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Conserved domains on  [gi|124505029|ref|XP_001351256|]
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cleavage and polyadenylation specificity factor, putative [Plasmodium falciparum 3D7]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440939)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme; similar to Thermus thermophilus ribonuclease TTHA0252, which exhibits endoribonuclease activity towards 23S and 16S rRNA in vitro and may function in RNA degradation

CATH:  3.60.15.30
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|11471246
SCOP:  3001057

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 11-551 7.37e-84

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 277.07  E-value: 7.37e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKdERKYPNFnllirgPDKINHcqkeefiddeieenieddeieenvn 90
Cdd:COG1236     3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGK-ERNWPPF------PFRPSD------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkrineiI 170
Cdd:COG1236    51 -------------------------------------------------------------------------------V 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTeILKYRGIILMSYPTKALSPILLLDScrvtdmkwekknferqIKMLNEKSDELLNYNinc 250
Cdd:COG1236    52 DAVVLTHAHLDHSGALPLLV-KEGFRGPIYATPATADLARILLGDS----------------AKIQEEEAEAEPLYT--- 111

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  251 ikkdpwninEDNIYNCIDKVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANIPS 330
Cdd:COG1236   112 ---------EEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVP 182

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  331 lNPEIFISESTYATYVRPTKKASELELCNLVHECVHKGGKVLIPVFAIGRAQELSILLDDYWKKMKI-HYPIYFGcGLTE 409
Cdd:COG1236   183 -PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYLLRELKKEGRLpDIPIYVS-GMAI 260

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  410 NANKYYKIYSSWINsscmsNEKENLFDFANISpFLNNY-----LNEKRPMVLFATPGMLHTGLSLKAFKAWAGNPQNLIV 484
Cdd:COG1236   261 RATEIYRRHGEYLR-----DEAQDPFALPNLR-FVTSVeeskaLNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTIL 334

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124505029  485 LPGYCVQGTVGHKLIMGEKQISLDGtTYIKVLCKI-IYLSFSAHADSNGIQQLIKHVS-PKNVIFVHGE 551
Cdd:COG1236   335 FVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVeRLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
 
Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 11-551 7.37e-84

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 277.07  E-value: 7.37e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKdERKYPNFnllirgPDKINHcqkeefiddeieenieddeieenvn 90
Cdd:COG1236     3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGK-ERNWPPF------PFRPSD------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkrineiI 170
Cdd:COG1236    51 -------------------------------------------------------------------------------V 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTeILKYRGIILMSYPTKALSPILLLDScrvtdmkwekknferqIKMLNEKSDELLNYNinc 250
Cdd:COG1236    52 DAVVLTHAHLDHSGALPLLV-KEGFRGPIYATPATADLARILLGDS----------------AKIQEEEAEAEPLYT--- 111

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  251 ikkdpwninEDNIYNCIDKVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANIPS 330
Cdd:COG1236   112 ---------EEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVP 182

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  331 lNPEIFISESTYATYVRPTKKASELELCNLVHECVHKGGKVLIPVFAIGRAQELSILLDDYWKKMKI-HYPIYFGcGLTE 409
Cdd:COG1236   183 -PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYLLRELKKEGRLpDIPIYVS-GMAI 260

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  410 NANKYYKIYSSWINsscmsNEKENLFDFANISpFLNNY-----LNEKRPMVLFATPGMLHTGLSLKAFKAWAGNPQNLIV 484
Cdd:COG1236   261 RATEIYRRHGEYLR-----DEAQDPFALPNLR-FVTSVeeskaLNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTIL 334

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124505029  485 LPGYCVQGTVGHKLIMGEKQISLDGtTYIKVLCKI-IYLSFSAHADSNGIQQLIKHVS-PKNVIFVHGE 551
Cdd:COG1236   335 FVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVeRLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 11-340 4.87e-80

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: 258.73  E-value: 4.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKDERKYPNFNLLIRGPdkinhcqkeefiddeieenieddeieenvn 90
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNG------------------------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkRINEII 170
Cdd:cd16291    51 --------------------------------------------------------------------------PFTEHI 56

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVT-DMKWEKKNFErqikmlneksdellnynin 249
Cdd:cd16291    57 DCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFT------------------- 117

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  250 cikkdpwninEDNIYNCIDKVIGLQINETFELG-DMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANI 328
Cdd:cd16291   118 ----------SQMIKDCMKKVIAVNLHETVQVDdELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWI 187

                         330
                  ....*....|..
gi 124505029  329 PSLNPEIFISES 340
Cdd:cd16291   188 DRLRPDLLITES 199
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 381-498 2.61e-33

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: 124.57  E-value: 2.61e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029    381 AQELSILLDDYWKKMKIH-YPIYFGCGLTENANKYYKIYSSWINSSC--MSNEKENLFDFANISPFLNN-----YLNEKR 452
Cdd:smart01027    1 TQELLLILEELWREGELPnVPIYLDSPMAARATEIYKSYPEWMSDEIrkRFEQGRNPFDFKNLKFVKSLeeskrLNDYKG 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 124505029    453 PMVLFATPGMLHTGLSLKAFKAWAGNPQNLIVLPGYCVQGTVGHKL 498
Cdd:smart01027   81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 381-496 1.45e-26

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: 104.90  E-value: 1.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   381 AQELSILLDDYWKKMKI-HYPIYFGCGLTENANKYYKIYSSWINSSC------MSNEKENLFDfanispflnnylneKRP 453
Cdd:pfam10996    1 AQELLYLLDELWREGRLpKIPIYLDSPLAIKATEVYRRYPEYLDDEArhfvisKSESKAINEG--------------KGP 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 124505029   454 MVLFATPGMLHTGLSLKAFKAWAGNPQNLIVLPGYCVQGTVGH 496
Cdd:pfam10996   67 KVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
 
Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 11-551 7.37e-84

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 277.07  E-value: 7.37e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKdERKYPNFnllirgPDKINHcqkeefiddeieenieddeieenvn 90
Cdd:COG1236     3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGK-ERNWPPF------PFRPSD------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkrineiI 170
Cdd:COG1236    51 -------------------------------------------------------------------------------V 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTeILKYRGIILMSYPTKALSPILLLDScrvtdmkwekknferqIKMLNEKSDELLNYNinc 250
Cdd:COG1236    52 DAVVLTHAHLDHSGALPLLV-KEGFRGPIYATPATADLARILLGDS----------------AKIQEEEAEAEPLYT--- 111

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  251 ikkdpwninEDNIYNCIDKVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANIPS 330
Cdd:COG1236   112 ---------EEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVP 182

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  331 lNPEIFISESTYATYVRPTKKASELELCNLVHECVHKGGKVLIPVFAIGRAQELSILLDDYWKKMKI-HYPIYFGcGLTE 409
Cdd:COG1236   183 -PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYLLRELKKEGRLpDIPIYVS-GMAI 260

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  410 NANKYYKIYSSWINsscmsNEKENLFDFANISpFLNNY-----LNEKRPMVLFATPGMLHTGLSLKAFKAWAGNPQNLIV 484
Cdd:COG1236   261 RATEIYRRHGEYLR-----DEAQDPFALPNLR-FVTSVeeskaLNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTIL 334

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124505029  485 LPGYCVQGTVGHKLIMGEKQISLDGtTYIKVLCKI-IYLSFSAHADSNGIQQLIKHVS-PKNVIFVHGE 551
Cdd:COG1236   335 FVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVeRLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 11-340 4.87e-80

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: 258.73  E-value: 4.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKDERKYPNFNLLIRGPdkinhcqkeefiddeieenieddeieenvn 90
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNG------------------------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkRINEII 170
Cdd:cd16291    51 --------------------------------------------------------------------------PFTEHI 56

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVT-DMKWEKKNFErqikmlneksdellnynin 249
Cdd:cd16291    57 DCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFT------------------- 117

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  250 cikkdpwninEDNIYNCIDKVIGLQINETFELG-DMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANI 328
Cdd:cd16291   118 ----------SQMIKDCMKKVIAVNLHETVQVDdELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWI 187

                         330
                  ....*....|..
gi 124505029  329 PSLNPEIFISES 340
Cdd:cd16291   188 DRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 11-577 1.32e-72

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: 248.12  E-value: 1.32e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKDERKYPNFNLLIRgPDKInhcqkeefiddeieenieddeieenvn 90
Cdd:COG1782     3 ITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNNDAFPFD-PEEL--------------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkrineii 170
Cdd:COG1782       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTeilK--YRGIILMSYPTKALSPILLLDSCRVTDMKWEKKNFERQIKmlnEKSDELLnYNi 248
Cdd:COG1782    55 DAVVLTHAHLDHSGLLPLLV---KygYRGPIYCTPPTRDLMALLLLDSAKIQEEEAEYANKKRYSG---HPPVEPL-YT- 126

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  249 ncikkdpwninEDNIYNCIDKVIGLQINETFELG-DMSITPYYAGHVLGACIYKIEVRN--FSVIYTGDyntipdkhLGS 325
Cdd:COG1782   127 -----------EKDVEKALKHFITLDYGEVTDIApDIKLTFYNAGHILGSAIVHLHIGDglHNIVFSGD--------LGR 187

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  326 ANIPSLNP-------EIFISESTYATYVRPTKKASELELCNLVHECVHKGGKVLIPVFAIGRAQELSILLDDYWKKMKI- 397
Cdd:COG1782   188 GKTPLLRPptpfpraDTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIp 267

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  398 HYPIYFGCGLTENANkyyKIYSSWINssCMSNEKENLFdFANISPFLNNYL-------------NEKRPMVLFATPGMLH 464
Cdd:COG1782   268 EVPVYLDSPMAIEAT---AIHTAYPE--YLDEELRDLI-FKGENPFLFENLhyvesveeskeinDSDEPAIIIATSGMLT 341

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  465 TGLSLKAFKAWAGNPQNLIVLPGYCVQGTVGHKLIMGEKQISLDGTTyIKVLCKIIYL-SFSAHADSNGIQQLIKHVS-- 541
Cdd:COG1782   342 GGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGET-IPVRAEVETIdGFSGHADRNELLNWLRRLKpk 420

                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 124505029  542 PKNVIFVHGEKNGMQKLAKYISNKHMINSMCPSLGQ 577
Cdd:COG1782   421 PKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLE 456
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 9-340 3.54e-42

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: 152.74  E-value: 3.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029    9 IIIQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKDERKYPnfnllirgpdkinhcqkeefiddeieenieddeieen 88
Cdd:cd16292     1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLP------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   89 vndqhinddninninddykdksdqkrnnrdiekvevkveenveepnFYDNSNADVvnisivnssitdkeklinnlkrine 168
Cdd:cd16292    44 ----------------------------------------------FFDEIDLSE------------------------- 52

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  169 iIDCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVTdmkwekknferqikmlNEKSDELLnyni 248
Cdd:cd16292    53 -IDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYVRVS----------------NISSDEML---- 111

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  249 ncikkdpwnINEDNIYNCIDKVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDYNTIPDKHLGSANI 328
Cdd:cd16292   112 ---------YTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEI 182

                         330
                  ....*....|..
gi 124505029  329 PSLNPEIFISES 340
Cdd:cd16292   183 PPIKPDVLIVES 194
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 149-340 3.95e-36

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 135.54  E-value: 3.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  149 VNSSITDKEKLI-NNLKRINEIiDCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVtdmkwekk 227
Cdd:cd07734    29 MNPGKEDPEACLpQFELLPPEI-DAILISHFHLDHCGALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKS-------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  228 nferqikmlneksdellnynINCIKKDPWNINEDNIYNCIDKVIGLQINETFEL-GDMSITPYYAGHVLGACIYKIEVRN 306
Cdd:cd07734   100 --------------------AERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLfPALSLTAYNAGHVLGAAMWEIQIYG 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 124505029  307 FSVIYTGDYNTIPDKHLGSANIPSLNPEIFISES 340
Cdd:cd07734   160 EKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 381-498 2.61e-33

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: 124.57  E-value: 2.61e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029    381 AQELSILLDDYWKKMKIH-YPIYFGCGLTENANKYYKIYSSWINSSC--MSNEKENLFDFANISPFLNN-----YLNEKR 452
Cdd:smart01027    1 TQELLLILEELWREGELPnVPIYLDSPMAARATEIYKSYPEWMSDEIrkRFEQGRNPFDFKNLKFVKSLeeskrLNDYKG 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 124505029    453 PMVLFATPGMLHTGLSLKAFKAWAGNPQNLIVLPGYCVQGTVGHKL 498
Cdd:smart01027   81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 11-340 2.60e-30

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: 118.72  E-value: 2.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   11 IQVLGAGQTVGRSCVIVELENRKVMFDCGCHLGYKDERKYPNFNLLIRGPDkinhcqkeefiddeieenieddeieenvn 90
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----------------------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   91 dqhinddninninddykdksdqkrnnrdiekvevkveenveepnfydnsnadvvnisivnssitdkeklinnlkrineiI 170
Cdd:cd16295    52 -------------------------------------------------------------------------------I 52

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  171 DCVIISHFHMDHIGALPFFTeILKYRGIILMSYPTKALSPILLLDSCRVTDMKwekknferqikmlNEKSDELLNYNinc 250
Cdd:cd16295    53 DAVILTHAHLDHSGRLPLLV-KEGFRGPIYATPATKDLAELLLLDSAKIQEEE-------------AEHPPAEPLYT--- 115

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  251 ikkdpwninEDNIYNCIDKVIGLQINETFELG-DMSITPYYAGHVLGACIYKIEVRNF-SVIYTGDYNTIPDKHLGSANI 328
Cdd:cd16295   116 ---------EEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVELEIGGGkRILFSGDLGRKNTPLLRDPAP 186

                         330
                  ....*....|..
gi 124505029  329 PSlNPEIFISES 340
Cdd:cd16295   187 PP-EADYLIMES 197
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 381-496 1.45e-26

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: 104.90  E-value: 1.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   381 AQELSILLDDYWKKMKI-HYPIYFGCGLTENANKYYKIYSSWINSSC------MSNEKENLFDfanispflnnylneKRP 453
Cdd:pfam10996    1 AQELLYLLDELWREGRLpKIPIYLDSPLAIKATEVYRRYPEYLDDEArhfvisKSESKAINEG--------------KGP 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 124505029   454 MVLFATPGMLHTGLSLKAFKAWAGNPQNLIVLPGYCVQGTVGH 496
Cdd:pfam10996   67 KVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 512-573 3.03e-13

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 65.33  E-value: 3.03e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124505029   512 YIKVLCKIIYLS-FSAHADSNGIQQLIKHVSPKNVIFVHGEKNGMQKLAKYISNKHMINSMCP 573
Cdd:pfam07521    1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 157-340 1.23e-12

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: 67.93  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  157 EKLINNLKRINEIIDCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVtdmkwekknferqiKML 236
Cdd:cd16293    36 MEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLYQS--------------RGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  237 NEksdellNYNIncikkdpwnINEDNIYNCIDKVIGLQINETFELGD----MSITPYYAGHVLGACIYKIEVRNFSVIYT 312
Cdd:cd16293   102 EE------DFNL---------FTLDDVDEAFDRITQLKYSQPVNLRGkgdgLTITAYNAGHTLGGTIWKITKDSEDIVYA 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 124505029  313 GDYNTIPDKHLGSANIPS---LNPEIFISES 340
Cdd:cd16293   167 VDWNHKKERHLNGAVLDSfggLRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 157-328 7.50e-11

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 62.23  E-value: 7.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   157 EKLINNLKRINEIIDCVIISHFHMDHIGALPF----FTEILKYRGIILMSYPTKALSPILLLDSCRVTDMkwekknferq 232
Cdd:pfam16661   22 ESDLKYLEKILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPVANLGRVSTYDLYASRGI---------- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029   233 ikMLNEKSDEllnynincikkdpwnINEDNIYNCIDKVIGLQINETFELGD----MSITPYYAGHVLGACIYKIEVRNFS 308
Cdd:pfam16661   92 --LGPYDSSE---------------LDLDDIDAAFDKIKTLKYSQTVDLKGkfdgLTITPYNSGHTLGGTIWKISKNSEK 154

                          170       180
                   ....*....|....*....|
gi 124505029   309 VIYTGDYNTIPDKHLGSANI 328
Cdd:pfam16661  155 IVYAVDWNHTKDSHLNGASL 174
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
170-343 2.39e-08

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 55.97  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  170 IDCVIISHFHMDHIGALPFFTEILKYRGiilmsyPTKALsPILLLdscrvtdmKWEKKNFERQIKMlnekSDELLNYNIN 249
Cdd:COG1234    53 IDAIFITHLHGDHIAGLPGLLSTRSLAG------REKPL-TIYGP--------PGTKEFLEALLKA----SGTDLDFPLE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  250 cikkdpwninedniyncidkVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDynTIPDKHLGSAnip 329
Cdd:COG1234   114 --------------------FHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD--TRPCEALVEL--- 168

                         170
                  ....*....|....
gi 124505029  330 SLNPEIFISESTYA 343
Cdd:COG1234   169 AKGADLLIHEATFL 182
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 170-315 2.45e-08

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: 55.31  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  170 IDCVIISHFHMDHIGALPFF-TEILKYrgiilMSYPTKALSPILlldscrvTDMKWEKKNFERQIkmlneksdellnyni 248
Cdd:cd07732    76 VDAVLLSHAHLDHYGLLNYLrPDIPVY-----MGEATKRILKAL-------LPFFGEGDPVPRNI--------------- 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124505029  249 ncikkdpwninedniyncidkvIGLQINETFELGDMSITPYYAGH-VLGACIYKIEVRNFSVIYTGDY 315
Cdd:cd07732   129 ----------------------RVFESGKSFTIGDFTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDF 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 148-314 6.07e-08

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: 53.71  E-value: 6.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029    148 IVNSSITDKEKLINNLKRINEI-IDCVIISHFHMDHIGALPFFTEILKYRgiILMSYPTKalspillldscrvtdmkwek 226
Cdd:smart00849   13 LIDTGPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAP--VYAPEGTA-------------------- 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029    227 knferqiKMLNEKSDELLNYNINCIKKDPwninedniyncidkVIGLQINETFELGDMSITPYYA-GHVLGACIYKIEVR 305
Cdd:smart00849   71 -------ELLKDLLALLGELGAEAEPAPP--------------DRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLPEG 129


                    ....*....
gi 124505029    306 NfsVIYTGD 314
Cdd:smart00849  130 K--ILFTGD 136
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 170-321 2.00e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 53.36  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  170 IDCVIISHFHMDHIGALPFFTEILKYRGI-ILMSYPTKAlspillldscrvtdmkwekkNFERQIKMLNEKSDELLNYNI 248
Cdd:COG1235    69 IDAILLTHEHADHIAGLDDLRPRYGPNPIpVYATPGTLE--------------------ALERRFPYLFAPYPGKLEFHE 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124505029  249 ncikkdpwninedniyncidkvigLQINETFELGDMSITPYYAGH-VLGACIYKIEVRNFSVIYTGDYNTIPDK 321
Cdd:COG1235   129 ------------------------IEPGEPFEIGGLTVTPFPVPHdAGDPVGYRIEDGGKKLAYATDTGYIPEE 178
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 158-340 2.02e-07

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 52.27  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  158 KLINNLKRINEIiDCVIISHFHMDHIGALPFFTEILKYRGIilmsyptkalspillLDSCRVTDMKWEKKNFERQIKMLN 237
Cdd:cd16272    40 RLLKAGVDPDKL-DAIFLSHFHLDHIGGLPTLLFARRYGGR---------------KKPLTIYGPKGIKEFLEKLLNFPV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  238 EKSDELLNYNINCIKKDpwninedniyncidkviglqiNETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGDynT 317
Cdd:cd16272   104 EILPLGFPLEIEELEEG---------------------GEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGD--T 160

                         170       180
                  ....*....|....*....|...
gi 124505029  318 IPDKHLGSAnipSLNPEIFISES 340
Cdd:cd16272   161 GPCENLVEL---AKGADLLIHEC 180
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 148-314 1.07e-05

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: 47.28  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  148 IVNSSITDKEKLINNLKRINEIIDCVIISHFHMDHIGALPFFTEilKYRGIILMSyptkalspillldscrvtdmKWEKK 227
Cdd:cd06262    24 LIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKE--APGAPVYIH--------------------EADAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  228 NFERqikmLNEKSDELLNYNINCIKKDpwninedniyncidkvIGLQINETFELGDMSITPYYA-GHVLGACIYKIEVRN 306
Cdd:cd06262    82 LLED----PELNLAFFGGGPLPPPEPD----------------ILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEG 141


                  ....*...
gi 124505029  307 fsVIYTGD 314
Cdd:cd06262   142 --VLFTGD 147
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 154-314 3.95e-05

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: 45.84  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  154 TDKEKLINNLKRINEIIDCVIISHFHMDHIGALPFFTEilKYRGIILMSYPTKALspillldscrvtdmkWEKKNFERQI 233
Cdd:COG0491    36 ADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAEA---------------LEAPAAGALF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  234 KMLNEKSDELLnynincikkdpwninEDniyncidkviglqiNETFELGDMSITPYYA-GHVLGACIYKIEVRNfsVIYT 312
Cdd:COG0491    99 GREPVPPDRTL---------------ED--------------GDTLELGGPGLEVIHTpGHTPGHVSFYVPDEK--VLFT 147


                  ..
gi 124505029  313 GD 314
Cdd:COG0491   148 GD 149
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
170-199 3.52e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.74  E-value: 3.52e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 124505029   170 IDCVIISHFHMDHIGALPFFTEILKYRGII 199
Cdd:pfam00753   44 IDAVILTHGHFDHIGGLGELAEATDVPVIV 73
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 173-314 3.77e-04

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


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 42.87  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  173 VIISHFHMDHIGALPFFTeilkyrgiilmsyptkalsPiLLLDSCRVT------DMKWEKKNFERQ-------IKMLNEK 239
Cdd:cd07715    61 LLLSHTHWDHIQGFPFFA-------------------P-AYDPGNRIHiygphkDGGSLEEVLRRQmsppyfpVPLEELL 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124505029  240 SDEllnynincikkdpwninedniyncidKVIGLQINETFELGDMSITPYYAGHVLGACIYKIEVRNFSVIYTGD 314
Cdd:cd07715   121 AAI--------------------------EFHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATD 169
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
159-192 4.46e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 43.33  E-value: 4.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 124505029  159 LINNLKRIN---EIIDCVIISHFHMDHIGALPFFTEI 192
Cdd:COG1237    44 LLKNAEKLGidlSDIDAVVLSHGHYDHTGGLPALLEL 80
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 156-314 5.43e-04

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.12  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  156 KEKLINNLKR--INEIiDCVIISHFHMDHIGALPfftEILKyrgiilmSYPTKALspillldscRVTDMKWEKKNFERQI 233
Cdd:cd07731    34 EDVVVPYLKArgIKKL-DYLILTHPDADHIGGLD---AVLK-------NFPVKEV---------YMPGVTHTTKTYEDLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  234 KMLNEKsdellnyNIncikkdpwninedniyncidKVIGLQINETFELGDMSITPYYAGHVLGA------CIYKIEVRNF 307
Cdd:cd07731    94 DAIKEK-------GI--------------------PVTPCKAGDRWQLGGVSFEVLSPPKDDYDdlnnnsCVLRLTYGGT 146


                  ....*..
gi 124505029  308 SVIYTGD 314
Cdd:cd07731   147 SFLLTGD 153
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 170-189 5.90e-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: 42.25  E-value: 5.90e-04
                          10        20
                  ....*....|....*....|
gi 124505029  170 IDCVIISHFHMDHIGALPFF 189
Cdd:cd07740    50 IDAIFITHLHGDHFGGLPFF 69
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 159-194 7.83e-04

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 42.61  E-value: 7.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 124505029  159 LINNLKRIN---EIIDCVIISHFHMDHIGALPFFTEILK 194
Cdd:cd07713    42 LLHNAKKLGidlSDIDAVVLSHGHYDHTGGLKALLELNP 80
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 170-190 8.44e-04

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 42.26  E-value: 8.44e-04
                          10        20
                  ....*....|....*....|.
gi 124505029  170 IDCVIISHFHMDHIGALPFFT 190
Cdd:cd07730    84 IDAVILSHLHWDHIGGLSDFP 104
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 156-314 1.00e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 42.15  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  156 KEKLINNLKR--INEIiDCVIISHFHMDHIGALPfftEILKYRGI--ILMSYPTKalspillldscrvtdmkwEKKNFER 231
Cdd:COG2333    38 ERVVLPYLRAlgIRRL-DLLVLTHPDADHIGGLA---AVLEAFPVgrVLVSGPPD------------------TSETYER 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  232 QIKMLNEKsdellnyNIncikkdpwninedniyncidKVIGLQINETFELGDMSIT---PYYAGHVLGA-----CIYKIE 303
Cdd:COG2333    96 LLEALKEK-------GI--------------------PVRPCRAGDTWQLGGVRFEvlwPPEDLLEGSDennnsLVLRLT 148

                         170
                  ....*....|.
gi 124505029  304 VRNFSVIYTGD 314
Cdd:COG2333   149 YGGFSFLLTGD 159
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 170-190 1.43e-03

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 41.43  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|.
gi 124505029  170 IDCVIISHFHMDHIGALPFFT 190
Cdd:cd07729    89 IDYVILSHLHFDHAGGLDLFP 109
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 155-190 1.69e-03

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 40.65  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 124505029  155 DKEKLINNLKRIN---EIIDCVIISHFHMDHIGALPFFT 190
Cdd:cd07711    43 DRDLLLKALAEHGlspEDIDYVVLTHGHPDHIGNLNLFP 81
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 153-315 2.26e-03

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


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 40.85  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  153 ITDKEKLINNLKRINEIIdcviISHFHMDHIGALPFFteILKYRGIILMSYPTKALspillldscrvtdmkwekknferq 232
Cdd:cd07714    43 IPDFSYLEENKDKIKGIF----ITHGHEDHIGALPYL--LPELNVPIYATPLTLAL------------------------ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124505029  233 IKMLNEKSDELLNYNINCIKKdpwninedniyncidkviglqiNETFELGDMSITPYYAGH-VLGACIYKIEVRNFSVIY 311
Cdd:cd07714    93 IKKKLEEFKLIKKVKLNEIKP----------------------GERIKLGDFEVEFFRVTHsIPDSVGLAIKTPEGTIVH 150


                  ....
gi 124505029  312 TGDY 315
Cdd:cd07714   151 TGDF 154
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 170-210 4.10e-03

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 39.59  E-value: 4.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 124505029  170 IDCVIISHFHMDHIGALPFFTEIlkyRGIILMSYPTKALSP 210
Cdd:cd07725    56 IDRVLLTHHHPDHIGLAGKLQEK---SGATVYILDVTPVKD 93
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 158-186 7.84e-03

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 39.45  E-value: 7.84e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 124505029  158 KLINNLKRIN---EIIDCVIISHFHMDHIGAL 186
Cdd:cd07720    77 KLLANLAAAGidpEDIDDVLLTHLHPDHIGGL 108
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 167-221 9.59e-03

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 38.28  E-value: 9.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124505029  167 NEIIDCVIISHFHMDHIGALPFFTEILKYRGIILMSYPTKALSPILLLDSCRVTD 221
Cdd:cd07722    54 NATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKFPRPEEDEDPDEDGGDIHD 108
 
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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