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Conserved domains on  [gi|374253819|ref|NP_001243385|]
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integrator complex subunit 11 isoform 1 [Homo sapiens]

Protein Classification

INTS11 family MBL fold metallo-hydrolase( domain architecture ID 11611275)

INTS11 family MBL fold metallo-hydrolase similar to metazoan Integrator complex subunit 11, which is part of the complex that is 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 16-210 8.49e-157

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: 447.48  E-value: 8.49e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 95
Cdd:cd16291    5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 175
Cdd:cd16291   85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 176 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 210
Cdd:cd16291  165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 15-452 3.97e-115

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


The actual alignment was detected with superfamily member COG1782:

Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 350.97  E-value: 3.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 89
Cdd:COG1782    7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  90 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 157
Cdd:COG1782   77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 158 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 235
Cdd:COG1782  156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 236 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 313
Cdd:COG1782  235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 314 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 388
Cdd:COG1782  315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253819 389 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 452
Cdd:COG1782  394 EVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 16-210 8.49e-157

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: 447.48  E-value: 8.49e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 95
Cdd:cd16291    5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 175
Cdd:cd16291   85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 176 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 210
Cdd:cd16291  165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 15-452 3.97e-115

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: 350.97  E-value: 3.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 89
Cdd:COG1782    7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  90 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 157
Cdd:COG1782   77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 158 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 235
Cdd:COG1782  156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 236 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 313
Cdd:COG1782  235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 314 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 388
Cdd:COG1782  315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253819 389 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 452
Cdd:COG1782  394 EVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 251-369 5.18e-43

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: 150.38  E-value: 5.18e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   251 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 323
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253819   324 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 369
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 ...
 251-367 6.23e-31

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: 116.46  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  251 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 329
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253819  330 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 367
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 27-207 1.51e-17

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 81.10  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   27 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 102
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  103 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 178
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 374253819  179 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 207
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 24-190 1.30e-14

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: 72.20  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819    24 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 103
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   104 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 182
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 374253819   183 GDYNMTPD 190
Cdd:smart00849 135 GDLLFAGG 142
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 23-212 1.28e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.00  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  23 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 100
Cdd:COG1235   35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 101 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 176
Cdd:COG1235  104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 374253819 177 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 212
Cdd:COG1235  164 KKLAYATDTGYIPEEVL--ELLRGAD--LLILDATY 195
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 16-210 8.49e-157

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: 447.48  E-value: 8.49e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 95
Cdd:cd16291    5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 175
Cdd:cd16291   85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 176 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 210
Cdd:cd16291  165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 15-452 3.97e-115

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: 350.97  E-value: 3.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 89
Cdd:COG1782    7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  90 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 157
Cdd:COG1782   77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 158 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 235
Cdd:COG1782  156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 236 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 313
Cdd:COG1782  235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 314 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 388
Cdd:COG1782  315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253819 389 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 452
Cdd:COG1782  394 EVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 16-422 1.56e-113

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 344.86  E-value: 1.56e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFnDDRRFPDFSYitqngRLTDfLDCVIISHFHLDHCGALPYFSEMvGYDGP 95
Cdd:COG1236    7 GAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPF-----RPSD-VDAVVLTHAHLDHSGALPLLVKE-GFRGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVG 175
Cdd:COG1236   79 IYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 176 SESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE- 253
Cdd:COG1236  158 GKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQEl 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 254 LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFIPWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFA 329
Cdd:COG1236  236 LYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIA 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 330 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLV 408
Cdd:COG1236  309 PSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWI 387

                        410
                 ....*....|....*
gi 374253819 409 GQAE-PESVLLVHGE 422
Cdd:COG1236  388 KATGkPERVFLVHGE 402
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 16-210 1.48e-96

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: 293.47  E-value: 1.48e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDrrfpdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 95
Cdd:cd07734    4 GGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 175
Cdd:cd07734   79 IYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIY 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 176 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 210
Cdd:cd07734  159 GEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 16-210 9.81e-68

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: 218.61  E-value: 9.81e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrlTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 95
Cdd:cd16292    7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEID-----LSEIDLLLITHFHLDHCGALPYFLQKTNFKGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIAvDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVG 175
Cdd:cd16292   82 VFMTHPTKAIYKWLLSDYVRVS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVEIA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 176 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 210
Cdd:cd16292  160 GVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 16-210 2.49e-59

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: 196.53  E-value: 2.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  16 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRltdfLDCVIISHFHLDHCGALPYFSEMvGYDGP 95
Cdd:cd16295    5 GAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----IDAVILTHAHLDHSGRLPLLVKE-GFRGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  96 IYMTHPTQAICPILLEDYRKIA---VDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQI 172
Cdd:cd16295   80 IYATPATKDLAELLLLDSAKIQeeeAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVEL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 374253819 173 KVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpNLLITES 210
Cdd:cd16295  160 EIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 251-369 5.18e-43

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: 150.38  E-value: 5.18e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   251 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 323
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253819   324 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 369
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 ...
 251-367 6.23e-31

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: 116.46  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  251 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 329
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253819  330 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 367
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 24-210 6.68e-29

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: 113.77  E-value: 6.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  24 SCILVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITqngRLTDFLDCVIISHFHLDHCGALPYfseMVGYDG---PIYMTH 100
Cdd:cd16293   13 LCYLLEIDDVTILLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPY---LVGKLGltcPVYATL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 101 PTQAICPI-LLEDYRKiavdKKGEANF--FTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKV 174
Cdd:cd16293   83 PVHKMGRMfMYDLYQS----RGLEEDFnlFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGHTLGGTIWKITK 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 374253819 175 GSESVVYTGDYNMTPDRHL-GAAWIDKC--RPNLLITES 210
Cdd:cd16293  159 DSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 27-207 1.51e-17

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 81.10  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   27 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 102
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  103 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 178
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 374253819  179 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 207
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-209 5.97e-17

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: 79.58  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGfNDDRRFPDFSYITQNGRLTDFL--------------------DCVIISH 74
Cdd:cd07732    6 RGTNE-IGGNCIEVETGGTRILLDFGLPLD-PESKYFDEVLDFLELGLLPDIVglyrdplllgglrseedpsvDAVLLSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  75 FHLDHCGALPYFSEmvgyDGPIYMTHPTQAIcpilLEDYRKIAVDKKGEANFFtsqmikdcmkKVVAvhLHQTVQVDDeL 154
Cdd:cd07732   84 AHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNI----------RVFE--SGKSFTIGD-F 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 374253819 155 EIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 209
Cdd:cd07732  143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 384-444 4.05e-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: 69.96  E-value: 4.05e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253819  384 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 444
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 24-190 1.30e-14

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: 72.20  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819    24 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 103
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   104 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 182
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 374253819   183 GDYNMTPD 190
Cdd:smart00849 135 GDLLFAGG 142
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 15-185 3.58e-14

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: 72.44  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFND----DRRFPDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSEMv 90
Cdd:cd07714    4 GGLGE-IGKNMYVVEYDDDIIIIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLLPE- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  91 gYDGPIYMTHPTQAICPILLEDYRKIavdkkGEANFftsqmikdcmkkvVAVHLHQTVQVDDeLEIKAYYAGH-VLGAAM 169
Cdd:cd07714   79 -LNVPIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPDSVG 138

                        170
                 ....*....|....*.
gi 374253819 170 FQIKVGSESVVYTGDY 185
Cdd:cd07714  139 LAIKTPEGTIVHTGDF 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 23-212 1.28e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.00  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  23 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 100
Cdd:COG1235   35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 101 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 176
Cdd:COG1235  104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 374253819 177 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 212
Cdd:COG1235  164 KKLAYATDTGYIPEEVL--ELLRGAD--LLILDATY 195
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 15-210 6.52e-12

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: 64.59  E-value: 6.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQDVGR--SCILVSIAGKNVMLDCGmhmgFNDDRRFPdfsyitQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGY 92
Cdd:cd16272    7 GGAVPSLTRntSSYLLETGGTRILLDCG----EGTVYRLL------KAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  93 DGPiymTHPTQAICPI-LLEDYRKIavdkkgeanFFTSQMIKDCMKKVVAVHL--HQTVQVDDELEIKAYYAGHVLGAAM 169
Cdd:cd16272   77 GGR---KKPLTIYGPKgIKEFLEKL---------LNFPVEILPLGFPLEIEELeeGGEVLELGDLKVEAFPVKHSVESLG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 374253819 170 FQIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpNLLITES 210
Cdd:cd16272  145 YRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
15-213 4.64e-11

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 63.29  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQDVGR--SCILVSIAGKNVMLDCG-------MHMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHLDHCGALPY 85
Cdd:COG1234    9 GGAVPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHGDHIAGLPG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  86 FSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFTSqmikdcmkKVVAVHLHQTVQVDDeLEIKAYYAGHVL 165
Cdd:COG1234   72 LLSTRSLAGR---EKPLTIYGPPGTKEFLEALLKASGTDLDFPL--------EFHEIEPGEVFEIGG-FTVTAFPLDHPV 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 374253819 166 GAAMFQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PNLLITESTYA 213
Cdd:COG1234  140 PAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
15-99 3.91e-10

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 62.39  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQdVGRSCILVSIAGKNVMLDCGMhmGFNDDRRF------PDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSE 88
Cdd:COG0595   12 GGLGE-IGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDHIGALPYLLK 85

                         90
                 ....*....|.
gi 374253819  89 MVgyDGPIYMT 99
Cdd:COG0595   86 EL--NVPVYGT 94
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
24-184 6.41e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.92  E-value: 6.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   24 SCILVSIAGKNVMLDCGMhmgfndDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEmvgydgpiymTHPTQ 103
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  104 AICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTvqVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTG 183
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 374253819  184 D 184
Cdd:pfam00753 149 D 149
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 18-181 9.34e-10

integrator subunit 9, 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 Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74). 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: 293852 [Multi-domain]  Cd Length: 166  Bit Score: 57.89  E-value: 9.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  18 GQDVGRSCILVSIAGKNVMLDCGMhmGFNDDRRFPDFSYItqngrltdflDCVIISHFHldHCGALPYFSEMVGYDGPIY 97
Cdd:cd16294    7 SGHPTLPCNVLKFKSTTIMLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  98 MTHPTQAICPILLEDyrkiavdkkgeanfftsqmIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE 177
Cdd:cd16294   73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                 ....
gi 374253819 178 SVVY 181
Cdd:cd16294  134 KISY 137
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 13-210 6.84e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 52.44  E-value: 6.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  13 AGGGAgqdvgrSCILVSIAGKNVMLDCGmhmgfnddrrfpdfsyitqNG------RLTDF--LDCVIISHFHLDHC---G 81
Cdd:cd07716   14 PGGAC------SGYLLEADGFRILLDCG-------------------SGvlsrlqRYIDPedLDAVVLSHLHPDHCadlG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  82 ALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFtsqmikdcmkkvvAVHLHQTVQVDDeLEIKAYYA 161
Cdd:cd07716   69 VLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIEPGEPLEIGP-FTITFFRT 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 374253819 162 GHVLGAAMFQIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PNLLITES 210
Cdd:cd07716  132 VHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 25-184 4.34e-07

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 50.36  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  25 CILVSI-AGKNVMLDCGMhmgfnddrrfPDFSYITQNGRLTDF-LDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPT 102
Cdd:cd06262   12 CYLVSDeEGEAILIDPGA----------GALEKILEAIEELGLkIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 103 QAicpiLLEDyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAMFqiKVGSESVVY 181
Cdd:cd06262   80 AE----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELGG-LELEVIHTpGHTPGSVCF--YIEEEGVLF 144


                 ...
gi 374253819 182 TGD 184
Cdd:cd06262  145 TGD 147
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 14-191 7.42e-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: 47.98  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  14 GGGAGQDVGR-SCILVSIAGKN--VMLDCGMHMG---FNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFS 87
Cdd:cd07735    7 GCSGGPDEGNtSSFLLDPAGSDgdILLDAGTGVGalsLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPLLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  88 EMVGYDG----PIYMTHPTqaicpilledyrkIAVDKK----GEA--NFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIK 157
Cdd:cd07735   87 PNDGGQRgspkTIYGLPET-------------IDALKKhifnWVIwpDFTSIPSGKYPYLRLEPIEPEYPIALTG-LSVT 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 374253819 158 AYYAGH-VLGAAMFQIKVGSESVVYTGDynMTPDR 191
Cdd:cd07735  153 AFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 20-85 7.55e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 46.74  E-value: 7.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253819  20 DVGRS-CILVSIAGKNVMLDCGMHMGFNDDRRFPdfsYITQNGRLTdfLDCVIISHFHLDHCGALPY 85
Cdd:cd07731    6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGIKK--LDYLILTHPDADHIGGLDA 67
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 23-104 7.97e-06

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: 46.70  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  23 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSY-ITQNGrlTDFLDCVIISHFHLDHCGALP---YFSEMVGYDGPIYM 98
Cdd:cd16279   35 RSSILIETGGKNILIDTG-----------PDFRQqALRAG--IRKLDAVLLTHAHADHIHGLDdlrPFNRLQQRPIPVYA 101


                 ....*.
gi 374253819  99 THPTQA 104
Cdd:cd16279  102 SEETLD 107
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 73-184 9.08e-06

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: 45.99  E-value: 9.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  73 SHFHLDHCGAL-PYFSEmvgydGPIYMTHPTQaicpILLEDyrKIAVDKkgeanfftsqmikdcmKKVVAVHLHQTVQVD 151
Cdd:cd16273   43 SHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVKL--KLKVDE----------------EYIVVLPMNTPVEID 95

                         90       100       110
                 ....*....|....*....|....*....|....
gi 374253819 152 DELEIKAYYAGHVLGAAMFQIKV-GSESVVYTGD 184
Cdd:cd16273   96 GDVSVTLLDANHCPGAVMFLFELpDGRRILHTGD 129
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 20-85 9.20e-06

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 47.54  E-value: 9.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374253819  20 DVGR-SCILV-SIAGKNVMLDCGMHMGFNDDRRFPDfSYITQNGRltDFLDCVIISHFHLDHCGALPY 85
Cdd:COG2333    7 DVGQgDAILIrTPDGKTILIDTGPRPSFDAGERVVL-PYLRALGI--RRLDLLVLTHPDADHIGGLAA 71
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-86 9.95e-06

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 46.48  E-value: 9.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819   2 CGAGFGhfewlaGGGAGQDvgrsCILVSIAGKNVMLDCGMHmgfnddrrfpdfSYITQN--GRLTDFLDCVIISHFHLDH 79
Cdd:cd07740    5 SGDAFG------SGGRLNT----CFHVASEAGRFLIDCGAS------------SLIALKraGIDPNAIDAIFITHLHGDH 62


                 ....*..
gi 374253819  80 CGALPYF 86
Cdd:cd07740   63 FGGLPFF 69
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 24-86 1.64e-05

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: 46.44  E-value: 1.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253819  24 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDF-------------LDCVIISHFHLDHCGALPYF 86
Cdd:cd07729   33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEEQTLeeqlarlgldpedIDYVILSHLHFDHAGGLDLF 108
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 25-101 2.20e-05

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: 46.46  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  25 CILVSIAGKNVMLDCGM---------HMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHLDHCGALPYFSEMVGyDGP 95
Cdd:cd07713   22 SLLIETEGKKILFDTGQsgvllhnakKLGIDLSD-----------------IDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                 ....*.
gi 374253819  96 IYMtHP 101
Cdd:cd07713   84 VYA-HP 88
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-184 3.97e-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: 45.07  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  11 WLAGGGAGQDVGRSCILVSIAGKNVMLDCGMhmGFNDDRRFPDfsYITQNGRLtdfLDCVIISHFHLDHCGALPYFSEmv 90
Cdd:COG0491    3 VLPGGTPGAGLGVNSYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALGLD---IKAVLLTHLHPDHVGGLAALAE-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  91 GYDGPIYMTHPTQAicpilledyrkiAVDKKGEANFFTSQMIKDcmkkVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAM 169
Cdd:COG0491   74 AFGAPVYAHAAEAE------------ALEAPAAGALFGREPVPP----DRTLEDGDTLELGG-PGLEVIHTpGHTPGHVS 136

                        170
                 ....*....|....*
gi 374253819 170 FQIKvgSESVVYTGD 184
Cdd:COG0491  137 FYVP--DEKVLFTGD 149
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 24-213 6.36e-05

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 44.75  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  24 SCILVSIAGKNVMLDCG-------MHMGFnddrRFPDfsyitqngrltdfLDCVIISHFHLDHCGALPYF---SEMVGYD 93
Cdd:cd07717   18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SPSK-------------IDRIFITHLHGDHILGLPGLlstMSLLGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  94 GPIYMTHPtqaicpilledyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLH------QTVQVDDELEIKAYYAGHVLGA 167
Cdd:cd07717   81 EPLTIYGP-------------------KGLKEFLETLLRLSASRLPYPIEVHelepdpGLVFEDDGFTVTAFPLDHRVPC 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 374253819 168 AMFQIKVGSeSVVYTGDyNMTPDRHLGAAWidkcRPNLLITESTYA 213
Cdd:cd07717  142 FGYRFEEGR-KIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 24-212 8.14e-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: 40.94  E-value: 8.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  24 SCILVSIAGKNVMLDCGMhmGFnddRRFPDfsYITQNGRLTDFLdcVIISHFHLDH-CGaLPYFsemvgydGPIYMthPT 102
Cdd:cd07715   24 SCVEVRAGGELLILDAGT--GI---RELGN--ELMKEGPPGEAH--LLLSHTHWDHiQG-FPFF-------APAYD--PG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819 103 QAI---CPILledyrkiavDKKGEANFFTSQM--------IKDCMKKVVAVHL--HQTVQVDDeLEIKAYYAGHVLGAAM 169
Cdd:cd07715   85 NRIhiyGPHK---------DGGSLEEVLRRQMsppyfpvpLEELLAAIEFHDLepGEPFSIGG-VTVTTIPLNHPGGALG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 374253819 170 FQIKVGSESVVYTGDYNMTP-DRHLGAAWIDKCR-PNLLITESTY 212
Cdd:cd07715  155 YRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
67-101 1.09e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.41  E-value: 1.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 374253819  67 LDCVIISHFHLDHCGALPYFSEMVGyDGPIYMtHP 101
Cdd:COG1237   58 IDAVVLSHGHYDHTGGLPALLELNP-KAPVYA-HP 90
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 15-184 1.24e-03

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: 40.19  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  15 GGAGQDVGR--SCILVSIAGKNVMLDCGMHMGfnddRRFpdfsyiTQNGRLTDFLDCVIISHFHLDHCGALP---YFSEM 89
Cdd:cd07719    8 GGPIPDPDRagPSTLVVVGGRVYLVDAGSGVV----RRL------AQAGLPLGDLDAVFLTHLHSDHVADLPallLTAWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  90 VGYDGP--IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCmkKVVAVHLHQTVQVDDELEIKAYYAGH--VL 165
Cdd:cd07719   78 AGRKTPlpVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALV--EVHEIAAGGVVYEDDGVKVTAFLVDHgpVP 155

                        170
                 ....*....|....*....
gi 374253819 166 GAAMFQIKVGSESVVYTGD 184
Cdd:cd07719  156 PALAYRFDTPGRSVVFSGD 174
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 27-88 3.11e-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: 39.20  E-value: 3.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253819  27 LVSIAGKNVMLDCGMHMgfNDDRRFPdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSE 88
Cdd:cd07725   19 LLRDGDETTLIDTGLAT--EEDAEAL-WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE 77
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 24-211 3.30e-03

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 39.07  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  24 SCILVSIAGK-NVMLDCG------MHmgfnddRRFPDFsyiTQNGRLTDfLDCVIISHFHLDHCGALPY-----FSEMVG 91
Cdd:cd07718   18 SGILLRIPGDgSILLDCGegtlgqLR------RHYGPE---EADEVLRN-LKCIFISHLHADHHLGLIRllaerKKLFKP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253819  92 YDGPIYMTHPTQ---------AICPILLEDYRKIAV---DKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDdeleikay 159
Cdd:cd07718   88 PSPPLYVVAPRQlrrwlreysSLEDLGLHDISFISNrvsQSLPESDDPLSRDLLSNLLEELGLKSIETVPVI-------- 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253819 160 yagHVLGAAMFQIKVGSE-SVVYTGDynmtpdrhlgaawidkCRPN-----------LLITEST 211
Cdd:cd07718  160 ---HCPDAYGIVLTHEDGwKIVYSGD----------------TRPCealveagkgadLLIHEAT 204
 
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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