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Conserved domains on  [gi|2089865772|ref|WP_222734468|]
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MBL fold metallo-hydrolase RNA specificity domain-containing protein [Vibrio fluvialis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-438 2.60e-165

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: 473.08  E-value: 2.60e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   1 MQLIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIESD----FPIEHIQALILTHAHIDHIGRLPWLIAAGFTG 76
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNdafpFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  77 PIYCTPATAELVPLMLDDGMKLQ---------SGFSRAQREVVL-------DKIDHLIePIEYEQRFRIESDsgvmLQCQ 140
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQeeeaeyankKRYSGHPPVEPLytekdveKALKHFI-TLDYGEVTDIAPD----IKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 141 FVPAGHILGSAYLEIQLPNQEV-IVFSGDLGPSNTPLLPDPVPPMHADYLVIETTYGDTHHDGVEERANKLREIIDRSLA 219
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGLHnIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 220 DGGTILIPAFSIGRTQELLFDIEQLVYEHQINaDLPIILDSPMAQKVTESYRRFKQLWGEEAKERLEMHRHPLAFDQCVL 299
Cdd:COG1782   236 RGGKVLIPAFAVGRTQEILYVLNELMREGKIP-EVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 300 VQDYRSHEALVNRlvstGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEGEEVE 379
Cdd:COG1782   315 VESVEESKEINDS----DEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIP 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 380 VNAQIHVMSGYSAHADQDDLLAFIEGIDEKPKEVHLIHGEQEAKQAFAQLLRDK-GYNVI 438
Cdd:COG1782   391 VRAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKlGIEVV 450
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-438 2.60e-165

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: 473.08  E-value: 2.60e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   1 MQLIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIESD----FPIEHIQALILTHAHIDHIGRLPWLIAAGFTG 76
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNdafpFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  77 PIYCTPATAELVPLMLDDGMKLQ---------SGFSRAQREVVL-------DKIDHLIePIEYEQRFRIESDsgvmLQCQ 140
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQeeeaeyankKRYSGHPPVEPLytekdveKALKHFI-TLDYGEVTDIAPD----IKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 141 FVPAGHILGSAYLEIQLPNQEV-IVFSGDLGPSNTPLLPDPVPPMHADYLVIETTYGDTHHDGVEERANKLREIIDRSLA 219
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGLHnIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 220 DGGTILIPAFSIGRTQELLFDIEQLVYEHQINaDLPIILDSPMAQKVTESYRRFKQLWGEEAKERLEMHRHPLAFDQCVL 299
Cdd:COG1782   236 RGGKVLIPAFAVGRTQEILYVLNELMREGKIP-EVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 300 VQDYRSHEALVNRlvstGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEGEEVE 379
Cdd:COG1782   315 VESVEESKEINDS----DEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIP 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 380 VNAQIHVMSGYSAHADQDDLLAFIEGIDEKPKEVHLIHGEQEAKQAFAQLLRDK-GYNVI 438
Cdd:COG1782   391 VRAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKlGIEVV 450
arCOG00543 TIGR03675
arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins ...
 7-437 2.09e-78

arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782.


Pssm-ID: 274718 [Multi-domain]  Cd Length: 630  Bit Score: 255.25  E-value: 2.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGL---FQGKDA---LDIEsDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYC 80
Cdd:TIGR03675 181 GGFREVGRSALLLSTPESRILLDCGVnvgADGDNAypyLDVP-EFDLDELDAVVITHAHLDHSGLVPLLFKYGYDGPVYC 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  81 TPATAELVPLMLDDGMKLQsgfSRAQREV------VLDKIDHLIePIEYEQRFRIESDsgvmLQCQFVPAGHILGSA--Y 152
Cdd:TIGR03675 260 TPPTRDLMVLLQLDYIDVA---QKEGKKPpysskdVREALKHTI-TLDYGEVTDIAPD----IKLTFYNAGHILGSAiaH 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 153 LEIQ--LPNqevIVFSGDLGPSNTPLLPDPVPPM-HADYLVIETTYG--DTHHDGVEERANKLREIIDRSLADGGTILIP 227
Cdd:TIGR03675 332 LHIGdgLYN---IVYTGDFKYEKTRLLDPAVNKFpRVETLIMESTYGgrDDYQPSREEAEKELIKVVNETIKRGGKVLIP 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 228 AFSIGRTQELLfdieqLVYEHQINADL----PIILDSpMAQKVTESYRRFKQLWGEEAKERLeMHR--HPLAFDQCVLVQ 301
Cdd:TIGR03675 409 VFAVGRAQEVM-----LVLEEAMRKGLipevPVYLDG-MIWEATAIHTAYPEYLNKELRERI-FHEgeNPFLSEIFVRVE 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 302 DYRSHEALVNrlvsTGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEG----EE 377
Cdd:TIGR03675 482 GSDERREIIE----SDEPAIILATSGMLNGGPVVEYLKLLAPDPRNSLVFVGYQAEGTLGRRIQSGWREIPLTDdgktET 557

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 378 VEVNAQIHVMSGYSAHADQDDLLAFIEGIDEKPKEVHLIHGEQEAKQAFAQLLRdKGYNV 437
Cdd:TIGR03675 558 IKINMEVETVDGFSGHSDRRQLMNYVRRMQPKPEKIILNHGEPSKCLDLASSIY-KKFKI 616
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-192 5.13e-73

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: 227.73  E-value: 5.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   3 LIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIES----DFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPI 78
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNnepfPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  79 YCTPATAELVPLMLDDGMKLQSGFSRAQREVVL------DKIDHLIEPIEYEQRFRIESDsgvmLQCQFVPAGHILGSAY 152
Cdd:cd16295    81 YATPATKDLAELLLLDSAKIQEEEAEHPPAEPLyteedvEKALKHFRPVEYGEPFEIGPG----VKVTFYDAGHILGSAS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2089865772 153 LEIQLPNQEVIVFSGDLGPSNTPLLPDPVPPMHADYLVIE 192
Cdd:cd16295   157 VELEIGGGKRILFSGDLGRKNTPLLRDPAPPPEADYLIME 196
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 234-364 4.73e-48

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: 160.40  E-value: 4.73e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  234 TQELLFDIEQLVYEHQInADLPIILDSPMAQKVTESYRRFKQLWGEEAKERLEMHRHPLAFDQCVLVQDYRSHEALVNRL 313
Cdd:smart01027   1 TQELLLILEELWREGEL-PNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLNDYK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2089865772  314 vstgEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAI 364
Cdd:smart01027  80 ----GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 234-362 1.83e-36

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: 129.56  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 234 TQELLFDIEQLVYEHQINaDLPIILDSPMAQKVTESYRRFKQLWGEEAKErlemhrhplafdqcvLVQDYRSHEALVNRl 313
Cdd:pfam10996   1 AQELLYLLDELWREGRLP-KIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------------FVISKSESKAINEG- 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2089865772 314 vstGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGR 362
Cdd:pfam10996  64 ---KGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
PRK02113 PRK02113
MBL fold metallo-hydrolase;
22-86 5.26e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 38.61  E-value: 5.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089865772  22 DDLAILVDCGlfqgkdaldieSDF-------PIEHIQALILTHAHIDHIGRLPWLIAAGFTG--PIYCTPATAE 86
Cdd:PRK02113   43 EGARILIDCG-----------PDFreqmlrlPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGevPIYAEQYVAE 105
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-438 2.60e-165

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: 473.08  E-value: 2.60e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   1 MQLIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIESD----FPIEHIQALILTHAHIDHIGRLPWLIAAGFTG 76
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNdafpFDPEELDAVVLTHAHLDHSGLLPLLVKYGYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  77 PIYCTPATAELVPLMLDDGMKLQ---------SGFSRAQREVVL-------DKIDHLIePIEYEQRFRIESDsgvmLQCQ 140
Cdd:COG1782    81 PIYCTPPTRDLMALLLLDSAKIQeeeaeyankKRYSGHPPVEPLytekdveKALKHFI-TLDYGEVTDIAPD----IKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 141 FVPAGHILGSAYLEIQLPNQEV-IVFSGDLGPSNTPLLPDPVPPMHADYLVIETTYGDTHHDGVEERANKLREIIDRSLA 219
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGLHnIVFSGDLGRGKTPLLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 220 DGGTILIPAFSIGRTQELLFDIEQLVYEHQINaDLPIILDSPMAQKVTESYRRFKQLWGEEAKERLEMHRHPLAFDQCVL 299
Cdd:COG1782   236 RGGKVLIPAFAVGRTQEILYVLNELMREGKIP-EVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 300 VQDYRSHEALVNRlvstGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEGEEVE 379
Cdd:COG1782   315 VESVEESKEINDS----DEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETIP 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 380 VNAQIHVMSGYSAHADQDDLLAFIEGIDEKPKEVHLIHGEQEAKQAFAQLLRDK-GYNVI 438
Cdd:COG1782   391 VRAEVETIDGFSGHADRNELLNWLRRLKPKPKKVFLVHGEPEAAEALASSIRKKlGIEVV 450
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-421 1.45e-156

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 448.48  E-value: 1.45e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   1 MQLIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIEsDFPIE--HIQALILTHAHIDHIGRLPWLIAAGFTGPI 78
Cdd:COG1236     1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWP-PFPFRpsDVDAVVLTHAHLDHSGALPLLVKEGFRGPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  79 YCTPATAELVPLMLDDGMKLQSgfSRAQREVVLDKID-----HLIEPIEYEQRFRIESdsgvmLQCQFVPAGHILGSAYL 153
Cdd:COG1236    80 YATPATADLARILLGDSAKIQE--EEAEAEPLYTEEDaeralELFQTVDYGEPFEIGG-----VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 154 EIQLPNqEVIVFSGDLGPSNTPLLPDPVPPMHADYLVIETTYGDTHHDGVEERANKLREIIDRSLADGGTILIPAFSIGR 233
Cdd:COG1236   153 ELEVGG-KRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 234 TQELLFDIEQLVYEHQINaDLPIILdSPMAQKVTESYRRFKQLWGEEAKErlemhrhPLAFDQCVLVQDYRSHEALVNRl 313
Cdd:COG1236   232 AQELLYLLRELKKEGRLP-DIPIYV-SGMAIRATEIYRRHGEYLRDEAQD-------PFALPNLRFVTSVEESKALNRK- 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 314 vstgEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEGEEVEVNAQIHVMSGYSAH 393
Cdd:COG1236   302 ----GPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEVPVRARVERLFGLSAH 377

                         410       420
                  ....*....|....*....|....*...
gi 2089865772 394 ADQDDLLAFIEGIdEKPKEVHLIHGEQE 421
Cdd:COG1236   378 ADWDELLEWIKAT-GKPERVFLVHGEPE 404
arCOG00543 TIGR03675
arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins ...
 7-437 2.09e-78

arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782.


Pssm-ID: 274718 [Multi-domain]  Cd Length: 630  Bit Score: 255.25  E-value: 2.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGL---FQGKDA---LDIEsDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYC 80
Cdd:TIGR03675 181 GGFREVGRSALLLSTPESRILLDCGVnvgADGDNAypyLDVP-EFDLDELDAVVITHAHLDHSGLVPLLFKYGYDGPVYC 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  81 TPATAELVPLMLDDGMKLQsgfSRAQREV------VLDKIDHLIePIEYEQRFRIESDsgvmLQCQFVPAGHILGSA--Y 152
Cdd:TIGR03675 260 TPPTRDLMVLLQLDYIDVA---QKEGKKPpysskdVREALKHTI-TLDYGEVTDIAPD----IKLTFYNAGHILGSAiaH 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 153 LEIQ--LPNqevIVFSGDLGPSNTPLLPDPVPPM-HADYLVIETTYG--DTHHDGVEERANKLREIIDRSLADGGTILIP 227
Cdd:TIGR03675 332 LHIGdgLYN---IVYTGDFKYEKTRLLDPAVNKFpRVETLIMESTYGgrDDYQPSREEAEKELIKVVNETIKRGGKVLIP 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 228 AFSIGRTQELLfdieqLVYEHQINADL----PIILDSpMAQKVTESYRRFKQLWGEEAKERLeMHR--HPLAFDQCVLVQ 301
Cdd:TIGR03675 409 VFAVGRAQEVM-----LVLEEAMRKGLipevPVYLDG-MIWEATAIHTAYPEYLNKELRERI-FHEgeNPFLSEIFVRVE 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 302 DYRSHEALVNrlvsTGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEG----EE 377
Cdd:TIGR03675 482 GSDERREIIE----SDEPAIILATSGMLNGGPVVEYLKLLAPDPRNSLVFVGYQAEGTLGRRIQSGWREIPLTDdgktET 557

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 378 VEVNAQIHVMSGYSAHADQDDLLAFIEGIDEKPKEVHLIHGEQEAKQAFAQLLRdKGYNV 437
Cdd:TIGR03675 558 IKINMEVETVDGFSGHSDRRQLMNYVRRMQPKPEKIILNHGEPSKCLDLASSIY-KKFKI 616
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-192 5.13e-73

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: 227.73  E-value: 5.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   3 LIHHGGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIES----DFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPI 78
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNnepfPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  79 YCTPATAELVPLMLDDGMKLQSGFSRAQREVVL------DKIDHLIEPIEYEQRFRIESDsgvmLQCQFVPAGHILGSAY 152
Cdd:cd16295    81 YATPATKDLAELLLLDSAKIQEEEAEHPPAEPLyteedvEKALKHFRPVEYGEPFEIGPG----VKVTFYDAGHILGSAS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2089865772 153 LEIQLPNQEVIVFSGDLGPSNTPLLPDPVPPMHADYLVIE 192
Cdd:cd16295   157 VELEIGGGKRILFSGDLGRKNTPLLRDPAPPPEADYLIME 196
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 234-364 4.73e-48

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: 160.40  E-value: 4.73e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  234 TQELLFDIEQLVYEHQInADLPIILDSPMAQKVTESYRRFKQLWGEEAKERLEMHRHPLAFDQCVLVQDYRSHEALVNRL 313
Cdd:smart01027   1 TQELLLILEELWREGEL-PNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRLNDYK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2089865772  314 vstgEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGRAI 364
Cdd:smart01027  80 ----GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 234-362 1.83e-36

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: 129.56  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 234 TQELLFDIEQLVYEHQINaDLPIILDSPMAQKVTESYRRFKQLWGEEAKErlemhrhplafdqcvLVQDYRSHEALVNRl 313
Cdd:pfam10996   1 AQELLYLLDELWREGRLP-KIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------------FVISKSESKAINEG- 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2089865772 314 vstGEASIVVAASGMCEGGRIVDYLKALLPDPRTDVIFAGFQAEGTLGR 362
Cdd:pfam10996  64 ---KGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 7-192 1.88e-32

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: 121.67  E-value: 1.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGLFQGKDalDIESDFP-----IEHIQALILTHAHIDHIGRLPWLIA-AGFTGPIYC 80
Cdd:cd07734     4 GGGQEVGRSCFLVEFKGRTVLLDCGMNPGKE--DPEACLPqfellPPEIDAILISHFHLDHCGALPYLFRgFIFRGPIYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  81 TPATAELVPLMLDDGMKLQSGFSRAQR----EVVLDKIDHlIEPIEYEQRFRIesDSGVMLQCQFvpAGHILGSAYLEIQ 156
Cdd:cd07734    82 THPTVALGRLLLEDYVKSAERIGQDQSlytpEDIEEALKH-IVPLGYGQSIDL--FPALSLTAYN--AGHVLGAAMWEIQ 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2089865772 157 LpNQEVIVFSGDLgpSNTP---LLPDPVPPMHADYLVIE 192
Cdd:cd07734   157 I-YGEKLVYTGDF--SNTEdrlLPAASILPPRPDLLITE 192
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 7-192 1.14e-19

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: 86.49  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGL---FQGKDALDIESDFPIEHIQALILTHAHIDHIGRLPWLIA-AGFTGPIYCTP 82
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIhpgYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQkTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  83 ATAELVPLMLDDGMKLQSGFSRAQ--REVVLDKIDHLIEPIEYEQRFRIesdSGVMLQCqfVPAGHILGSAYLEIQLPNQ 160
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMlyTETDLEASMDKIETIDFHQEVEV---NGIKFTA--YNAGHVLGAAMFMVEIAGV 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2089865772 161 EvIVFSGDLGPSNT-PLLPDPVPPMHADYLVIE 192
Cdd:cd16292   162 R-VLYTGDYSREEDrHLPAAEIPPIKPDVLIVE 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-193 2.52e-19

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 84.91  E-value: 2.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   15 SCHELVVDDLAILVDCGLFQGKDALDIESDFPIEHIQALILTHAHIDHIGRLPWLIAAgFTGPIYCTPATAELvplmldd 94
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAEL------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   95 gmkLQSGFSRAQREVVLDKIDHLIEPIEYEQRFRIESDSgvmLQCQFVPaGHILGSAYLEIqlpNQEVIVFSGDLGPSNT 174
Cdd:smart00849  73 ---LKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGE---LEVIHTP-GHTPGSIVLYL---PEGKILFTGDLLFAGG 142

                          170
                   ....*....|....*....
gi 2089865772  175 PLLPDPVPPMHADYLVIET 193
Cdd:smart00849 143 DGRTLVDGGDAAASDALES 161
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-179 1.71e-16

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: 77.69  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGLFQGKDAldiESDFP-----------IEHIQALILTHAHIDHIGRLPWLI-AAGF 74
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYND---ERRFPdfsyisqngpfTEHIDCVIISHFHLDHCGALPYFTeVVGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  75 TGPIYCTPATAELVPLMLDDGMKLQSGFSRAQREVVLDKIDHLIE---PIEYEQRFRIESDsgvmLQCQFVPAGHILGSA 151
Cdd:cd16291    82 DGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKkviAVNLHETVQVDDE----LEIKAYYAGHVLGAA 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2089865772 152 YLEIQLPNQEViVFSGD--------LGPSNTP-LLPD 179
Cdd:cd16291   158 MFYVRVGDESV-VYTGDynmtpdrhLGAAWIDrLRPD 193
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 377-438 3.59e-15

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: 69.57  E-value: 3.59e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089865772 377 EVEVNAQIHVMSGYSAHADQDDLLAFIEGIdeKPKEVHLIHGEQEAKQAFAQLLRDK-GYNVI 438
Cdd:pfam07521   1 GIPVRARIETIDGFSGHADRRELLELIKGL--KPKPIVLVHGEPRALLALAELLKEElGIEVF 61
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-163 4.47e-13

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: 67.55  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGLFQGKDALDIES-DFPIEHIQALILTHAHIDHIGRLPWLIAA-GFTGPIYCTPAT 84
Cdd:cd16293     5 SGAGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESlKRIAPTIDAVLLSHPDLEHLGALPYLVGKlGLTCPVYATLPV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  85 AELVPL-MLDD--GMKLQSGFSRAQREVVLDKIDHlIEPIEYEQRFRIES-DSGVMLQCqfVPAGHILGSAYLEIQLPNQ 160
Cdd:cd16293    85 HKMGRMfMYDLyqSRGLEEDFNLFTLDDVDEAFDR-ITQLKYSQPVNLRGkGDGLTITA--YNAGHTLGGTIWKITKDSE 161


                  ...
gi 2089865772 161 EVI 163
Cdd:cd16293   162 DIV 164
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
15-206 7.46e-12

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 65.22  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  15 SCHELVVDDLAILVDCG-----LFQgkdaldiESDFPIEHIQALILTHAHIDHIGRLPWLIAA----GFTGP--IYCTPA 83
Cdd:COG1234    20 SSYLLEAGGERLLIDCGegtqrQLL-------RAGLDPRDIDAIFITHLHGDHIAGLPGLLSTrslaGREKPltIYGPPG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  84 TAELVplmlddgmklqsgfsRAQREVVLDKIDHLIEPIEYEQRFRIEsDSGVMLQCqfVPAGHILGS-AYLeIQLPNQeV 162
Cdd:COG1234    93 TKEFL---------------EALLKASGTDLDFPLEFHEIEPGEVFE-IGGFTVTA--FPLDHPVPAyGYR-FEEPGR-S 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2089865772 163 IVFSGDLGPSNT--PLLPDpvppmhADYLVIETTYGDTHHDGVEER 206
Cdd:COG1234   153 LVYSGDTRPCEAlvELAKG------ADLLIHEATFLDEEAELAKET 192
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 14-172 5.51e-11

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 61.38  E-value: 5.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  14 GSCHELVVDDLAILVDCGLfqGkdALD--IESDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTG------PIYCTPATA 85
Cdd:cd07719    18 GPSTLVVVGGRVYLVDAGS--G--VVRrlAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAgrktplPVYGPPGTR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  86 ELVPLmLDDGMKLQSGFSRAQREVVLDKIDHLIEPIEYEQRFRIESDSGVMLQCQFVPAGHILGS-AYlEIQLPNQeVIV 164
Cdd:cd07719    94 ALVDG-LLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDDGVKVTAFLVDHGPVPPAlAY-RFDTPGR-SVV 170


                  ....*...
gi 2089865772 165 FSGDLGPS 172
Cdd:cd07719   171 FSGDTGPS 178
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-215 6.47e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 61.23  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  14 GSCHELVVDDLAILVDCGLFQGKDALDIES--DFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCtpatAELVPLM 91
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLLLAalGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV----AEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  92 LDDGmkLQSGFSRAQREVVLDKIDHLIEPIEYEQRFRIESDSGVmlqcqfVPAGHILGSAYLEIQLPNQEViVFSGDLGP 171
Cdd:pfam00753  82 LDEE--LGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLL------VTHGPGHGPGHVVVYYGGGKV-LFTGDLLF 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2089865772 172 SNTPLLPDPVPPMHADYlviettygdtHHDGVEERANKLREIID 215
Cdd:pfam00753 153 AGEIGRLDLPLGGLLVL----------HPSSAESSLESLLKLAK 186
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 21-168 8.90e-11

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: 62.04  E-value: 8.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  21 VDDLAILVDCGL-FQGKDALDIES---DFP--IEH---IQALILTHAHIDHIGRLPWLIAAGFTgPIYCTPATAELVplm 91
Cdd:cd07714    18 YDDDIIIIDCGLkFPDEDMPGVDYiipDFSylEENkdkIKGIFITHGHEDHIGALPYLLPELNV-PIYATPLTLALI--- 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2089865772  92 lddgmKlqsgfSRAQREVVLDKIDhlIEPIEYEQRFRIESdsgvmLQCQFVPAGH-ILGSAYLEIQLPNQeVIVFSGD 168
Cdd:cd07714    94 -----K-----KKLEEFKLIKKVK--LNEIKPGERIKLGD-----FEVEFFRVTHsIPDSVGLAIKTPEG-TIVHTGD 153
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-179 7.03e-10

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: 58.07  E-value: 7.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  19 LVVDDL--AILVDCGLFQGKDALDIESDFPiEHIQALILTHAHIDHIGRLPWLiAAGFTGPIYCTPATAElvplMLDDGM 96
Cdd:cd06262    14 LVSDEEgeAILIDPGAGALEKILEAIEELG-LKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHEADAE----LLEDPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  97 KLQSGFSRAqrEVVLDKIDHLIEPieyEQRFRIEsdsGVMLQCQFVP---AGHIlgSAYLEiqlpnQEVIVFSGDLGPSN 173
Cdd:cd06262    88 LNLAFFGGG--PLPPPEPDILLED---GDTIELG---GLELEVIHTPghtPGSV--CFYIE-----EEGVLFTGDTLFAG 152


                  ....*.
gi 2089865772 174 TPLLPD 179
Cdd:cd06262   153 SIGRTD 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 7-199 7.80e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 59.14  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGLfqgkDALDIESDFP--IEHIQALILTHAHIDHIGRLPWLIAAGFTG--PIYCTP 82
Cdd:COG1235    28 DPRYGRTRSSILVEADGTRLLIDAGP----DLREQLLRLGldPSKIDAILLTHEHADHIAGLDDLRPRYGPNpiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  83 ATAELvplmlddgmkLQSGFSRAQREvVLDKIDhlIEPIEYEQRFRIESdsgvmLQCQFVPAGHILGSAY-LEIQLPNQe 161
Cdd:COG1235   104 GTLEA----------LERRFPYLFAP-YPGKLE--FHEIEPGEPFEIGG-----LTVTPFPVPHDAGDPVgYRIEDGGK- 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2089865772 162 VIVFSGDLGPsntplLPDPVPPM--HADYLVIETTYGDTH 199
Cdd:COG1235   165 KLAYATDTGY-----IPEEVLELlrGADLLILDATYDDPE 199
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 46-195 1.58e-09

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


Pssm-ID: 293831  Cd Length: 160  Bit Score: 56.39  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  46 PIEHIQALILTHAHIDHIGRL--PWLiaagfTGPIYCTPATAELVPLMLddgmklqsgfsraqrevvldKID-HLIEPIE 122
Cdd:cd16273    33 KIPGISAYFLSHFHSDHYGGLtkSWS-----HGPIYCSEITANLVKLKL--------------------KVDeEYIVVLP 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089865772 123 YEQRFRIESDSGVMLqcqfVPAGHILGSAYLEIQLPNQEVIVFSGDLgPSNTPLLPDPVP--PMHADYLVIETTY 195
Cdd:cd16273    88 MNTPVEIDGDVSVTL----LDANHCPGAVMFLFELPDGRRILHTGDF-RANPEMLEHPLLlgKRRIDTVYLDTTY 157
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 7-435 2.90e-09

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


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   7 GGKQTVTGSCHELVVDDLAILVDCGLFQGKDALD-----IESDFPIEHIQ----ALILTHAHIDHIGRLPWLIAAGFTGP 77
Cdd:TIGR00649   7 GGLGEIGKNMYVVEIDDEIVIFDAGILFPEDEMLgvdgvIPDFTYLQENEdkvkGIFITHGHEDHIGAVPYLLHQVGFFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  78 IYCTPATAELVPLMLDdgmklQSGFSRAQREVVLdkidHLIEPIEYEQRFRIEsdsgvmlqcqFVPAGH-ILGSAYLEIQ 156
Cdd:TIGR00649  87 IYGTPLTIALIKSKIK-----EHGLNVRTDLLEI----HEGEPVEFGENTAIE----------FFRITHsIPDSVGFALH 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 157 LPNQeVIVFSGDLGPSNTPLLPDPvppmhADY-----------LVIETTYGDTHHDGVEERANKLREIIDRSLAD-GGTI 224
Cdd:TIGR00649 148 TPLG-YIVYTGDFKFDNTPVIGEP-----PDLnriaeigkkgvLCLISDSTNVENPGFTPSEAKVLEQLNDIFKNaDGRI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 225 LIPAFS--IGRTQELLfdieqlvyEHQINADLPIILDSPMAQKVTESYRRFKQLwgeeakerlemHRHPLAFDQCVLVQD 302
Cdd:TIGR00649 222 IVATFAsnIHRVQQLI--------QIARKNGRKVAVYGRSMESLIGIARRLGYI-----------KCPHNNFISLKEINN 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772 303 YRSHEALVNRLVSTGEASIVVAASGMCEGGRIvDYlkallpDPRTDVIFAGFQAEGTLGRAIKQGDKVVMIEgEEVEVNA 382
Cdd:TIGR00649 283 SPDENYLIITTGSQGEPMAALTRIANGEHRQI-RI------RPGDTVVFSAPPIPGNENIAVSITLDIRLNR-AGARVIK 354

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2089865772 383 QIHVmSGYSAHADQDDLLAFIegideKPKEVHLIHGEQEAKQAFAQLLRDKGY 435
Cdd:TIGR00649 355 GIHV-SGHASQEDHKLMLRLL-----KPKYIIPVHGEYRMLKNHTKLAEEEGY 401
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-172 4.92e-09

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: 55.35  E-value: 4.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  14 GSCHELVVDDLAILVDCG---LFQgkdaLDiESDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGP------IYCTPAT 84
Cdd:cd16272    17 TSSYLLETGGTRILLDCGegtVYR----LL-KAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGrkkpltIYGPKGI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  85 AELVPLMLDDGmklqsgfsraqREVVLDKIDHLIEPIEYEQRFRIESDsgvmLQCQFVPAGHILGSAYLEIQLPNQeVIV 164
Cdd:cd16272    92 KEFLEKLLNFP-----------VEILPLGFPLEIEELEEGGEVLELGD----LKVEAFPVKHSVESLGYRIEAEGK-SIV 155


                  ....*...
gi 2089865772 165 FSGDLGPS 172
Cdd:cd16272   156 YSGDTGPC 163
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
21-88 2.76e-08

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 55.84  E-value: 2.76e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089865772  21 VDDLAILVDCGL-FQGKDALDIESDFP--------IEHIQALILTHAHIDHIGRLPWLIAAgFTGPIYCTPATAELV 88
Cdd:COG0595    26 YDDDIIIVDCGLkFPEDEMPGVDLVIPdisyleenKDKIKGIVLTHGHEDHIGALPYLLKE-LNVPVYGTPLTLALL 101
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
22-201 5.63e-07

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 51.11  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  22 DDLAILVDCG-LFQG------KDALDIESDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCTPATAELV------ 88
Cdd:COG5212    38 SDDYVLLDAGtVVSGlelaeqKGAFKGRQGYVLEHIKGYLISHAHLDHIAGLPILSPDDSPKTIYALPETIDALrnhyfn 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  89 ----PLMLDDGMKLQSGFSRaqrevvldkidhlIEPIEYEQRFRIEsdsGVMLQCQFVPAGH-ILGSAYLeIQLPNqEVI 163
Cdd:COG5212   118 wviwPDFTDIGSAPHLPKYR-------------YVPLKPGQTFPLG---GTGLRVTAFPLSHsVPSSAFL-IESGG-GAF 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2089865772 164 VFSGDLGP---SNTPLLPD------PVPPMHA-DYLVIETTYGDTHHD 201
Cdd:COG5212   180 LYSGDTGPdevEKSTNLDAlwealaPLVRSKKlKAIIIEVSFPNEQPD 227
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-88 8.75e-07

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: 49.14  E-value: 8.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089865772  19 LVVDDL-AILVDCGL-FQGKDALDI--ESDFPIEHIQALILTHAHIDHIGRLPWLIAAgfTG-PIYCTPATAELV 88
Cdd:cd07721    15 LIEDDDgLTLIDTGLpGSAKRILKAlrELGLSPKDIRRILLTHGHIDHIGSLAALKEA--PGaPVYAHEREAPYL 87
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 6-169 9.30e-07

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: 49.15  E-value: 9.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772   6 HGGKQTVTGSCHELVVDDLAILVDCGLfqgkdALDIESDFPIEHIQ--------------------------------AL 53
Cdd:cd07732     5 HRGTNEIGGNCIEVETGGTRILLDFGL-----PLDPESKYFDEVLDflelgllpdivglyrdplllgglrseedpsvdAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  54 ILTHAHIDHIGRLPWL---IaagftgPIYCTPATAELvplmlddgMKLQSGFSRAQrevvlDKIDHLIEPIEYEQRFRIE 130
Cdd:cd07732    80 LLSHAHLDHYGLLNYLrpdI------PVYMGEATKRI--------LKALLPFFGEG-----DPVPRNIRVFESGKSFTIG 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2089865772 131 SdsgvmLQCQFVPAGH-ILGSAYLEIQLPNqEVIVFSGDL 169
Cdd:cd07732   141 D-----FTVTPYLVDHsAPGAYAFLIEAPG-KRIFYTGDF 174
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-189 2.77e-06

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: 48.15  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  19 LVVDDLAILVDCGlFQGKDALDI-----ESDFPIEHIqalILTHAHIDHIGRLPWLiAAGFTGPIYCTPATAELvplmld 93
Cdd:COG0491    20 IVGGDGAVLIDTG-LGPADAEALlaalaALGLDIKAV---LLTHLHPDHVGGLAAL-AEAFGAPVYAHAAEAEA------ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  94 dgmkLQSGFSRAQREVVLDKIDHLIEPieyEQRFRIEsdsGVMLQCQFVPaGHILGSAYLEIQlpnQEVIVFSGDLGPSN 173
Cdd:COG0491    89 ----LEAPAAGALFGREPVPPDRTLED---GDTLELG---GPGLEVIHTP-GHTPGHVSFYVP---DEKVLFTGDALFSG 154

                         170
                  ....*....|....*.
gi 2089865772 174 TPLLPDPVPPMHADYL 189
Cdd:COG0491   155 GVGRPDLPDGDLAQWL 170
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-86 3.08e-06

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 47.69  E-value: 3.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089865772  26 ILVDCG--LFQGKDALDIESDFPIEHIQALILTHAHIDHIGRLPwLIAAGFTGPIYCTPATAE 86
Cdd:pfam12706   3 ILIDPGpdLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLL-DLREGRPRPLYAPLGVLA 64
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 22-201 6.12e-06

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 47.59  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  22 DDLAILVDCG----------LFQGKDALDIESDFPI-EHIQALILTHAHIDHIGRLPWLIAAGFTG-----PIYCTPATA 85
Cdd:cd07735    27 SDGDILLDAGtgvgalsleeMFNDILFPSQKAAYELyQRIRHYLITHAHLDHIAGLPLLSPNDGGQrgspkTIYGLPETI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  86 ElvplMLDDGM----------KLQSGFSRAQRevvldkidhlIEPIEYEQRFRIESDSGVMLqcqfvPAGH--ILGSAYL 153
Cdd:cd07735   107 D----ALKKHIfnwviwpdftSIPSGKYPYLR----------LEPIEPEYPIALTGLSVTAF-----PVSHgvPVSTAFL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2089865772 154 eIQLPNQEvIVFSGDLGP---SNTPLLPD------PVPPMHADYLVIETTYGDTHHD 201
Cdd:cd07735   168 -IRDGGDS-FLFFGDTGPdsvSKSPRLDAlwralaPLIPKKLKAIIIECSFPNSRPD 222
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 13-86 8.97e-06

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: 45.33  E-value: 8.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089865772  13 TGSCHELVVDDLAILVDCGL-FQGKDALDIESDFPIEHIQALILTHAHIDHIGRLPwLIAAGFTGPIYCTPATAE 86
Cdd:cd07733     8 KGNCTYLETEDGKLLIDAGLsGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLG-VLARKYNVPIYATAGTLR 81
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 21-86 2.47e-05

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 44.77  E-value: 2.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089865772  21 VDDLAILVDCGlfqgKD----ALDiesdFPIEHIQALILTHAHIDHIGRL----PWLIAAGFTGPIYCTPATAE 86
Cdd:cd16279    42 TGGKNILIDTG----PDfrqqALR----AGIRKLDAVLLTHAHADHIHGLddlrPFNRLQQRPIPVYASEETLD 107
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 26-170 2.70e-05

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: 44.83  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  26 ILVDCGlfQGKDALD--IES---DFPIEHIQALILTHAHIDHIGRLPWLIAAgFTGP---IYctpataelvplmlddgmK 97
Cdd:cd07722    30 ILIDTG--EGRPSYIplLKSvldSEGNATISDILLTHWHHDHVGGLPDVLDL-LRGPsprVY-----------------K 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2089865772  98 LQSGFSRAQrevvLDKIDHLIEPIEYEQRFRIEsdsGVMLQCQFVP---AGHIlgSAYLEiqlpnQEVIVFSGD--LG 170
Cdd:cd07722    90 FPRPEEDED----PDEDGGDIHDLQDGQVFKVE---GATLRVIHTPghtTDHV--CFLLE-----EENALFTGDcvLG 153
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 19-163 3.94e-05

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 44.12  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  19 LVVDDLAILVDCGLFQGKDALDIeSDFPIEHIQ---ALILTHAHIDHIGRLPWLIAA-----GFTGPIYCTPATAEL--V 88
Cdd:pfam16661   2 LEFDNVRILLDPGWDGSFSYESD-LKYLEKILPevdLILLSHPTLEHLGAYPLLYYKfgshlGSNIPVYATLPVANLgrV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  89 pLMLDD----GMKLQSGFSraqrEVVLDKIDH---LIEPIEYEQRFRIES-DSGVMLqcqfVP--AGHILGSAYLEIQLP 158
Cdd:pfam16661  81 -STYDLyasrGILGPYDSS----ELDLDDIDAafdKIKTLKYSQTVDLKGkFDGLTI----TPynSGHTLGGTIWKISKN 151


                  ....*
gi 2089865772 159 NQEVI 163
Cdd:pfam16661 152 SEKIV 156
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 25-72 2.58e-04

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: 42.54  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2089865772  25 AILVDCGlfqGKDALDIESD--------FPIEHIQALILTHAHIDHIGRLPWLIAA 72
Cdd:COG2333    23 TILIDTG---PRPSFDAGERvvlpylraLGIRRLDLLVLTHPDADHIGGLAAVLEA 75
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 16-82 5.52e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 40.68  E-value: 5.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2089865772  16 CHELVVDDLAILVDCGLfqgkdaLDIESDFPIEHIQALILTHAHIDHI-GRLPWLIAAGFTGPIYCTP 82
Cdd:cd07736    39 SALIEVDGERILLDAGL------TDLAERFPPGSIDAILLTHFHMDHVqGLFHLRWGVGDPIPVYGPP 100
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-192 7.49e-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: 40.32  E-value: 7.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  26 ILVDCG--LFQGKDALDIESDfpieHIQALILTHAHIDHIGRLPWLI--AAGFTG-----PIYCTPATAELVPLMLDdgm 96
Cdd:cd07740    28 FLIDCGasSLIALKRAGIDPN----AIDAIFITHLHGDHFGGLPFFLldAQFVAKrtrplTIAGPPGLRERLRRAME--- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  97 KLQSGFSRAQRevvldKIDhlIEPIEYEQRFRIESDSgvmLQCQFVPAGHI--LGSAYLEIqLPNQEVIVFSGDLGPSNT 174
Cdd:cd07740   101 ALFPGSSKVPR-----RFD--LEVIELEPGEPTTLGG---VTVTAFPVVHPsgALPLALRL-EAAGRVLAYSGDTEWTDA 169

                         170
                  ....*....|....*...
gi 2089865772 175 pLLPdpvPPMHADYLVIE 192
Cdd:cd07740   170 -LVP---LARGADLFICE 183
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 13-85 8.36e-04

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: 40.55  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  13 TGSCHELVVDDLAILVDCG-------LFQGKDALDIEsdfpIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCTPATA 85
Cdd:cd07726    15 RIASYLLDGEGRPALIDTGpsssvprLLAALEALGIA----PEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGA 90
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-88 1.01e-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) 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: 40.71  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2089865772  35 GKDALDI--ESDFPIEHIQALILTHAHIDHIGRLPWLIAAgftgPIYCTPATAELV 88
Cdd:cd07730    67 EEDVAEQlaAGGIDPEDIDAVILSHLHWDHIGGLSDFPNA----RLIVGPGAKEAL 118
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 26-82 1.33e-03

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: 40.30  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089865772  26 ILVDCG----LFQGKDALDIesdfPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCTP 82
Cdd:cd07713    32 ILFDTGqsgvLLHNAKKLGI----DLSDIDAVVLSHGHYDHTGGLKALLELNPKAPVYAHP 88
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 25-87 2.39e-03

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 39.25  E-value: 2.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089865772  25 AILVDCGlFQGKDALDIESDFPIEhIQALILTHAHIDHIGRLPWLIAAgfTG-PIYCTPATAEL 87
Cdd:cd16322    24 AVLVDPG-DESEKLLARFGTTGLT-LLYILLTHAHFDHVGGVADLRRH--PGaPVYLHPDDLPL 83
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 19-89 2.46e-03

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 39.19  E-value: 2.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089865772  19 LVVDDLAILVDC--GLFQGKDALD-IESDFPIEhIQALILTHAHIDHIGRLPWLIAAGFtgPIYCTPATAELVP 89
Cdd:cd16285    31 VIDGKGLVLIDTpwTEAQTATLLDwIEKKLGKP-VTAAISTHSHDDRTGGIKALNARGI--PTYATALTNELAK 101
PRK02113 PRK02113
MBL fold metallo-hydrolase;
22-86 5.26e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 38.61  E-value: 5.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089865772  22 DDLAILVDCGlfqgkdaldieSDF-------PIEHIQALILTHAHIDHIGRLPWLIAAGFTG--PIYCTPATAE 86
Cdd:PRK02113   43 EGARILIDCG-----------PDFreqmlrlPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGevPIYAEQYVAE 105
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-169 5.40e-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) 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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 37.93  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  19 LVV-DDLAILVDCG--LFQGKDALD-IESDFPiEHIQALILTHAHIDHigrlpWLIAAGFTG---PIYCTPATAElvpLM 91
Cdd:cd16282    19 FIVgDDGVVVIDTGasPRLARALLAaIRKVTD-KPVRYVVNTHYHGDH-----TLGNAAFADagaPIIAHENTRE---EL 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2089865772  92 LDDGMKLQSGFSRAQREVvlDKIDHLIEP-IEYEQRFRIESDsGVMLQCQFVPAGHILGSAYLEiqLPNQEViVFSGDL 169
Cdd:cd16282    90 AARGEAYLELMRRLGGDA--MAGTELVLPdRTFDDGLTLDLG-GRTVELIHLGPAHTPGDLVVW--LPEEGV-LFAGDL 162
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 47-195 5.54e-03

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 37.50  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089865772  47 IEHIQALILTHAHIDHIGRLpwliAAGFTGPIYCTPATAELVplmlDDGMKLQSGFsraqrevvldkIDHLiePIEYEQr 126
Cdd:cd16298    34 IEGCTAYFLTHFHSDHYCGL----TKKFKFPIYCSKITGNLV----KSKLKVEEQY-----------INVL--PMNTEC- 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089865772 127 frIESDSGVMLqcqfVPAGHILGSAYLEIQLPNQEVIVFSGDL--GPS--NTPLLPDpvPPMHADYLviETTY 195
Cdd:cd16298    92 --IVNGVKVVL----LDANHCPGAVMILFRLPSGTLVLHTGDFraDPSmeRYPELIG--QKIHTLYL--DTTY 154
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-64 7.36e-03

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 37.51  E-value: 7.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2089865772  22 DDLAILVDCGL-----FQGKDALDIESdfpiEHIQALILTHAHIDHIG 64
Cdd:cd07743    17 DKEALLIDSGLdedagRKIRKILEELG----WKLKAIINTHSHADHIG 60
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
21-82 7.74e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 37.94  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2089865772  21 VDDLAILVDCGlfQGK------DALDIEsdfpIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCTP 82
Cdd:COG1237    29 TEGKRILFDTG--QSDvllknaEKLGID----LSDIDAVVLSHGHYDHTGGLPALLELNPKAPVYAHP 90
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 40-81 9.41e-03

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 38.20  E-value: 9.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2089865772  40 DIESDFPIEHIQALILTHAHIDHIGRLPWLIAAGFTGPIYCT 81
Cdd:PRK05452   62 NLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCT 103
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 47-72 9.97e-03

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.11  E-value: 9.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 2089865772  47 IEHIQALILTHAHIDHIGRLPWLIAA 72
Cdd:cd07731    46 IKKLDYLILTHPDADHIGGLDAVLKN 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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