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Conserved domains on  [gi|2462510563|ref|XP_054193242|]
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integrator complex subunit 11 isoform X2 [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; ...
 32-226 2.34e-156

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: 447.09  E-value: 2.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 111
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 191
Cdd:cd16291    85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 192 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 226
Cdd:cd16291   165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 31-468 4.56e-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: 351.35  E-value: 4.56e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 105
Cdd:COG1782     7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 106 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 173
Cdd:COG1782    77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 174 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 251
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 252 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 329
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 330 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 404
Cdd:COG1782   315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462510563 405 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 468
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; ...
 32-226 2.34e-156

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: 447.09  E-value: 2.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 111
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 191
Cdd:cd16291    85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 192 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 226
Cdd:cd16291   165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 31-468 4.56e-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: 351.35  E-value: 4.56e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 105
Cdd:COG1782     7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 106 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 173
Cdd:COG1782    77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 174 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 251
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 252 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 329
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 330 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 404
Cdd:COG1782   315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462510563 405 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 468
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 ...
 267-385 6.01e-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: 6.01e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  267 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 339
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462510563  340 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 385
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 ...
 267-383 7.30e-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: 7.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 267 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 345
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462510563 346 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 383
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 43-223 1.44e-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: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  43 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 118
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 119 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 194
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462510563 195 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 223
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-206 1.03e-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: 72.59  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563   40 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 119
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  120 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 198
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 2462510563  199 GDYNMTPD 206
Cdd:smart00849 135 GDLLFAGG 142
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 39-228 1.23e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.38  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  39 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 116
Cdd:COG1235    35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 117 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 192
Cdd:COG1235   104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462510563 193 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 228
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; ...
 32-226 2.34e-156

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: 447.09  E-value: 2.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 111
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 191
Cdd:cd16291    85 IYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 192 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 226
Cdd:cd16291   165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 31-468 4.56e-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: 351.35  E-value: 4.56e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEm 105
Cdd:COG1782     7 GAARE-VTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 106 vGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIK 173
Cdd:COG1782    77 -GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 174 AYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETV 251
Cdd:COG1782   156 FYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 252 ERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKA 329
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 330 FD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKM 404
Cdd:COG1782   315 VEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRA 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462510563 405 QVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 468
Cdd:COG1782   394 EVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 32-438 1.73e-113

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 345.25  E-value: 1.73e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFnDDRRFPDFSYitqngRLTDfLDCVIISHFHLDHCGALPYFSEMvGYDGP 111
Cdd:COG1236     7 GAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPF-----RPSD-VDAVVLTHAHLDHSGALPLLVKE-GFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVG 191
Cdd:COG1236    79 IYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 192 SESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE- 269
Cdd:COG1236   158 GKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQEl 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 270 LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFIPWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFA 345
Cdd:COG1236   236 LYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 346 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLV 424
Cdd:COG1236   309 PSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWI 387

                         410
                  ....*....|....*
gi 2462510563 425 GQAE-PESVLLVHGE 438
Cdd:COG1236   388 KATGkPERVFLVHGE 402
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 32-226 3.19e-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: 293.08  E-value: 3.19e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDrrfpdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 111
Cdd:cd07734     4 GGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVG 191
Cdd:cd07734    79 IYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIY 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 192 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 226
Cdd:cd07734   159 GEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 32-226 1.28e-67

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: 1.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrlTDFLDCVIISHFHLDHCGALPYFSEMVGYDGP 111
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEID-----LSEIDLLLITHFHLDHCGALPYFLQKTNFKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIAvDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVG 191
Cdd:cd16292    82 VFMTHPTKAIYKWLLSDYVRVS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVEIA 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 192 SESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 226
Cdd:cd16292   160 GVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 32-226 2.92e-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: 2.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  32 GAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRltdfLDCVIISHFHLDHCGALPYFSEMvGYDGP 111
Cdd:cd16295     5 GAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----IDAVILTHAHLDHSGRLPLLVKE-GFRGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 112 IYMTHPTQAICPILLEDYRKIA---VDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQI 188
Cdd:cd16295    80 IYATPATKDLAELLLLDSAKIQeeeAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVEL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462510563 189 KVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpNLLITES 226
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 ...
 267-385 6.01e-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: 6.01e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  267 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 339
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462510563  340 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 385
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 ...
 267-383 7.30e-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: 7.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 267 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 345
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462510563 346 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 383
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 40-226 7.00e-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: 7.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  40 SCILVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITqngRLTDFLDCVIISHFHLDHCGALPYfseMVGYDG---PIYMTH 116
Cdd:cd16293    13 LCYLLEIDDVTILLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPY---LVGKLGltcPVYATL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 117 PTQAICPI-LLEDYRKiavdKKGEANF--FTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKV 190
Cdd:cd16293    83 PVHKMGRMfMYDLYQS----RGLEEDFnlFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGHTLGGTIWKITK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462510563 191 GSESVVYTGDYNMTPDRHL-GAAWIDKC--RPNLLITES 226
Cdd:cd16293   159 DSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 43-223 1.44e-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: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  43 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 118
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 119 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 194
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462510563 195 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 223
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-225 5.24e-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: 79.96  E-value: 5.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGfNDDRRFPDFSYITQNGRLTDFL--------------------DCVIISH 90
Cdd:cd07732     6 RGTNE-IGGNCIEVETGGTRILLDFGLPLD-PESKYFDEVLDFLELGLLPDIVglyrdplllgglrseedpsvDAVLLSH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  91 FHLDHCGALPYFSEmvgyDGPIYMTHPTQAIcpilLEDYRKIAVDKKGEANFFtsqmikdcmkKVVAvhLHQTVQVDDeL 170
Cdd:cd07732    84 AHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNI----------RVFE--SGKSFTIGD-F 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510563 171 EIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 225
Cdd:cd07732   143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 400-460 3.56e-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: 70.34  E-value: 3.56e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462510563 400 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 460
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-206 1.03e-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: 72.59  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563   40 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 119
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  120 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 198
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 2462510563  199 GDYNMTPD 206
Cdd:smart00849 135 GDLLFAGG 142
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 31-201 3.41e-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: 72.82  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMHMGFND----DRRFPDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSEMv 106
Cdd:cd07714     4 GGLGE-IGKNMYVVEYDDDIIIIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLLPE- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 107 gYDGPIYMTHPTQAICPILLEDYRKIavdkkGEANFftsqmikdcmkkvVAVHLHQTVQVDDeLEIKAYYAGH-VLGAAM 185
Cdd:cd07714    79 -LNVPIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPDSVG 138

                         170
                  ....*....|....*.
gi 2462510563 186 FQIKVGSESVVYTGDY 201
Cdd:cd07714   139 LAIKTPEGTIVHTGDF 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 39-228 1.23e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.38  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  39 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 116
Cdd:COG1235    35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 117 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 192
Cdd:COG1235   104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462510563 193 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 228
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 ...
 31-226 5.67e-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: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQDVGR--SCILVSIAGKNVMLDCGmhmgFNDDRRFPdfsyitQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGY 108
Cdd:cd16272     7 GGAVPSLTRntSSYLLETGGTRILLDCG----EGTVYRLL------KAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 109 DGPiymTHPTQAICPI-LLEDYRKIavdkkgeanFFTSQMIKDCMKKVVAVHL--HQTVQVDDELEIKAYYAGHVLGAAM 185
Cdd:cd16272    77 GGR---KKPLTIYGPKgIKEFLEKL---------LNFPVEILPLGFPLEIEELeeGGEVLELGDLKVEAFPVKHSVESLG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462510563 186 FQIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpNLLITES 226
Cdd:cd16272   145 YRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
31-229 4.10e-11

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 63.68  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQDVGR--SCILVSIAGKNVMLDCG-------MHMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHLDHCGALPY 101
Cdd:COG1234     9 GGAVPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHGDHIAGLPG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 102 FSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFTSqmikdcmkKVVAVHLHQTVQVDDeLEIKAYYAGHVL 181
Cdd:COG1234    72 LLSTRSLAGR---EKPLTIYGPPGTKEFLEALLKASGTDLDFPL--------EFHEIEPGEVFEIGG-FTVTAFPLDHPV 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462510563 182 GAAMFQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PNLLITESTYA 229
Cdd:COG1234   140 PAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
31-115 3.91e-10

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 62.77  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQdVGRSCILVSIAGKNVMLDCGMhmGFNDDRRF------PDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSE 104
Cdd:COG0595    12 GGLGE-IGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDHIGALPYLLK 85

                          90
                  ....*....|.
gi 2462510563 105 MVgyDGPIYMT 115
Cdd:COG0595    86 EL--NVPVYGT 94
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
40-200 5.63e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.30  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  40 SCILVSIAGKNVMLDCGMhmgfndDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEmvgydgpiymTHPTQ 119
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 120 AICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTvqVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTG 199
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 2462510563 200 D 200
Cdd:pfam00753 149 D 149
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 34-197 1.28e-09

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: 57.51  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  34 GQDVGRSCILVSIAGKNVMLDCGMhmGFNDDRRFPDFSYItqngrltdflDCVIISHFHldHCGALPYFSEMVGYDGPIY 113
Cdd:cd16294     7 SGHPTLPCNVLKFKSTTIMLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 114 MTHPTQAICPILLEDyrkiavdkkgeanfftsqmIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE 193
Cdd:cd16294    73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                  ....
gi 2462510563 194 SVVY 197
Cdd:cd16294   134 KISY 137
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 29-226 7.54e-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: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  29 AGGGAgqdvgrSCILVSIAGKNVMLDCGmhmgfnddrrfpdfsyitqNG------RLTDF--LDCVIISHFHLDHC---G 97
Cdd:cd07716    14 PGGAC------SGYLLEADGFRILLDCG-------------------SGvlsrlqRYIDPedLDAVVLSHLHPDHCadlG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  98 ALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFtsqmikdcmkkvvAVHLHQTVQVDDeLEIKAYYA 177
Cdd:cd07716    69 VLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIEPGEPLEIGP-FTITFFRT 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462510563 178 GHVLGAAMFQIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PNLLITES 226
Cdd:cd07716   132 VHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 41-200 3.92e-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: 50.75  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  41 CILVSI-AGKNVMLDCGMhmgfnddrrfPDFSYITQNGRLTDF-LDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPT 118
Cdd:cd06262    12 CYLVSDeEGEAILIDPGA----------GALEKILEAIEELGLkIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 119 QAicpiLLEDyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAMFqiKVGSESVVY 197
Cdd:cd06262    80 AE----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELGG-LELEVIHTpGHTPGSVCF--YIEEEGVLF 144


                  ...
gi 2462510563 198 TGD 200
Cdd:cd06262   145 TGD 147
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-102 3.81e-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: 48.02  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  15 ILMCGAGFGhfewlaGGGAGQDvgrsCILVSIAGKNVMLDCGMHmgfnddrrfpdfSYITQN--GRLTDFLDCVIISHFH 92
Cdd:cd07740     2 FLGSGDAFG------SGGRLNT----CFHVASEAGRFLIDCGAS------------SLIALKraGIDPNAIDAIFITHLH 59

                          90
                  ....*....|
gi 2462510563  93 LDHCGALPYF 102
Cdd:cd07740    60 GDHFGGLPFF 69
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 36-101 6.89e-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: 6.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462510563  36 DVGRS-CILVSIAGKNVMLDCGMHMGFNDDRRFPdfsYITQNGRLTdfLDCVIISHFHLDHCGALPY 101
Cdd:cd07731     6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGIKK--LDYLILTHPDADHIGGLDA 67
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 30-207 7.53e-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: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  30 GGGAGQDVGR-SCILVSIAGKN--VMLDCGMHMG---FNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFS 103
Cdd:cd07735     7 GCSGGPDEGNtSSFLLDPAGSDgdILLDAGTGVGalsLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPLLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 104 EMVGYDG----PIYMTHPTqaicpilledyrkIAVDKK----GEA--NFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIK 173
Cdd:cd07735    87 PNDGGQRgspkTIYGLPET-------------IDALKKhifnWVIwpDFTSIPSGKYPYLRLEPIEPEYPIALTG-LSVT 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462510563 174 AYYAGH-VLGAAMFQIKVGSESVVYTGDynMTPDR 207
Cdd:cd07735   153 AFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 39-120 8.15e-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: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  39 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSY-ITQNGrlTDFLDCVIISHFHLDHCGALP---YFSEMVGYDGPIYM 114
Cdd:cd16279    35 RSSILIETGGKNILIDTG-----------PDFRQqALRAG--IRKLDAVLLTHAHADHIHGLDdlrPFNRLQQRPIPVYA 101


                  ....*.
gi 2462510563 115 THPTQA 120
Cdd:cd16279   102 SEETLD 107
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 89-200 8.59e-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: 46.38  E-value: 8.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  89 SHFHLDHCGAL-PYFSEmvgydGPIYMTHPTQaicpILLEDyrKIAVDKkgeanfftsqmikdcmKKVVAVHLHQTVQVD 167
Cdd:cd16273    43 SHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVKL--KLKVDE----------------EYIVVLPMNTPVEID 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462510563 168 DELEIKAYYAGHVLGAAMFQIKV-GSESVVYTGD 200
Cdd:cd16273    96 GDVSVTLLDANHCPGAVMFLFELpDGRRILHTGD 129
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 36-101 8.76e-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: 8.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462510563  36 DVGR-SCILV-SIAGKNVMLDCGMHMGFNDDRRFPDfSYITQNGRltDFLDCVIISHFHLDHCGALPY 101
Cdd:COG2333     7 DVGQgDAILIrTPDGKTILIDTGPRPSFDAGERVVL-PYLRALGI--RRLDLLVLTHPDADHIGGLAA 71
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 40-102 1.63e-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: 1.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462510563  40 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDF-------------LDCVIISHFHLDHCGALPYF 102
Cdd:cd07729    33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEEQTLeeqlarlgldpedIDYVILSHLHFDHAGGLDLF 108
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 41-117 1.94e-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: 46.85  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  41 CILVSIAGKNVMLDCGM---------HMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHLDHCGALPYFSEMVGyDGP 111
Cdd:cd07713    22 SLLIETEGKKILFDTGQsgvllhnakKLGIDLSD-----------------IDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                  ....*.
gi 2462510563 112 IYMtHP 117
Cdd:cd07713    84 VYA-HP 88
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-200 3.35e-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: 45.45  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  27 WLAGGGAGQDVGRSCILVSIAGKNVMLDCGMhmGFNDDRRFPDfsYITQNGRLtdfLDCVIISHFHLDHCGALPYFSEmv 106
Cdd:COG0491     3 VLPGGTPGAGLGVNSYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALGLD---IKAVLLTHLHPDHVGGLAALAE-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 107 GYDGPIYMTHPTQAicpilledyrkiAVDKKGEANFFTSQMIKDcmkkVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAM 185
Cdd:COG0491    74 AFGAPVYAHAAEAE------------ALEAPAAGALFGREPVPP----DRTLEDGDTLELGG-PGLEVIHTpGHTPGHVS 136

                         170
                  ....*....|....*
gi 2462510563 186 FQIKvgSESVVYTGD 200
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 ...
 40-229 6.11e-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: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  40 SCILVSIAGKNVMLDCG-------MHMGFnddrRFPDfsyitqngrltdfLDCVIISHFHLDHCGALPYF---SEMVGYD 109
Cdd:cd07717    18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SPSK-------------IDRIFITHLHGDHILGLPGLlstMSLLGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 110 GPIYMTHPtqaicpilledyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLH------QTVQVDDELEIKAYYAGHVLGA 183
Cdd:cd07717    81 EPLTIYGP-------------------KGLKEFLETLLRLSASRLPYPIEVHelepdpGLVFEDDGFTVTAFPLDHRVPC 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462510563 184 AMFQIKVGSeSVVYTGDyNMTPDRHLGAAWidkcRPNLLITESTYA 229
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 ...
 40-228 7.74e-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: 41.33  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  40 SCILVSIAGKNVMLDCGMhmGFnddRRFPDfsYITQNGRLTDFLdcVIISHFHLDH-CGaLPYFsemvgydGPIYMthPT 118
Cdd:cd07715    24 SCVEVRAGGELLILDAGT--GI---RELGN--ELMKEGPPGEAH--LLLSHTHWDHiQG-FPFF-------APAYD--PG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 119 QAI---CPILledyrkiavDKKGEANFFTSQM--------IKDCMKKVVAVHL--HQTVQVDDeLEIKAYYAGHVLGAAM 185
Cdd:cd07715    85 NRIhiyGPHK---------DGGSLEEVLRRQMsppyfpvpLEELLAAIEFHDLepGEPFSIGG-VTVTTIPLNHPGGALG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462510563 186 FQIKVGSESVVYTGDYNMTP-DRHLGAAWIDKCR-PNLLITESTY 228
Cdd:cd07715   155 YRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
83-117 1.06e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.41  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462510563  83 LDCVIISHFHLDHCGALPYFSEMVGyDGPIYMtHP 117
Cdd:COG1237    58 IDAVVLSHGHYDHTGGLPALLELNP-KAPVYA-HP 90
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 31-200 1.28e-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: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  31 GGAGQDVGR--SCILVSIAGKNVMLDCGMHMGfnddRRFpdfsyiTQNGRLTDFLDCVIISHFHLDHCGALP---YFSEM 105
Cdd:cd07719     8 GGPIPDPDRagPSTLVVVGGRVYLVDAGSGVV----RRL------AQAGLPLGDLDAVFLTHLHSDHVADLPallLTAWL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 106 VGYDGP--IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCmkKVVAVHLHQTVQVDDELEIKAYYAGH--VL 181
Cdd:cd07719    78 AGRKTPlpVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALV--EVHEIAAGGVVYEDDGVKVTAFLVDHgpVP 155

                         170
                  ....*....|....*....
gi 2462510563 182 GAAMFQIKVGSESVVYTGD 200
Cdd:cd07719   156 PALAYRFDTPGRSVVFSGD 174
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 40-227 3.02e-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: 39.45  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563  40 SCILVSIAGK-NVMLDCG------MHmgfnddRRFPDFsyiTQNGRLTDfLDCVIISHFHLDHCGALPY-----FSEMVG 107
Cdd:cd07718    18 SGILLRIPGDgSILLDCGegtlgqLR------RHYGPE---EADEVLRN-LKCIFISHLHADHHLGLIRllaerKKLFKP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510563 108 YDGPIYMTHPTQ---------AICPILLEDYRKIAV---DKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDdeleikay 175
Cdd:cd07718    88 PSPPLYVVAPRQlrrwlreysSLEDLGLHDISFISNrvsQSLPESDDPLSRDLLSNLLEELGLKSIETVPVI-------- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462510563 176 yagHVLGAAMFQIKVGSE-SVVYTGDynmtpdrhlgaawidkCRPN-----------LLITEST 227
Cdd:cd07718   160 ---HCPDAYGIVLTHEDGwKIVYSGD----------------TRPCealveagkgadLLIHEAT 204
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 43-104 3.04e-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: 3.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462510563  43 LVSIAGKNVMLDCGMHMgfNDDRRFPdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSE 104
Cdd:cd07725    19 LLRDGDETTLIDTGLAT--EEDAEAL-WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE 77
 
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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