NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2055645045|ref|WP_216560923|]
View 

MBL fold metallo-hydrolase RNA specificity domain-containing protein [Tissierella carlieri]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-465 0e+00

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


:

Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 678.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   1 MDIQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRG 80
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  81 RIITTNATYDLCKIMLKDSAKIQESDVEWENRKRqRAGKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDA 160
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKR-YSGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 161 GHILGSAILELWVREvnEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIESTYGDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:COG1782   160 GHILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 241 GTVIIPSFAVGRTQELIYKLNKYYEYN--PEVeeymkvPIYIDSPMAVDATEAFKRNSSSFNDEARALILKGDNPFQFSN 318
Cdd:COG1782   238 GKVLIPAFAVGRTQEILYVLNELMREGkiPEV------PVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFEN 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 319 LRYIKSQEESMALNKYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRILLDGKRQVKILGEEIHV 398
Cdd:COG1782   312 LHYVESVEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPV 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055645045 399 RAQIYDIKGFSGHADQNMLLDWINKFKKKPKKIFVVHGEEEPANALSTLIRHLYKIETIIPNINDSF 465
Cdd:COG1782   392 RAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETI 458
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-465 0e+00

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 678.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   1 MDIQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRG 80
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  81 RIITTNATYDLCKIMLKDSAKIQESDVEWENRKRqRAGKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDA 160
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKR-YSGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 161 GHILGSAILELWVREvnEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIESTYGDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:COG1782   160 GHILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 241 GTVIIPSFAVGRTQELIYKLNKYYEYN--PEVeeymkvPIYIDSPMAVDATEAFKRNSSSFNDEARALILKGDNPFQFSN 318
Cdd:COG1782   238 GKVLIPAFAVGRTQEILYVLNELMREGkiPEV------PVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFEN 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 319 LRYIKSQEESMALNKYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRILLDGKRQVKILGEEIHV 398
Cdd:COG1782   312 LHYVESVEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPV 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055645045 399 RAQIYDIKGFSGHADQNMLLDWINKFKKKPKKIFVVHGEEEPANALSTLIRHLYKIETIIPNINDSF 465
Cdd:COG1782   392 RAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETI 458
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-212 2.49e-106

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: 316.32  E-value: 2.49e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   3 IQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRGRI 82
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  83 ITTNATYDLCKIMLKDSAKIQESDVEwenrkrqragKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDAGH 162
Cdd:cd16295    81 YATPATKDLAELLLLDSAKIQEEEAE----------HPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGH 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2055645045 163 ILGSAILELwvrEVNEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIES 212
Cdd:cd16295   151 ILGSASVEL---EIGGGKRILFSGDLGRKNTPLLRDPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 253-382 8.41e-54

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 178.12  E-value: 8.41e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  253 TQELIYKLNKYYEYNpeveEYMKVPIYIDSPMAVDATEAFKRNSSSFNDEARALILKGDNPFQFSNLRYIKSQEESMALN 332
Cdd:smart01027   1 TQELLLILEELWREG----ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2055645045  333 KYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRIL 382
Cdd:smart01027  77 DYKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 253-380 1.97e-46

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 158.06  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 253 TQELIYKLNKYYEYNpeveEYMKVPIYIDSPMAVDATEAFKRNSSSFNDEARalilkgdnpfqfsnlRYIKSQEESMALN 332
Cdd:pfam10996   1 AQELLYLLDELWREG----RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEAR---------------HFVISKSESKAIN 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2055645045 333 KYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGR 380
Cdd:pfam10996  62 EGKGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 5-73 3.92e-03

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 39.74  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   5 FYGAA-KMVTGSNY---LVKTEKyNILVD------CGMFQGNEEME-KLNynnfpynpsEIDFLILTHAHIDHSGRIPKL 73
Cdd:PRK05452   22 FHGTEyKTLRGSSYnsyLIREEK-NVLIDtvdhkfSREFVQNLRNEiDLA---------DIDYIVINHAEEDHAGALTEL 91
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-465 0e+00

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 678.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   1 MDIQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRG 80
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNDAFPFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  81 RIITTNATYDLCKIMLKDSAKIQESDVEWENRKRqRAGKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDA 160
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKR-YSGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 161 GHILGSAILELWVREvnEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIESTYGDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:COG1782   160 GHILGSAIVHLHIGD--GLHNIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 241 GTVIIPSFAVGRTQELIYKLNKYYEYN--PEVeeymkvPIYIDSPMAVDATEAFKRNSSSFNDEARALILKGDNPFQFSN 318
Cdd:COG1782   238 GKVLIPAFAVGRTQEILYVLNELMREGkiPEV------PVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFEN 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 319 LRYIKSQEESMALNKYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRILLDGKRQVKILGEEIHV 398
Cdd:COG1782   312 LHYVESVEESKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIPV 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055645045 399 RAQIYDIKGFSGHADQNMLLDWINKFKKKPKKIFVVHGEEEPANALSTLIRHLYKIETIIPNINDSF 465
Cdd:COG1782   392 RAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETI 458
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-439 0e+00

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 591.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   1 MDIQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEmekLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRG 80
Cdd:COG1236     1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKE---RNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  81 RIITTNATYDLCKIMLKDSAKIQESDVEwenrkrqragkkpIEPLYTMKDAENSLKYFEPYFIDQKIKINDnIQIRFKDA 160
Cdd:COG1236    78 PIYATPATADLARILLGDSAKIQEEEAE-------------AEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 161 GHILGSAILELWVrevnEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIESTYGDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:COG1236   144 GHILGSAQVELEV----GGKRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRETLARG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 241 GTVIIPSFAVGRTQELIYKLNKYYEYNpeveEYMKVPIYIdSPMAVDATEAFKRNSSSFNDEARalilkgdNPFQFSNLR 320
Cdd:COG1236   220 GTVLIPAFALGRAQELLYLLRELKKEG----RLPDIPIYV-SGMAIRATEIYRRHGEYLRDEAQ-------DPFALPNLR 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 321 YIKSQEESMALNKyTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRILLDGKRQVKILGEEIHVRA 400
Cdd:COG1236   288 FVTSVEESKALNR-KGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEVPVRA 366

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2055645045 401 QIYDIKGFSGHADQNMLLDWINkFKKKPKKIFVVHGEEE 439
Cdd:COG1236   367 RVERLFGLSAHADWDELLEWIK-ATGKPERVFLVHGEPE 404
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-212 2.49e-106

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: 316.32  E-value: 2.49e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   3 IQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRGRI 82
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  83 ITTNATYDLCKIMLKDSAKIQESDVEwenrkrqragKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDAGH 162
Cdd:cd16295    81 YATPATKDLAELLLLDSAKIQEEEAE----------HPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGH 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2055645045 163 ILGSAILELwvrEVNEEVKVVFSGDLGMPGRPIINSPDYIDEADYLVIES 212
Cdd:cd16295   151 ILGSASVEL---EIGGGKRILFSGDLGRKNTPLLRDPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 253-382 8.41e-54

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 178.12  E-value: 8.41e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  253 TQELIYKLNKYYEYNpeveEYMKVPIYIDSPMAVDATEAFKRNSSSFNDEARALILKGDNPFQFSNLRYIKSQEESMALN 332
Cdd:smart01027   1 TQELLLILEELWREG----ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2055645045  333 KYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGRIL 382
Cdd:smart01027  77 DYKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 253-380 1.97e-46

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 158.06  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 253 TQELIYKLNKYYEYNpeveEYMKVPIYIDSPMAVDATEAFKRNSSSFNDEARalilkgdnpfqfsnlRYIKSQEESMALN 332
Cdd:pfam10996   1 AQELLYLLDELWREG----RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEAR---------------HFVISKSESKAIN 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2055645045 333 KYTFPKVIISSSGMATAGRIRHHLKHNLWDEKNSLVFVGYQAEGTLGR 380
Cdd:pfam10996  62 EGKGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 6-212 1.93e-36

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: 134.00  E-value: 1.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   6 YGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKlnynNFPYN---PSEIDFLILTHAHIDHSGRIPKLVK-DGFRGR 81
Cdd:cd07734     3 LGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEA----CLPQFellPPEIDAILISHFHLDHCGALPYLFRgFIFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  82 IITTNATYDLCKIMLKDSAKIQESdvewenrkrqragKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKDAG 161
Cdd:cd07734    79 IYATHPTVALGRLLLEDYVKSAER-------------IGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055645045 162 HILGSAIlelWVREVNEEvKVVFSGDLGM-PGRPIinSPDYID--EADYLVIES 212
Cdd:cd07734   146 HVLGAAM---WEIQIYGE-KLVYTGDFSNtEDRLL--PAASILppRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 7-187 2.34e-21

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: 91.88  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   7 GAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKLNYNNFpYNPSEIDFLILTHAHIDHSGRIPKLV-KDGFRGRIITT 85
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDE-IDLSEIDLLLITHFHLDHCGALPYFLqKTNFKGRVFMT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  86 NATYDLCKIMLKDSAKIQESDVEwenrkrqragkkpiEPLYTMKDAENSLKYFEPYFIDQKIKINDniqIRFK--DAGHI 163
Cdd:cd16292    86 HPTKAIYKWLLSDYVRVSNISSD--------------EMLYTETDLEASMDKIETIDFHQEVEVNG---IKFTayNAGHV 148

                         170       180
                  ....*....|....*....|....
gi 2055645045 164 LGSAILELwvrEVnEEVKVVFSGD 187
Cdd:cd16292   149 LGAAMFMV---EI-AGVRVLYTGD 168
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-193 2.45e-21

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: 91.94  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   7 GAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEMEKlnYNNFPYNPSE------IDFLILTHAHIDHSGRIPKLVKD-GFR 79
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERR--FPDFSYISQNgpftehIDCVIISHFHLDHCGALPYFTEVvGYD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  80 GRIITTNATYDLCKIMLKDSAKIQesdvewenrkrqrAGKKPIEPLYTMKDAENSLKYFEPYFIDQKIKINDNIQIRFKD 159
Cdd:cd16291    83 GPIYMTHPTKAICPILLEDYRKIA-------------VERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYY 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2055645045 160 AGHILGSAIleLWVReVNEEvKVVFSGDLGM-PGR 193
Cdd:cd16291   150 AGHVLGAAM--FYVR-VGDE-SVVYTGDYNMtPDR 180
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-240 6.22e-16

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: 75.67  E-value: 6.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   17 YLVKTEKYNILVDCGMFQGNEEMEKLNYnnfpYNPSEIDFLILTHAHIDHSGRIPKLVKDgFRGRIITTNATYDLckiml 96
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAEDLLAELKK----LGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAEL----- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   97 kdsakIQESDVEWENRKRQRAGKKPIEPLYTmkdaenslkyfepyfiDQKIKInDNIQIRFKDA-GHILGSAILELwvre 175
Cdd:smart00849  73 -----LKDLLALLGELGAEAEPAPPDRTLKD----------------GDELDL-GGGELEVIHTpGHTPGSIVLYL---- 126

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055645045  176 vnEEVKVVFSGDLGMPGrpiinspdyideaDYLVIESTYGDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:smart00849 127 --PEGKILFTGDLLFAG-------------GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPG 176
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
17-240 2.92e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.55  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMFQGNEEMEKLNYNNFPynPSEIDFLILTHAHIDHSGRIPKLVKdgfrgriittnaTYDLCKIMl 96
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEAALLLLLAALGLG--PKDIDAVILTHGHFDHIGGLGELAE------------ATDVPVIV- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  97 kdsakIQESDVEWENRKRQRAGKKPIEPLYTMKDaenslkyFEPYFIDQKIKINDNIQIRFKDAGHILGSAILelwVREV 176
Cdd:pfam00753  74 -----VAEEARELLDEELGLAASRLGLPGPPVVP-------LPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH---VVVY 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055645045 177 NEEVKVVFSGDLGMPGRPIINSPDYIDEADYLviestygDTIHESYEESTEKLIDIINKTVLRG 240
Cdd:pfam00753 139 YGGGKVLFTGDLLFAGEIGRLDLPLGGLLVLH-------PSSAESSLESLLKLAKLKAAVIVPG 195
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 395-459 3.13e-13

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: 64.56  E-value: 3.13e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055645045 395 EIHVRAQIYDIKGFSGHADQNMLLDWINkfKKKPKKIFVVHGEEEPANALSTLIRHLYKIETIIP 459
Cdd:pfam07521   1 GIPVRARIETIDGFSGHADRRELLELIK--GLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-68 1.00e-08

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 55.28  E-value: 1.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  18 LVKTEKYNILVDCGMFQGNEE-MEKLNYNNfpYNPSEIDFLILTHAHIDHSG 68
Cdd:cd07711    26 LIKDGGKNILVDTGTPWDRDLlLKALAEHG--LSPEDIDYVVLTHGHPDHIG 75
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 17-75 1.32e-08

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 54.92  E-value: 1.32e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055645045  17 YLVKTEKYNILVDCGM-FQGN---EEMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLVK 75
Cdd:cd07721    14 YLIEDDDGLTLIDTGLpGSAKrilKALRELGLS-----PKDIRRILLTHGHIDHIGSLAALKE 71
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-199 1.54e-08

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 55.58  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  18 LVKTEKYNILVDCGMfqGNEEMEKLNYNNFP--------------YNPSEIDFLILTHAHIDHSGRIPKLVKDGfRGRII 83
Cdd:cd16281    47 LIETGGRNILIDTGI--GDKQDPKFRSIYVQhsehsllkslarlgLSPEDITDVILTHLHFDHCGGATRADDDG-LVELL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  84 TTNATYDLCKimlkdsakiqesdVEWENRK----RQRAG--KKPIEPLYtmkdAENSLKyfepyFIDQK-IKINDNIQIR 156
Cdd:cd16281   124 FPNATYWVQK-------------RHWEWALnpnpRERASflPENIEPLE----ESGRLK-----LIDGSdAELGPGIRFH 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2055645045 157 FKDaGHILGSAIlelwVREVNEEVKVVFSGDLgMPGRPIINSP 199
Cdd:cd16281   182 LSD-GHTPGQML----PEISTPGGTVVFAADL-IPTSAHIPLP 218
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
17-153 2.94e-08

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 54.89  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGmfQGN---EEMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLVKdgFRGRIittnatydlcK 93
Cdd:COG1237    25 ALIETEGKRILFDTG--QSDvllKNAEKLGID-----LSDIDAVVLSHGHYDHTGGLPALLE--LNPKA----------P 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  94 IMLKDSAkiqesdveWENRKRQRAGKKPIEPLYTMKDAENslKYFEPYFIDQKIKINDNI 153
Cdd:COG1237    86 VYAHPDA--------FEKRYSKRPGGKYIGIPFSREELEK--LGARLILVKEPTEIAPGV 135
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 17-192 2.25e-07

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: 51.13  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTE-KYNILVDCGMfQGNEEMEKLNYNNfpynPSEIDFLILTHAHIDHSGRIPKLvKDGFRGRIIttnatydlckim 95
Cdd:cd06262    13 YLVSDEeGEAILIDPGA-GALEKILEAIEEL----GLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVY------------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  96 lkdsakIQESDVEWENRKRQRAGKKPIEPLYTMKDaensLKYFEPyfiDQKIKInDNIQIRFKDA-GHILGSAILelwvr 174
Cdd:cd06262    75 ------IHEADAELLEDPELNLAFFGGGPLPPPEP----DILLED---GDTIEL-GGLELEVIHTpGHTPGSVCF----- 135

                         170
                  ....*....|....*...
gi 2055645045 175 eVNEEVKVVFSGDLGMPG 192
Cdd:cd06262   136 -YIEEEGVLFTGDTLFAG 152
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-237 2.43e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 52.20  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  13 TGSNYLVKTEKYNILVDCG---MFQGNEemeklnynnFPYNPSEIDFLILTHAHIDHSGRIPKLVKdGFRGRIIT---TN 86
Cdd:COG1235    34 TRSSILVEADGTRLLIDAGpdlREQLLR---------LGLDPSKIDAILLTHEHADHIAGLDDLRP-RYGPNPIPvyaTP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  87 ATYDLCKIMLKDSAKIQESDVEWenrkrqragkKPIEPlytmkdaenslkyFEPYFIDQkIKI---------NDNIQIRF 157
Cdd:COG1235   104 GTLEALERRFPYLFAPYPGKLEF----------HEIEP-------------GEPFEIGG-LTVtpfpvphdaGDPVGYRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 158 KDAGHilgsailelwvrevneevKVVFSGDLGMPGRPIInspDYIDEADYLVIESTYGDTI--HESYEESTEKLIDIINK 235
Cdd:COG1235   160 EDGGK------------------KLAYATDTGYIPEEVL---ELLRGADLLILDATYDDPEpgHLSNEEALELLARLGPK 218


                  ..
gi 2055645045 236 TV 237
Cdd:COG1235   219 RL 220
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 17-208 2.51e-07

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: 51.61  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMfqGNEEMEKLnYNNFPYNPSEIDFLILTHAHIDHSGRIPKLvKDGFRGRIITTNATYDLckiml 96
Cdd:COG0491    18 YLIVGGDGAVLIDTGL--GPADAEAL-LAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAEAEA----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  97 kdsakiqesdveWENRKRQRA-GKKPIEPLYTMKDaenslkyfepyfiDQKIKInDNIQIRFKDA-GHILGSAILelwvr 174
Cdd:COG0491    89 ------------LEAPAAGALfGREPVPPDRTLED-------------GDTLEL-GGPGLEVIHTpGHTPGHVSF----- 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2055645045 175 eVNEEVKVVFSGD-LGMPGRPIINSPDYiDEADYL 208
Cdd:COG0491   138 -YVPDEKVLFTGDaLFSGGVGRPDLPDG-DLAQWL 170
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 17-68 4.02e-07

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: 51.06  E-value: 4.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  17 YLVKTEKYNILVDCGMfqgNEEMEKLNYNNFP--------------------YNPSEIDFLILTHAHIDHSG 68
Cdd:cd07729    35 YLIEHPEGTILVDTGF---HPDAADDPGGLELafppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAG 103
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 15-192 5.93e-07

metallo-beta-lactamases, subclass B3; 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 B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 51.01  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQgNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKDgfrgriitTNATYdlcki 94
Cdd:cd07708    23 AAYLIVTPQGNILIDGDMEQ-NAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQ--------TGAKV----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  95 MLKDsakiqesdvewENRKRQRAGKKPIEPlytmkDAENSLKYFEPYFIDQKIKINDNIQ---IRFK---DAGHILGSAI 168
Cdd:cd07708    89 MAGA-----------EDVSLLLSGGSSDFH-----YANDSSTYFPQSTVDRAVHDGERVTlggTVLTahaTPGHTPGCTT 152

                         170       180
                  ....*....|....*....|....
gi 2055645045 169 LELWVREVNEEVKVVFSGDLGMPG 192
Cdd:cd07708   153 WTMTLKDHGKQYQVVFADSLTVNP 176
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 4-89 7.04e-07

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 50.62  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   4 QFYGAAKMVTGSN-YLVKTEKYNILVDCGM---FQGN-----EEMEKLNYNnfpynPSEIDFLILTHAHIDHSGripKLV 74
Cdd:cd07720    38 AFLPPDPVETSVNaFLVRTGGRLILVDTGAgglFGPTagkllANLAAAGID-----PEDIDDVLLTHLHPDHIG---GLV 109

                          90
                  ....*....|....*
gi 2055645045  75 KDGfrGRIITTNATY 89
Cdd:cd07720   110 DAG--GKPVFPNAEV 122
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 17-155 8.38e-07

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: 50.70  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGM---FQGNeeMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLVKDGFRGRIIttnatydlck 93
Cdd:cd07713    23 LLIETEGKKILFDTGQsgvLLHN--AKKLGID-----LSDIDAVVLSHGHYDHTGGLKALLELNPKAPVY---------- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  94 imLKDSAkiqesdveWENRKRQRAGKKPIEPlytMKDAENSLKYFEPYFIDQKIKINDNIQI 155
Cdd:cd07713    86 --AHPDA--------FEPRYSKRGGGKKGIG---IGREELEKAGARLVLVEEPTEIAPGVYL 134
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 17-110 2.35e-06

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 48.06  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMFQGNEEMEKLNY-NNFPYNPSEIDFLILTHAHIDHSGRIPKLV-KDGFRGRIITTNAtydlcki 94
Cdd:cd07725    18 YLLRDGDETTLIDTGLATEEDAEALWEGlKELGLKPSDIDRVLLTHHHPDHIGLAGKLQeKSGATVYILDVTP------- 90

                          90
                  ....*....|....*.
gi 2055645045  95 mLKDSAKIQESDVEWE 110
Cdd:cd07725    91 -VKDGDKIDLGGLRLK 105
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 1-75 2.44e-06

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: 48.64  E-value: 2.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055645045   1 MDIQFYGAAKMVtgSNYLVKTEKYNILVDCG----MFQGNEEMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLVK 75
Cdd:cd07726     5 IDLGFLGFPGRI--ASYLLDGEGRPALIDTGpsssVPRLLAALEALGIA-----PEDVDYIILTHIHLDHAGGAGLLAE 76
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-225 6.17e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.88  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   1 MDIQFYGaakmvTG----------SNYLVKTEKYNILVDCG---MFQgneeMEKLNYNnfpynPSEIDFLILTHAHIDHS 67
Cdd:COG1234     1 MKLTFLG-----TGgavptpgratSSYLLEAGGERLLIDCGegtQRQ----LLRAGLD-----PRDIDAIFITHLHGDHI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  68 GRIPKLVKD-GFRGR-----IITTNATYDLCKIMLKDSAKIQESDVEWEnrkrqragkkPIEPlytmkdaenslkyfepy 141
Cdd:COG1234    67 AGLPGLLSTrSLAGRekpltIYGPPGTKEFLEALLKASGTDLDFPLEFH----------EIEP----------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045 142 fiDQKIKINDnIQIRFKDAGHILGS-AILelwVREvnEEVKVVFSGDlgmpGRPIINSPDYIDEADYLVIESTYGDTIHE 220
Cdd:COG1234   120 --GEVFEIGG-FTVTAFPLDHPVPAyGYR---FEE--PGRSLVYSGD----TRPCEALVELAKGADLLIHEATFLDEEAE 187


                  ....*
gi 2055645045 221 SYEES 225
Cdd:COG1234   188 LAKET 192
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 17-212 1.20e-05

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: 46.10  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCG---MFQgneeMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLV---KDGFRGRIITTnatyd 90
Cdd:cd16272    20 YLLETGGTRILLDCGegtVYR----LLKAGVD-----PDKLDAIFLSHFHLDHIGGLPTLLfarRYGGRKKPLTI----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  91 lckIMLKDSAKIQESDVEWENrkrqrAGKKPIEPLYTMKDAENSLKYFEPYFIdqkikindniqIRFKDAGHILGSAILE 170
Cdd:cd16272    86 ---YGPKGIKEFLEKLLNFPV-----EILPLGFPLEIEELEEGGEVLELGDLK-----------VEAFPVKHSVESLGYR 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2055645045 171 LWVrevnEEVKVVFSGDlGMPGRPIInspDYIDEADYLVIES 212
Cdd:cd16272   147 IEA----EGKSIVYSGD-TGPCENLV---ELAKGADLLIHEC 180
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 18-191 1.80e-05

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 46.48  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  18 LVKTEKYNILVDCGMfqGNEEMEKLNYNNFPYN---------------PSEIDFLILTHAHIDHSGRIPKLVKDGFRGri 82
Cdd:cd07728    47 LIQYQGKNYLIDAGI--GNGKLTEKQKRNFGVTeessieeslaelgltPEDIDYVLMTHLHFDHASGLTKVKGEQLVS-- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  83 ITTNATydlckimlkdsakIQESDVEWE-----NRKRQ----RAGKKPIeplytmkdaENSLKYFEpyfidQKIKINDNI 153
Cdd:cd07728   123 VFPNAT-------------IYVSEIEWEemrnpNIRSKntywKENWEPI---------EDQVKTFS-----DEIEIVPGI 175

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2055645045 154 QIRfKDAGHILGSAILELwvrEVNEEvKVVFSGDLgMP 191
Cdd:cd07728   176 TMI-HTGGHSDGHSIIEI---EQGGE-TAIHMADL-MP 207
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 13-66 5.76e-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: 43.41  E-value: 5.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055645045  13 TGSNYLVKTEKYNILVDCGmFQGNEEMEKLNynNFPYNPSEIDFLILTHAHIDH 66
Cdd:cd07733     8 KGNCTYLETEDGKLLIDAG-LSGRKITGRLA--EIGRDPEDIDAILVTHEHADH 58
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-76 6.17e-05

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. 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 B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 44.62  E-value: 6.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQgNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKD 76
Cdd:cd16288    23 ASYLITTPQGLILIDTGLES-SAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKL 83
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-75 1.15e-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: 43.29  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055645045  14 GSN-YLVKTEKYNILVDCGmfQGNEEMEklnynnfPY--------NPSEIDFLILTHAHIDHSGRIPKLVK 75
Cdd:cd07722    17 GTNtYLVGTGKRRILIDTG--EGRPSYI-------PLlksvldseGNATISDILLTHWHHDHVGGLPDVLD 78
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 15-66 2.54e-04

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: 42.04  E-value: 2.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2055645045  15 SNYLVKTEKYNILVDCgmfqGNEEMEKL-NYnnfpYNPSEIDFLILTHAHIDH 66
Cdd:cd07716    19 SGYLLEADGFRILLDC----GSGVLSRLqRY----IDPEDLDAVVLSHLHPDH 63
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-73 2.89e-04

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: 42.21  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   2 DIQFYGAAKMVTGSNYLVKTEKYNILVDCGMFQGNEEM-----------------------EKLNYNNFPYNPSEIDFLI 58
Cdd:cd07732     1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLDPESKyfdevldflelgllpdivglyrdPLLLGGLRSEEDPSVDAVL 80

                          90
                  ....*....|....*
gi 2055645045  59 LTHAHIDHSGRIPKL 73
Cdd:cd07732    81 LSHAHLDHYGLLNYL 95
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 18-90 3.48e-04

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 41.74  E-value: 3.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055645045  18 LVKTEKYNILVDCGMFQGNEEMEKLNYNNfPYNPSEIDFLILTHAHIDHSGRIPKLVKDgFR-GRIITTNATYD 90
Cdd:cd07731    14 LIQTPGKTILIDTGPRDSFGEDVVVPYLK-ARGIKKLDYLILTHPDADHIGGLDAVLKN-FPvKEVYMPGVTHT 85
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-89 3.91e-04

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.12  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMfqGN----EEMEKLNYNNFPY---------NPSEIDFLILTHAHIDHSGRIPKLVkdgfRGRII 83
Cdd:cd16277    16 WLVRTPGRTILVDTGI--GNdkprPGPPAFHNLNTPYlerlaaagvRPEDVDYVLCTHLHVDHVGWNTRLV----DGRWV 89


                  ....*...
gi 2055645045  84 TT--NATY 89
Cdd:cd16277    90 PTfpNARY 97
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 17-201 4.60e-04

Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; 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 GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 42.07  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMfQGNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKdgfrgriiTTNAtydlcKIMl 96
Cdd:cd16308    25 YLIVTPKGNILINTGL-AESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQ--------QTGA-----KMM- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  97 kdsakIQESDVewenrKRQRAGKKPIeplYTMKDAENSlkyFEPYFIDQKIKINDNIQI------RFKDAGHILGSAILE 170
Cdd:cd16308    90 -----VDEKDA-----KVLADGGKSD---YEMGGYGST---FAPVKADKLLHDGDTIKLggtkltLLHHPGHTKGSCSFL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2055645045 171 LWVREVNEEVKVVFSGD---------LGMPGRPIINSpDY 201
Cdd:cd16308   154 FDVKDEKRTYRVLIANMptilpdtklSGMPGYPGIAK-DY 192
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-68 4.80e-04

Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; 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 BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 42.09  E-value: 4.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQgNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSG 68
Cdd:cd16309    23 GVFLITTPEGHILIDGAMPQ-STPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAG 75
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-103 6.19e-04

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 41.80  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQGNEE-----MEKLNYNnfpynPSEIDFLILTHAHIDHSGRiPKLVKDGFRGRIITTNATY 89
Cdd:cd16280    23 SAWAIDTGDGLILIDALNNNEAADlivdgLEKLGLD-----PADIKYILITHGHGDHYGG-AAYLKDLYGAKVVMSEADW 96

                          90
                  ....*....|....
gi 2055645045  90 DLckiMLKDSAKIQ 103
Cdd:cd16280    97 DM---MEEPPEEGD 107
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-93 7.16e-04

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 41.48  E-value: 7.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2055645045  49 YNPSEIDFLILTHAHIDHSGRIpklvKDGFRGRIITTNATYDLCK 93
Cdd:cd07730    79 IDPEDIDAVILSHLHWDHIGGL----SDFPNARLIVGPGAKEALR 119
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-81 7.93e-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: 40.71  E-value: 7.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055645045  18 LVKTEKYNILVDCG--MFQGneeMEKLNYNnfpynPSEIDFLILTHAHIDHSGRIPKLVKDG--FRGR 81
Cdd:cd07740    20 HVASEAGRFLIDCGasSLIA---LKRAGID-----PNAIDAIFITHLHGDHFGGLPFFLLDAqfVAKR 79
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-76 8.45e-04

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 41.18  E-value: 8.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQGNEEMEKlNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKD 76
Cdd:cd16290    23 SAVLITSPQGLILIDGALPQSAPQIEA-NIRALGFRLEDVKLILNSHAHFDHAGGIAALQRD 83
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-76 8.66e-04

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; 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 Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 41.28  E-value: 8.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055645045  15 SNYLVKTEKYNILVDCGMFQGNEEMEKlNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLVKD 76
Cdd:cd16310    23 GSYLITSNHGAILLDGGLEENAALIEQ-NIKALGFKLSDIKIIINTHAHYDHAGGLAQLKAD 83
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 17-168 2.10e-03

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293851  Cd Length: 199  Bit Score: 39.43  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKYNILVDCGMfqgNEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSGRIPKLV-KDGFRGRIITTNATYDLCKIM 95
Cdd:cd16293    15 YLLEIDDVTILLDCGW---DESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVgKLGLTCPVYATLPVHKMGRMF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  96 LKD---SAKIQESdvewenrkrqragkkpiEPLYTMKDAE------NSLKYFEPYFIDQKikiNDNIQIRFKDAGHILGS 166
Cdd:cd16293    92 MYDlyqSRGLEED-----------------FNLFTLDDVDeafdriTQLKYSQPVNLRGK---GDGLTITAYNAGHTLGG 151


                  ..
gi 2055645045 167 AI 168
Cdd:cd16293   152 TI 153
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-86 2.40e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 39.48  E-value: 2.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2055645045  45 NNFPYNPSEIDFLILTHAHIDHSGRIPKLV----KDGF--RGRIITTN 86
Cdd:cd07741    45 CRPKLDPTKLDAIILSHRHLDHSNDANVLIeamtEGGFkkRGTLLAPE 92
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-66 2.47e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.52  E-value: 2.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055645045   1 MDIQFYGaakmvtGSNYLVKTEKYNILVDcGMFQGNEEMeklnYNNFPYNPSE---IDFLILTHAHIDH 66
Cdd:COG2220     4 MKITWLG------HATFLIETGGKRILID-PVFSGRASP----VNPLPLDPEDlpkIDAVLVTHDHYDH 61
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 18-76 3.18e-03

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: 39.46  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055645045  18 LVKT-EKYNILVDCGMFQGNEEMEK-----LNYNNFpynpSEIDFLILTHAHIDHSGRIPKLVKD 76
Cdd:COG2333    15 LIRTpDGKTILIDTGPRPSFDAGERvvlpyLRALGI----RRLDLLVLTHPDADHIGGLAAVLEA 75
NorV COG0426
Flavorubredoxin [Energy production and conversion];
17-107 3.57e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.81  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKyNILVDCG--MFQGN--EEMEKLnynnfpYNPSEIDFLILTHAHIDHSGRIPKLVKDGFRGRIITTNatydLC 92
Cdd:COG0426    37 YLIVDEK-TALIDTVgeSFFEEflENLSKV------IDPKKIDYIIVNHQEPDHSGSLPELLELAPNAKIVCSK----KA 105

                          90
                  ....*....|....*
gi 2055645045  93 KIMLKDSAKIQESDV 107
Cdd:COG0426   106 ARFLPHFYGIPDFRF 120
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 18-68 3.89e-03

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; 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 L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 39.03  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055645045  18 LVKTEKYNILVDCGMFQGnEEMEKLNYNNFPYNPSEIDFLILTHAHIDHSG 68
Cdd:cd16289    26 LVKTPDGAVLLDGGMPQA-ADMLLDNMRALGVAPGDLKLILHSHAHADHAG 75
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 5-73 3.92e-03

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 39.74  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045   5 FYGAA-KMVTGSNY---LVKTEKyNILVD------CGMFQGNEEME-KLNynnfpynpsEIDFLILTHAHIDHSGRIPKL 73
Cdd:PRK05452   22 FHGTEyKTLRGSSYnsyLIREEK-NVLIDtvdhkfSREFVQNLRNEiDLA---------DIDYIVINHAEEDHAGALTEL 91
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 17-98 4.73e-03

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: 39.01  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  17 YLVKTEKyNILVDCGMFQGNEE-MEKLNYNNfpyNPSEIDFLILTHAHIDHSGRIPKLVKDGFRGRIITTNATYDLCKIM 95
Cdd:cd07709    35 YLIKDEK-TALIDTVKEPFFDEfLENLEEVI---DPRKIDYIVVNHQEPDHSGSLPELLELAPNAKIVCSKKAARFLKHF 110


                  ...
gi 2055645045  96 LKD 98
Cdd:cd07709   111 YPG 113
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 14-125 5.36e-03

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: 38.93  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055645045  14 GSN-YLVKTEKYNILVDCGMFQGNEEMEKLNY--NNFPY---NPSEIDFLILTHAHIDHSGRIPKLVKDgFRGRIITTNA 87
Cdd:cd07714    10 GKNmYVVEYDDDIIIIDCGLKFPDEDMPGVDYiiPDFSYleeNKDKIKGIFITHGHEDHIGALPYLLPE-LNVPIYATPL 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2055645045  88 TYDLCKIMLKDSAKIQESD-VEWENRKRQRAGKKPIEPL 125
Cdd:cd07714    89 TLALIKKKLEEFKLIKKVKlNEIKPGERIKLGDFEVEFF 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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