-ELNVPVYGTPLTLALLEAKLKEHGLLkkVKLHVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIRTPAGTIVHTGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 221 IKLDQLPLDHKITDLVEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGPVLDRVFAEATRKIIVASFSSHVHRVQQVVD 300
Cdd:COG0595  162 FKFDQTPVDGEPTDLARLAELGEEGVLALLSDSTNAERPGFTPSEREVGPTLEEIFAKAKGRIIVATFASNVHRIQQIID 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 301 AAHKYGRKVVFVGRSMVRNMSIAADLGYLHIPEGTVVDLKKAKDIQDDKIVYMCTGSQGEPMAALGRIADGNHRDITVNE 380
Cdd:COG0595  242 AAKKHGRKVALVGRSMERNVEIARELGYLKIPDGLLIDLKEINKLPDEKVVILCTGSQGEPMAALSRMANGEHRQIKIKP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 381 FDTVILASSLIPGNENGVYRVINKLVQLGARVVNKDNAAVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIA 460
Cdd:COG0595  322 GDTVIFSSSPIPGNEKAVARVINELYRLGAEVIYDSDAKVHVSGHASQEELKLMLNLVKPKYFIPVHGEYRHLVAHAKLA 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 461 VKTGVAPDNVVLAEDGDVVDLYHGKAAVVGSVPCGYVYVDGDSVGELTDEDLEKRRILGTEGFVSSFVVVNTDTADVLSG 540
Cdd:COG0595  402 EEMGVPEENIFIAENGDVVELTPGKARIVGKVPAGRVYVDGLGVGDVGNIVLRDRRRLSEDGIVIVVVTIDKKTGKLVGG 481

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262897 541 PKIY---LNAVAEDESEFEKVRHQIVEQLQDAMMQGTRDTHKLQQIMRRTLGSWVARQLHRKPVIVPVVADI 609
Cdd:COG0595  482 PDIVsrgFVYVRESEELLEEAEELVEKALEKALEKKRRDWDALKEAIRRALRRFLYEKTGRRPMILPVIMEV 553
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 67-486 3.32e-139

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: 411.75  E-value: 3.32e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   67 RIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKL 146
Cdd:TIGR00649   2 KIFALGGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLGVDGVIPDFTYLQENEDKVKGIFITHGHEDHIGAVPYLLHQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  147 RPDIPLIGSKLTLAFVEAKCKEHHIN--PTMIEVKGRDKIKAGP-FNLEFVTVTHSIPDALAVCVRTPAGSLIDTGDIKL 223
Cdd:TIGR00649  82 VGFFPIYGTPLTIALIKSKIKEHGLNvrTDLLEIHEGEPVEFGEnTAIEFFRITHSIPDSVGFALHTPLGYIVYTGDFKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  224 DQLPLDHKITDLVEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGPVLDRVFAEATRKIIVASFSSHVHRVQQVVDAAH 303
Cdd:TIGR00649 162 DNTPVIGEPPDLNRIAEIGKKGVLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNADGRIIVATFASNIHRVQQLIQIAR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  304 KYGRKVVFVGRSMVRNMSIAADLGYLHIPEGTVVDLKKAKDIQDDKIVYMCTGSQGEPMAALGRIADGNHRDITVNEFDT 383
Cdd:TIGR00649 242 KNGRKVAVYGRSMESLIGIARRLGYIKCPHNNFISLKEINNSPDENYLIITTGSQGEPMAALTRIANGEHRQIRIRPGDT 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  384 VILASSLIPGNENGVYRVI--NKLVQLGARVVNKdnaaVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIAV 461
Cdd:TIGR00649 322 VVFSAPPIPGNENIAVSITldIRLNRAGARVIKG----IHVSGHASQEDHKLMLRLLKPKYIIPVHGEYRMLKNHTKLAE 397

                         410       420
                  ....*....|....*....|....*
gi 505262897  462 KTGVAPDNVVLAEDGDVVDLYHGKA 486
Cdd:TIGR00649 398 EEGYPGENIFILRNGEVLEINGDEI 422
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 69-481 1.65e-95

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 293.16  E-value: 1.65e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  69 VPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRp 148
Cdd:cd07714    1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGVDYIIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPEL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 149 DIPLIGSKLTLAFVEAKCKEHHI--NPTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLIDTGDIKLDQL 226
Cdd:cd07714   80 NVPIYATPLTLALIKKKLEEFKLikKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIKTPEGTIVHTGDFKFDQT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 227 PLDHKITDLVEFGKLGERGIDLLMMDStnaevpgfvrpettigpvldrvfaeatrkiivasfsshvhrvqqvvdaahkyg 306
Cdd:cd07714  160 PVDGKPTDLEKLAELGKEGVLLLLSDS----------------------------------------------------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 307 rkvvfvgrsmvrnmsiaadlgylhipegtvvdlkkakdiqddkivymctgsqgepmaalgriadgnhrditvnefdtvil 386
Cdd:cd07714      --------------------------------------------------------------------------------

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 387 asslipgnengvyrvinklvqlgarvvnkdnaaVHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVANGLIAVKTGVA 466
Cdd:cd07714  187 ---------------------------------VHVSGHASQEDLKLMINLLKPKYFIPVHGEYRHLVAHAKLAEELGIP 233

                        410
                 ....*....|....*
gi 505262897 467 PDNVVLAEDGDVVDL 481
Cdd:cd07714  234 EENIFLLENGDVLEL 248
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 67-251 4.04e-22

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: 94.60  E-value: 4.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  67 RIVPLGGLGEIGRNMNVVEYNGHLLLIDCG-------VLFPEEEQPGVDLILPDF-----------HYIKDRLDKVEALV 128
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGlpldpesKYFDEVLDFLELGLLPDIvglyrdplllgGLRSEEDPSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 129 LTHGHEDHIGGVPYLlklRPDIPLIGSKLTLAFVEA--KCKEHHINPT--MIEVKGRDKIKAGPFNLEFVTVTHSIPDAL 204
Cdd:cd07732   81 LSHAHLDHYGLLNYL---RPDIPVYMGEATKRILKAllPFFGEGDPVPrnIRVFESGKSFTIGDFTVTPYLVDHSAPGAY 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505262897 205 AVCVRTPAGSLIDTGDIKLdqlpldH----KIT-DLVEFGKlgeRGIDLLMM 251
Cdd:cd07732  158 AFLIEAPGKRIFYTGDFRF------HgrkpELTeAFVEKAP---KNIDVLLM 200
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-270 1.01e-19

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: 86.84  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897    80 NMNVVEYNGHLLLIDCGVLFPEEEQPGVDLILPDfhyikdrldKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTL 159
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---------KIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   160 AFVEAKCKEH-------HINPTMIEVKGRDKIKAGPFNLEFVTVTHSIPDalAVCVRTPAGSLIDTGDIKLDQlpldhki 232
Cdd:smart00849  71 ELLKDLLALLgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPG--SIVLYLPEGKILFTGDLLFAG------- 141

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 505262897   233 tdlvEFGKLGERGIDLLMMDSTNAEVPGFVRPETTIGP 270
Cdd:smart00849 142 ----GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
66-257 3.65e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.17  E-value: 3.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  66 MRIVPLG---GLGEIGRNMN--VVEYNGHLLLIDCGvlfpeeeqPGVDLILPDFhyiKDRLDKVEALVLTHGHEDHIGGV 140
Cdd:COG1234    1 MKLTFLGtggAVPTPGRATSsyLLEAGGERLLIDCG--------EGTQRQLLRA---GLDPRDIDAIFITHLHGDHIAGL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 141 PYLLKLR------PDIPLIGSKLTLAFVEAKCKEHHINPTM----IEVKGRDKIKAGPFNLEFVTVTHSIPdALAVCVRT 210
Cdd:COG1234   70 PGLLSTRslagreKPLTIYGPPGTKEFLEALLKASGTDLDFplefHEIEPGEVFEIGGFTVTAFPLDHPVP-AYGYRFEE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505262897 211 PAGSLIDTGDIKLDQlpldhkitDLVEFGklgeRGIDLLMMDSTNAE 257
Cdd:COG1234  149 PGRSLVYSGDTRPCE--------ALVELA----KGADLLIHEATFLD 183
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 68-253 1.26e-17

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 81.35  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  68 IVPLGGLGEIGRNMNVVEYNGHLLLIDCGvLFPEEEQpGVDLILPDFHYIKDRLDkveALVLTHGHEDHIGGVPYLLKLR 147
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCG-LFQGGKE-LEELNNEPFPFDPKEID---AVILTHAHLDHSGRLPLLVKEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 148 PDIPLIGSKLTLAFV-----------EAKCKEHHINP--TMIEVKG-RDKIKAGPFNLEF-----VTVT-----HsIPDA 203
Cdd:cd16295   76 FRGPIYATPATKDLAelllldsakiqEEEAEHPPAEPlyTEEDVEKaLKHFRPVEYGEPFeigpgVKVTfydagH-ILGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505262897 204 LAVCVRTPAG-SLIDTGDIKLDQLPLdHKITDLVEfgklgerGIDLLMMDS 253
Cdd:cd16295  155 ASVELEIGGGkRILFSGDLGRKNTPL-LRDPAPPP-------EADYLIMES 197
RNase_J_C pfam17770
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ...
 512-609 8.76e-16

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: 73.30  E-value: 8.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  512 LEKRRILGTEGFVSSFVVVNTDTADVLSGPKIYLN-AVAEDESE--FEKVRHQIVEQLQDAMMQGTRDTHKLQQIMRRTL 588
Cdd:pfam17770   2 LRDRKRLSEDGLVIVVVTIDKETGKLVAGPDIISRgFVYVRESEdlIEEAEEVVREALERADEKGIADWGALKEKIRRAL 81

                          90       100
                  ....*....|....*....|.
gi 505262897  589 GSWVARQLHRKPVIVPVVADI 609
Cdd:pfam17770  82 RRFLYEKTKRRPMILPIIMEV 102
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 66-307 9.44e-16

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 79.46  E-value: 9.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  66 MRIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVLFPEEEQPgvdliLPDFHYikdRLDKVEALVLTHGHEDHIGGVPYLLK 145
Cdd:COG1236    1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERN-----WPPFPF---RPSDVDAVVLTHAHLDHSGALPLLVK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 146 LRPDIPLIGSKLTLAFVE------AKC--KEHHINP--TMIEVKG----RDKIKAG-PFNLEFVTVT-----HsIPDALA 205
Cdd:COG1236   73 EGFRGPIYATPATADLARillgdsAKIqeEEAEAEPlyTEEDAERalelFQTVDYGePFEIGGVRVTfhpagH-ILGSAQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 206 VCVRTPAGSLIDTGDIKLDQLPLdHKITDLVEfgklgerGIDLLMMDST--NAEVPGFVRPETTIGPVLDRVFAEAtRKI 283
Cdd:COG1236  152 VELEVGGKRIVFSGDYGREDDPL-LAPPEPVP-------PADVLITESTygDRLHPPREEVEAELAEWVRETLARG-GTV 222

                        250       260
                 ....*....|....*....|....*..
gi 505262897 284 IVASFSshVHRVQQVV---DAAHKYGR 307
Cdd:COG1236  223 LIPAFA--LGRAQELLyllRELKKEGR 247
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 78-254 2.04e-14

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 73.39  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  78 GRNMN--VVEYNGHLLLIDCGvlfpeeeqpgvdlilPDFHYIKDRL----DKVEALVLTHGHEDHIGGVPYLLK--LRPD 149
Cdd:COG1235   32 GRTRSsiLVEADGTRLLIDAG---------------PDLREQLLRLgldpSKIDAILLTHEHADHIAGLDDLRPryGPNP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 150 IPLIGSKLTLAFVEAKC----KEHHINPTMIEVKGRDKIKAGPFNLEFVTVTHSIPDALAVCVRTPAGSLI---DTGDIk 222
Cdd:COG1235   97 IPVYATPGTLEALERRFpylfAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAyatDTGYI- 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 505262897 223 ldqlplDHKITDLVefgklgeRGIDLLMMDST 254
Cdd:COG1235  176 ------PEEVLELL-------RGADLLILDAT 194
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 67-221 2.30e-12

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 66.16  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  67 RIVPLGGLGEigrNMNVVEY-NGHLLLIDCGvlfpeeeQPGVDLILpdfHYIKDRLDKVEALVLTHGHEDHIGGVPYLLK 145
Cdd:cd06262    1 KRLPVGPLQT---NCYLVSDeEGEAILIDPG-------AGALEKIL---EAIEELGLKIKAILLTHGHFDHIGGLAELKE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 146 lRPDIPLIGSKLTLAFVEAKCK--------EHHINPTMIEVKGRDKIKAGPFNLEFVTVT-HSiPDalAVCVRTPAGSLI 216
Cdd:cd06262   68 -APGAPVYIHEADAELLEDPELnlaffgggPLPPPEPDILLEDGDTIELGGLELEVIHTPgHT-PG--SVCFYIEEEGVL 143


                 ....*
gi 505262897 217 DTGDI 221
Cdd:cd06262  144 FTGDT 148
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 66-144 6.37e-11

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293850  Cd Length: 194  Bit Score: 61.83  E-value: 6.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  66 MRIVPLGGLGEIGRNMNVVEYNGHLLLIDCGVlfpeeeQPGVDLI--LPDFHYIKdrLDKVEALVLTHGHEDHIGGVPYL 143
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGI------HPGYSGLasLPFFDEID--LSEIDLLLITHFHLDHCGALPYF 72


                 .
gi 505262897 144 L 144
Cdd:cd16292   73 L 73
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 87-221 6.71e-11

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 62.95  E-value: 6.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  87 NGHLLLIDCGVlfPEEEQPGVDLILPdfhYIKDR-LDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKL-----TLA 160
Cdd:COG2333   20 DGKTILIDTGP--RPSFDAGERVVLP---YLRALgIRRLDLLVLTHPDADHIGGLAAVLEAFPVGRVLVSGPpdtseTYE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262897 161 FVEAKCKEHHINPTmiEVKGRDKIKAGPFNLEFVTVTHSIPDA-------LAVCVRTPAGSLIDTGDI 221
Cdd:COG2333   95 RLLEALKEKGIPVR--PCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnsLVLRLTYGGFSFLLTGDA 160
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 91-254 2.45e-10

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: 60.40  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   91 LLIDCGvlfPEEEQPgvdlILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPdIPLIGSKLTLAFVEAKC---- 166
Cdd:pfam12706   3 ILIDPG---PDLRQQ----ALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRP-RPLYAPLGVLAHLRRNFpylf 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  167 KEHHINPTMIEVKGRDKIKAGPFNLEF--VTVTHSIPDALAVCVRTPAGSLIDTGDIKLdqlpldHKITDLVEF-GKLGE 243
Cdd:pfam12706  75 LLEHYGVRVHEIDWGESFTVGDGGLTVtaTPARHGSPRGLDPNPGDTLGFRIEGPGKRV------YYAGDTGYFpDEIGE 148

                         170
                  ....*....|...
gi 505262897  244 R--GIDLLMMDST 254
Cdd:pfam12706 149 RlgGADLLLLDGG 161
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 84-200 4.99e-10

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: 60.71  E-value: 4.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGHLLLIDCG---VLFPEEEQPGVDLilpdfhyikdrlDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKltLA 160
Cdd:cd07713   25 IETEGKKILFDTGqsgVLLHNAKKLGIDL------------SDIDAVVLSHGHYDHTGGLKALLELNPKAPVYAHP--DA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505262897 161 FVEAKCKEHHINPTMIEvkGRDKIKAGPFNLEFVTVTHSI 200
Cdd:cd07713   91 FEPRYSKRGGGKKGIGI--GREELEKAGARLVLVEEPTEI 128
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 83-145 7.56e-10

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: 58.30  E-value: 7.56e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262897  83 VVEYNGHLLLIDCGvlfpEEEQPGVDLILPdfhYIKDR-LDKVEALVLTHGHEDHIGGVPYLLK 145
Cdd:cd07731   14 LIQTPGKTILIDTG----PRDSFGEDVVVP---YLKARgIKKLDYLILTHPDADHIGGLDAVLK 70
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
84-200 1.22e-09

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 59.51  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGHLLLIDCG---VLFPEEEQPGVDLilpdfhyikdrlDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKltlA 160
Cdd:COG1237   27 IETEGKRILFDTGqsdVLLKNAEKLGIDL------------SDIDAVVLSHGHYDHTGGLPALLELNPKAPVYAHP---D 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505262897 161 FVEAKCKEHHINPTMIEVKGRDKIKAGPFNLEFVTVTHSI 200
Cdd:COG1237   92 AFEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEI 131
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 83-221 3.35e-09

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: 57.39  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  83 VVEYNGHLLLIDCGVlfpeeEQPGVDLILpdfHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTLAFV 162
Cdd:COG0491   19 LIVGGDGAVLIDTGL-----GPADAEALL---AALAALGLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAHAAEAEAL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262897 163 EAKCKEHHINPTMIE----VKGRDKIKAGPFNLEFV-TVTHSiPDalAVCVRTPAGSLIDTGDI 221
Cdd:COG0491   90 EAPAAGALFGREPVPpdrtLEDGDTLELGGPGLEVIhTPGHT-PG--HVSFYVPDEKVLFTGDA 150
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 80-167 3.51e-09

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: 56.85  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  80 NMNVVEYNGHLLLIDCGVlfpeeeqPG-VDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLT 158
Cdd:cd07721   12 NAYLIEDDDGLTLIDTGL-------PGsAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKE-APGAPVYAHERE 83


                 ....*....
gi 505262897 159 LAFVEAKCK 167
Cdd:cd07721   84 APYLEGEKP 92
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
74-221 3.82e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.99  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   74 LGEIGRNMNVVEYNGHLLLIDCGVlfpeeeqPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLI 153
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGG-------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262897  154 GSKLTLAF---VEAKCKEHHINPT-------MIEVKGRDKIKAGPFNLEFVTVTHSiPDALAVCVRTPAGSLIDTGDI 221
Cdd:pfam00753  74 VAEEARELldeELGLAASRLGLPGppvvplpPDVVLEEGDGILGGGLGLLVTHGPG-HGPGHVVVYYGGGKVLFTGDL 150
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 121-196 4.98e-09

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 57.11  E-value: 4.98e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505262897 121 LDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKLTLAFVEAKCkeHHINPTMIEVKGRDKIKAGPFNLEFVTV 196
Cdd:cd07709   66 PRKIDYIVVNHQEPDHSGSLPELLELAPNAKIVCSKKAARFLKHFY--PGIDERFVVVKDGDTLDLGKHTLKFIPA 139
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 84-253 5.17e-09

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: 55.91  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGHLLLIDCGvlfpeeeqPGVDLILpdFHYIkdRLDKVEALVLTHGHEDHIGGVP---YLLKLRPD------IPLIG 154
Cdd:cd07716   23 LEADGFRILLDCG--------SGVLSRL--QRYI--DPEDLDAVVLSHLHPDHCADLGvlqYARRYHPRgarkppLPLYG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 155 SKLTLAFVEAKCKEHHInPTMIEVKGRDKIKAGPFNLEFVTVTHSIPdALAVCVRTPAGSLIDTGDikldqlpldhkiTD 234
Cdd:cd07716   91 PAGPAERLAALYGLEDV-FDFHPIEPGEPLEIGPFTITFFRTVHPVP-CYAMRIEDGGKVLVYTGD------------TG 156

                        170       180
                 ....*....|....*....|...
gi 505262897 235 ----LVEFGklgeRGIDLLMMDS 253
Cdd:cd07716  157 ycdeLVEFA----RGADLLLCEA 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 82-220 1.31e-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: 54.96  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  82 NVVEYNGHLLLIDCGvlfpeeeqPGVDLILPDFHYIKDRLDkveALVLTHGHEDHIGGVPYLLKLR------PDIPLIGS 155
Cdd:cd16272   20 YLLETGGTRILLDCG--------EGTVYRLLKAGVDPDKLD---AIFLSHFHLDHIGGLPTLLFARryggrkKPLTIYGP 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262897 156 KLTLAFVEAKC------KEHHINPTMIEVK-GRDKIKAGPFNLEFVTVTHSIPdALAVCVRTPAGSLIDTGD 220
Cdd:cd16272   89 KGIKEFLEKLLnfpveiLPLGFPLEIEELEeGGEVLELGDLKVEAFPVKHSVE-SLGYRIEAEGKSIVYSGD 159
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 115-192 1.73e-08

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 54.00  E-value: 1.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262897 115 HYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSkltlafveakcKEHHINPTMIEVKGRDKIKAGPFNLE 192
Cdd:cd07723   35 AALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGP-----------AEDRIPGLDHPVKDGDEIKLGGLEVK 101
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 84-165 2.21e-08

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: 54.40  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGHLLLIDCGvlfpeeeqpgvdlilPDFHY--IKDRLDKVEALVLTHGHEDHIGGV----PYLLKLRPDIPLIGSKL 157
Cdd:cd16279   40 IETGGKNILIDTG---------------PDFRQqaLRAGIRKLDAVLLTHAHADHIHGLddlrPFNRLQQRPIPVYASEE 104


                 ....*...
gi 505262897 158 TLAFVEAK 165
Cdd:cd16279  105 TLDDLKRR 112
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 69-145 3.20e-08

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 53.87  E-value: 3.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505262897  69 VPLGGLGEIGRNMNVVEYNGHLLLIDCGVlfpeeeQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLK 145
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGM------NPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFR 71
NorV COG0426
Flavorubredoxin [Energy production and conversion];
121-196 8.64e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 51.37  E-value: 8.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262897 121 LDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKLTLAFVeakckEHHINPT---MIEVKGRDKIKAGPFNLEFVTV 196
Cdd:COG0426   68 PKKIDYIIVNHQEPDHSGSLPELLELAPNAKIVCSKKAARFL-----PHFYGIPdfrFIVVKEGDTLDLGGHTLQFIPA 141
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 68-143 1.06e-06

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


Pssm-ID: 293849  Cd Length: 199  Bit Score: 49.57  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  68 IVPLGGLGEIGRNMNVVEYNGHLLLIDCGVL--FPEEEQpgvdliLPDFHYI--KDRLDK-VEALVLTHGHEDHIGGVPY 142
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHmgYNDERR------FPDFSYIsqNGPFTEhIDCVIISHFHLDHCGALPY 74


                 .
gi 505262897 143 L 143
Cdd:cd16291   75 F 75
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 63-251 5.05e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.99  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  63 KGSMRIVPLGGlgeigrNMNVVEYNGHLLLIDcGVLFPEEEQPGVDLILPDfhyikdRLDKVEALVLTHGHEDHIGGVPY 142
Cdd:COG2220    1 PGGMKITWLGH------ATFLIETGGKRILID-PVFSGRASPVNPLPLDPE------DLPKIDAVLVTHDHYDHLDDATL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 143 LLKLRPDIPLIGSKLtlafVEAKCKEHHInPTMIEVKGRDKIKAGPFNLEFVTVTHSiPDALAVCVRTPAGSLIDTGDIK 222
Cdd:COG2220   68 RALKRTGATVVAPLG----VAAWLRAWGF-PRVTELDWGESVELGGLTVTAVPARHS-SGRPDRNGGLWVGFVIETDGKT 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505262897 223 L----DqlpldhkiTDLV-EFGKLGER-GIDLLMM 251
Cdd:COG2220  142 IyhagD--------TGYFpEMKEIGERfPIDVALL 168
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-163 7.46e-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: 47.14  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  83 VVEYNGHLLLIDCGvlfPEEEQPGvdlilPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTLAFV 162
Cdd:cd07743   13 YVFGDKEALLIDSG---LDEDAGR-----KIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYAPKIEKAFI 83


                 .
gi 505262897 163 E 163
Cdd:cd07743   84 E 84
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 107-220 2.90e-05

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 44.84  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 107 VDLILpdfHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTLAFVEAKCkehhinPTMIEVKGRDKIKA 186
Cdd:cd16275   34 IEKIL---AKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVYMSKEEIDYYGFRC------PNLIPLEDGDTIKI 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 505262897 187 GPFNLEFV-TVTHSipdALAVCVRTPaGSLIdTGD 220
Cdd:cd16275  104 GDTEITCLlTPGHT---PGSMCYLLG-DSLF-TGD 133
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 91-223 3.01e-05

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: 44.56  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  91 LLIDCGVLFPEeeqpgvdlILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKlRPDIPLIGSKLTLAFVEAKCKEHH 170
Cdd:cd07733   21 LLIDAGLSGRK--------ITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLAR-KYNVPIYATAGTLRAMERKVGLID 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505262897 171 INPTMIEVKGrDKIKAGPFNLEFVTVTHsipDAlavcvRTPAGSLIDTGDIKL 223
Cdd:cd07733   92 VDQKQIFEPG-ETFSIGDFDVESFGVSH---DA-----ADPVGYRFEEGGRRF 135
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
121-194 3.61e-05

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 46.61  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505262897 121 LDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKLTLAFVEakcKEHHINPTMIEVKGRDKIKAGPFNLEFV 194
Cdd:PRK11921  67 LDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCTKNGAKSLK---GHYHQDWNFVVVKTGDRLEIGSNELIFI 137
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 82-220 5.59e-05

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 44.43  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  82 NVVEYNGHLLLIDCGvlfpeeeqPGVdliLPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLR------PDIPLIG- 154
Cdd:cd07719   21 TLVVVGGRVYLVDAG--------SGV---VRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAwlagrkTPLPVYGp 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 155 ---SKLTLAFVEA---------KCKEHHINPTMIEVKGRDkIKAGPFNLEF--VTVT-----HS-IPDALAVCVRTPAGS 214
Cdd:cd07719   90 pgtRALVDGLLAAyaldidyraRIGDEGRPDPGALVEVHE-IAAGGVVYEDdgVKVTaflvdHGpVPPALAYRFDTPGRS 168


                 ....*.
gi 505262897 215 LIDTGD 220
Cdd:cd07719  169 VVFSGD 174
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 83-222 1.13e-04

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


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 45.27  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897   83 VVEYNGHLLLIDCGVLFPEEEQpGVDLILPdfhYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKltlAFV 162
Cdd:TIGR00361 454 FIGANGKGILYDTGEPWREGSL-GEKVIIP---FLTAKGIKLEALILSHADQDHIGGAEIILKHHPVKRLVIPK---GFV 526

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505262897  163 EakcKEHHINPTmieVKGRD-KIKagpfNLEFVTVTHSIPD-------ALAVCVRTPAGSLIDTGDIK 222
Cdd:TIGR00361 527 E---EGVAIEEC---KRGDVwQWQ----GLQFHVLSPEAPDpasknnhSCVLWVDDGGNSWLLTGDLE 584
PRK11539 PRK11539
ComEC family competence protein; Provisional
 83-151 1.39e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 44.98  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505262897  83 VVEYNGHLLLIDCGVLFPEEEQpGVDLILPdfhYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIP 151
Cdd:PRK11539 515 VIERNGKAILYDTGNAWPTGDS-AQQVIIP---WLRWHGLTPEGIILSHEHLDHRGGLASLLHAWPMAW 579
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 410-455 1.76e-04

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: 39.91  E-value: 1.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 505262897  410 ARVVNKDnaavHVSGHANEGELLYLYNIIKPKCAMPIHGENRHLVA 455
Cdd:pfam07521   6 ARIETID----GFSGHADRRELLELIKGLKPKPIVLVHGEPRALLA 47
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 91-173 1.80e-04

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 42.91  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  91 LLIDCGvlfpEEEQPGVDlilpdfhYIKDRLDK-----VEALVLTHGHEDHIGGVPYLLKL--RPDIPLIGSKLTLAFVE 163
Cdd:cd07722   30 ILIDTG----EGRPSYIP-------LLKSVLDSegnatISDILLTHWHHDHVGGLPDVLDLlrGPSPRVYKFPRPEEDED 98

                         90
                 ....*....|
gi 505262897 164 AKCKEHHINP 173
Cdd:cd07722   99 PDEDGGDIHD 108
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 84-172 1.87e-04

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


Pssm-ID: 293860  Cd Length: 212  Bit Score: 43.00  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGhLLLIDCG--VLF--PEEEQPGVDLIlpdfHYIKDRLD-KVEALVLTHGHEDHIGGVPYLLKLrpDIPLIGSKLT 158
Cdd:cd16302   25 VPCNG-MIVINGGeaVVFdtPTNDSQSEELI----DWIENSLKaKVKAVVPTHFHDDCLGGLKAFHRR--GIPSYANQKT 97

                         90
                 ....*....|....
gi 505262897 159 LAFveakCKEHHIN 172
Cdd:cd16302   98 IAL----AKEKGLP 107
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
55-235 2.93e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 43.02  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  55 LIAPPKYRKGSMRIVPLGGLGEIG-RNMN----VVEYNGHLLLIDCGVLFPE---EEQPGVDLILPDfhyikDRLDKVEA 126
Cdd:COG5212    1 LLFTAAAAAPSMEVRVLGCSGGISdGNLTtyllRPLGSDDYVLLDAGTVVSGlelAEQKGAFKGRQG-----YVLEHIKG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 127 LVLTHGHEDHIGGVPYLLKLRPDIPLIGskltLAFVEAKCKEHHIN----P--------------TMIEVKGRDKIKAG- 187
Cdd:COG5212   76 YLISHAHLDHIAGLPILSPDDSPKTIYA----LPETIDALRNHYFNwviwPdftdigsaphlpkyRYVPLKPGQTFPLGg 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 505262897 188 -PFNLEFVTVTHSIPdALAVCVRTPAGSLIDTGDIKLDQLPLDHKITDL 235
Cdd:COG5212  152 tGLRVTAFPLSHSVP-SSAFLIESGGGAFLYSGDTGPDEVEKSTNLDAL 199
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 83-206 4.31e-04

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 41.89  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  83 VVEYNGHLLLIDCgvlfPEEEQPGVDLIlpdfHYIKDRLDK-VEALVLTHGHEDHIGGVPYLLKlrPDIPLIGSKLTLAF 161
Cdd:cd16285   30 IVIDGKGLVLIDT----PWTEAQTATLL----DWIEKKLGKpVTAAISTHSHDDRTGGIKALNA--RGIPTYATALTNEL 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505262897 162 VEAKCKEHhinPTMiEVKGRDKIKAGPFNLEFVTVTHSiPDALAV 206
Cdd:cd16285  100 AKKEGKPV---PTH-SLKGALTLGFGPLEVFYPGPGHT-PDNIVV 139
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 84-144 5.69e-04

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 41.48  E-value: 5.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505262897  84 VEYNGHLLLIDCGV-LFPEEEQPGVDLilpdfhyikdrlDKVEALVLTHGHEDHIGGVPYLL 144
Cdd:cd07740   21 VASEAGRFLIDCGAsSLIALKRAGIDP------------NAIDAIFITHLHGDHFGGLPFFL 70
PRK02113 PRK02113
MBL fold metallo-hydrolase;
66-197 9.20e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 41.31  E-value: 9.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  66 MRIVPLG-----GLGEIG----------------RNMNVVEYNGHLLLIDCGvlfpeeeqpgvdlilPDFHY--IKDRLD 122
Cdd:PRK02113   1 MKIRILGsgtstGVPEIGctcpvctskdprdnrlRTSALVETEGARILIDCG---------------PDFREqmLRLPFG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 123 KVEALVLTHGHEDHIGGvpyLLKLRP-----DIPLIGSKLTLAFVEAK---CKEHHINPTMIEVKGRDKIKAGPFNLEFV 194
Cdd:PRK02113  66 KIDAVLITHEHYDHVGG---LDDLRPfcrfgEVPIYAEQYVAERLRSRmpyCFVEHSYPGVPNIPLREIEPDRPFLVNHT 142


                 ...
gi 505262897 195 TVT 197
Cdd:PRK02113 143 EVT 145
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 112-158 9.21e-04

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 41.35  E-value: 9.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 505262897 112 PDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLIGSKLT 158
Cdd:PRK10241  34 PVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 83-164 9.84e-04

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 40.73  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  83 VVEYNGHLLLIDCgvlfPEEEQPGVDLILpdfhYIKDRLDK-VEALVLTHGHEDHIGGVPYLLKlrPDIPLIGSKLTLAF 161
Cdd:cd16304   30 IVETSKGVVLIDT----PWDDEQTEELLD----WIKKKLKKpVTLAIVTHAHDDRIGGIKALQK--RGIPVYSTKLTAQL 99


                 ...
gi 505262897 162 VEA 164
Cdd:cd16304  100 AKK 102
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 105-155 1.30e-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: 40.23  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505262897 105 PG--VDLILPdfhYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRpDIPLIGS 155
Cdd:cd07737   29 PGgdADKILQ---AIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIGP 77
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 83-143 1.42e-03

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 40.66  E-value: 1.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505262897  83 VVEYNGHLLLIDCG-----VLFPEEEQPGVDLILPDFHYIKDRLDK-------VEALVLTHGHEDHIGGVPYL 143
Cdd:cd07729   36 LIEHPEGTILVDTGfhpdaADDPGGLELAFPPGVTEEQTLEEQLARlgldpedIDYVILSHLHFDHAGGLDLF 108
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 83-153 2.62e-03

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 39.78  E-value: 2.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505262897  83 VVEYNGHLLLIDCGVlfpeeeQPGVDLILPDFHYIKDRLDKVEALVLTHGHEDHIGGVPYLLKLRPDIPLI 153
Cdd:cd07726   20 LLDGEGRPALIDTGP------SSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVY 84
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 66-220 4.71e-03

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: 39.12  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  66 MRIVPLG--GlGEIGRNM-----NVVEYNGHLLlIDCG----VLfpEEEQPGVDLILPDFHYIKDRLDKVEALVLTHGHE 134
Cdd:cd07735    1 FELVVLGcsG-GPDEGNTssfllDPAGSDGDIL-LDAGtgvgAL--SLEEMFNDILFPSQKAAYELYQRIRHYLITHAHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 135 DHIGGVP------YLLKLRPdIPLIGSKLTLA--------------FVEAKCKEHHINPtMIEVKGRDKIKAGPFNLEFV 194
Cdd:cd07735   77 DHIAGLPllspndGGQRGSP-KTIYGLPETIDalkkhifnwviwpdFTSIPSGKYPYLR-LEPIEPEYPIALTGLSVTAF 154

                        170       180
                 ....*....|....*....|....*.
gi 505262897 195 TVTHSIPDALAVCVRTPAGSLIDTGD 220
Cdd:cd07735  155 PVSHGVPVSTAFLIRDGGDSFLFFGD 180
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 84-234 7.26e-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: 7.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897  84 VEYNGHLLLIDCGVLFPEEEQPGVDLilpdfhyikdrldkvEALVLTHGHEDHIGGvpyLLKLR----PDIPLIGSKltl 159
Cdd:cd07736   42 IEVDGERILLDAGLTDLAERFPPGSI---------------DAILLTHFHMDHVQG---LFHLRwgvgDPIPVYGPP--- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 160 afVEAKCKEHHINPTMIEVKgrdKIKAG--PFNLEFVTVT-----HSIPdALAVCVRTPAGS---LIDTGDIK------L 223
Cdd:cd07736  101 --DPQGCADLFKHPGILDFQ---PLVAPfqSFELGGLKITplplnHSKP-TFGYLLESGGKRlayLTDTLGLPeetlefL 174

                        170
                 ....*....|.
gi 505262897 224 DQLPLDHKITD 234
Cdd:cd07736  175 KQQQPDVLVLD 185
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 123-221 9.89e-03

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: 37.71  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505262897 123 KVEALVLTHGHEDHIGGVPYlLKLRPDIPLIGSKLTLAFVE-----AKCKEHHINPTM---IEVKGRDKIKAGPFNLEFV 194
Cdd:cd16322   46 TLLYILLTHAHFDHVGGVAD-LRRHPGAPVYLHPDDLPLYEaadlgAKAFGLGIEPLPppdRLLEDGQTLTLGGLEFKVL 124

                         90       100
                 ....*....|....*....|....*...
gi 505262897 195 -TVTHSiPDalAVCVRTPAGSLIDTGDI 221
Cdd:cd16322  125 hTPGHS-PG--HVCFYVEEEGLLFSGDL 149
 
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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