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Conserved domains on  [gi|33300633|ref|NP_060341|]
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integrator complex subunit 11 isoform 2 [Homo sapiens]

Protein Classification

INTS11 family MBL fold metallo-hydrolase( domain architecture ID 11440945)

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; ...
 6-204 2.34e-160

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: 456.34  E-value: 2.34e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   6 VTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVG 85
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  86 YDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQ 165
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33300633 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 204
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 4-446 3.77e-117

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: 355.98  E-value: 3.77e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   4 IRVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY 79
Cdd:COG1782   1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  80 -FSEmvGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDD 146
Cdd:COG1782  73 lVKY--GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 147 ELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKK 224
Cdd:COG1782 151 DIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKV 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 225 VHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEF 302
Cdd:COG1782 230 INETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLF 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 303 KHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQV 377
Cdd:COG1782 310 ENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI 389

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33300633 378 lEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 446
Cdd:COG1782 390 -PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 6-204 2.34e-160

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: 456.34  E-value: 2.34e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   6 VTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVG 85
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  86 YDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQ 165
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33300633 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 204
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 4-446 3.77e-117

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: 355.98  E-value: 3.77e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   4 IRVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY 79
Cdd:COG1782   1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  80 -FSEmvGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDD 146
Cdd:COG1782  73 lVKY--GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 147 ELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKK 224
Cdd:COG1782 151 DIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKV 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 225 VHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEF 302
Cdd:COG1782 230 INETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLF 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 303 KHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQV 377
Cdd:COG1782 310 ENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI 389

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33300633 378 lEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 446
Cdd:COG1782 390 -PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-363 6.66e-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: 150.00  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    245 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 33300633    318 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 363
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 ...
 245-361 7.23e-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: 116.07  E-value: 7.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   245 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 323
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 33300633   324 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 361
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 21-201 1.59e-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: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    21 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    97 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 33300633   173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 201
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-184 1.11e-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: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633     18 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633     98 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 33300633    177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 17-206 1.07e-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: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  17 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 94
Cdd:COG1235  35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  95 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 170
Cdd:COG1235 104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33300633 171 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 206
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; ...
 6-204 2.34e-160

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: 456.34  E-value: 2.34e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   6 VTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVG 85
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  86 YDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQ 165
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33300633 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 204
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 4-446 3.77e-117

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: 355.98  E-value: 3.77e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   4 IRVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY 79
Cdd:COG1782   1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  80 -FSEmvGYDGPIYMTHPTQAICPILLEDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDD 146
Cdd:COG1782  73 lVKY--GYRGPIYCTPPTRDLMALLLLDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 147 ELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKK 224
Cdd:COG1782 151 DIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKV 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 225 VHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEF 302
Cdd:COG1782 230 INETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLF 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 303 KHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQV 377
Cdd:COG1782 310 ENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI 389

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33300633 378 lEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 446
Cdd:COG1782 390 -PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 4.04e-116

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 351.41  E-value: 4.04e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   5 RVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFnDDRRFPDFSYitqngRLTDfLDCVIISHFHLDHCGALPYFSEMv 84
Cdd:COG1236   2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPF-----RPSD-VDAVVLTHAHLDHSGALPLLVKE- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  85 GYDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMF 164
Cdd:COG1236  74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 165 QIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALG 243
Cdd:COG1236 153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 244 RAQE-LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFIPWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGP 318
Cdd:COG1236 231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGP 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633 319 MVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKG 397
Cdd:COG1236 304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDE 382

                       410       420
                ....*....|....*....|
gi 33300633 398 IMQLVGQAE-PESVLLVHGE 416
Cdd:COG1236 383 LLEWIKATGkPERVFLVHGE 402
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 7-204 1.81e-98

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: 298.09  E-value: 1.81e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   7 TPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDrrfpdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGY 86
Cdd:cd07734   1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  87 DGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQI 166
Cdd:cd07734  76 RGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEI 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 33300633 167 KVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 204
Cdd:cd07734 156 QIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 4-204 4.14e-71

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: 227.08  E-value: 4.14e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   4 IRVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrlTDFLDCVIISHFHLDHCGALPYFSEM 83
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEID-----LSEIDLLLITHFHLDHCGALPYFLQK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  84 VGYDGPIYMTHPTQAICPILLEDYRKIAvDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAM 163
Cdd:cd16292  76 TNFKGRVFMTHPTKAIYKWLLSDYVRVS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAM 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33300633 164 FQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 204
Cdd:cd16292 154 FMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 6-204 2.41e-61

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: 201.53  E-value: 2.41e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   6 VTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRltdfLDCVIISHFHLDHCGALPYFSEMvG 85
Cdd:cd16295   1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----IDAVILTHAHLDHSGRLPLLVKE-G 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  86 YDGPIYMTHPTQAICPILLEDYRKIA---VDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAA 162
Cdd:cd16295  76 FRGPIYATPATKDLAELLLLDSAKIQeeeAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSA 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 33300633 163 MFQIKVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpNLLITES 204
Cdd:cd16295 156 SVELEIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-363 6.66e-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: 150.00  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    245 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 33300633    318 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 363
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 ...
 245-361 7.23e-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: 116.07  E-value: 7.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   245 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 323
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 33300633   324 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 361
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 2.15e-30

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: 118.01  E-value: 2.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   7 TPLGAGQDVGRSCILVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITqngRLTDFLDCVIISHFHLDHCGALPYfseMVGY 86
Cdd:cd16293   2 TPLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPY---LVGK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  87 DG---PIYMTHPTQAICPI-LLEDYRKiavdKKGEANF--FTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGH 157
Cdd:cd16293  72 LGltcPVYATLPVHKMGRMfMYDLYQS----RGLEEDFnlFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGH 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 33300633 158 VLGAAMFQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--RPNLLITES 204
Cdd:cd16293 148 TLGGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 21-201 1.59e-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: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    21 LVSIAGKNVMLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    97 QAICPI-LLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 33300633   173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 201
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-203 4.25e-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: 4.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   5 RVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGfNDDRRFPDFSYITQNGRLTDFL--------------------DCV 64
Cdd:cd07732   1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLPLD-PESKYFDEVLDFLELGLLPDIVglyrdplllgglrseedpsvDAV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  65 IISHFHLDHCGALPYFSEmvgyDGPIYMTHPTQAIcpilLEDYRKIAVDKKGEANFFtsqmikdcmkKVVAvhLHQTVQV 144
Cdd:cd07732  80 LLSHAHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNI----------RVFE--SGKSFTI 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33300633 145 DDeLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 203
Cdd:cd07732 140 GD-FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 378-438 4.38e-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: 4.38e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33300633   378 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 438
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-184 1.11e-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: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633     18 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQ 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633     98 AicpiLLEDYRKIAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 33300633    177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-179 4.26e-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: 4.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   7 TPLGaGQD-VGRSCILVSIAGKNVMLDCGMHMGFND----DRRFPDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFS 81
Cdd:cd07714   1 IPLG-GLGeIGKNMYVVEYDDDIIIIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  82 EMvgYDGPIYMTHPTQAICPILLEDYRKIavdkkGEANFftsqmikdcmkkvVAVHLHQTVQVDDeLEIKAYYAGH-VLG 160
Cdd:cd07714  77 PE--LNVPIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPD 135

                       170
                ....*....|....*....
gi 33300633 161 AAMFQIKVGSESVVYTGDY 179
Cdd:cd07714 136 SVGLAIKTPEGTIVHTGDF 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 17-206 1.07e-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: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  17 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTH 94
Cdd:COG1235  35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  95 PTQAicpILLEDYRKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGS 170
Cdd:COG1235 104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33300633 171 ESVVYTGDYNMTPDRHLgaAWIDKCRpnLLITESTY 206
Cdd:COG1235 164 KKLAYATDTGYIPEEVL--ELLRGAD--LLILDATY 195
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-93 2.53e-12

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 69.32  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   1 MPEIRVTPLGaGQD-VGRSCILVSIAGKNVMLDCGMhmGFNDDRRF------PDFSYITQNGrltDFLDCVIISHFHLDH 73
Cdd:COG0595   3 KDKLRIIPLG-GLGeIGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDH 76

                        90       100
                ....*....|....*....|
gi 33300633  74 CGALPYFSEMVgyDGPIYMT 93
Cdd:COG0595  77 IGALPYLLKEL--NVPVYGT 94
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-204 5.48e-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: 5.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   6 VTPLGAG-----QDVGRSCILVSIAGKNVMLDCGmhmgFNDDRRFPdfsyitQNGRLTDFLDCVIISHFHLDHCGALPYF 80
Cdd:cd16272   1 LTFLGTGgavpsLTRNTSSYLLETGGTRILLDCG----EGTVYRLL------KAGVDPDKLDAIFLSHFHLDHIGGLPTL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  81 SEMVGYDGPiymTHPTQAICPI-LLEDYRKIavdkkgeanFFTSQMIKDCMKKVVAVHL--HQTVQVDDELEIKAYYAGH 157
Cdd:cd16272  71 LFARRYGGR---KKPLTIYGPKgIKEFLEKL---------LNFPVEILPLGFPLEIEELeeGGEVLELGDLKVEAFPVKH 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 33300633 158 VLGAAMFQIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpNLLITES 204
Cdd:cd16272 139 SVESLGYRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-207 1.43e-11

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 64.83  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   4 IRVTPLGAG---QDVGR--SCILVSIAGKNVMLDCG-------MHMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHL 71
Cdd:COG1234   1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  72 DHCGALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFTSqmikdcmkKVVAVHLHQTVQVDDeLEIK 151
Cdd:COG1234  64 DHIAGLPGLLSTRSLAGR---EKPLTIYGPPGTKEFLEALLKASGTDLDFPL--------EFHEIEPGEVFEIGG-FTVT 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33300633 152 AYYAGHVLGAAMFQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PNLLITESTYA 207
Cdd:COG1234 132 AFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-178 5.59e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.30  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    18 SCILVSIAGKNVMLDCGMhmgfndDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEmvgydgpiymTHPTQ 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633    98 AICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTvqVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTG 177
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 33300633   178 D 178
Cdd:pfam00753 149 D 149
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 12-175 1.10e-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: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  12 GQDVGRSCILVSIAGKNVMLDCGMhmGFNDDRRFPDFSYItqngrltdflDCVIISHFHldHCGALPYFSEMVGYDGPIY 91
Cdd:cd16294   7 SGHPTLPCNVLKFKSTTIMLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  92 MTHPTQAICPILLEDyrkiavdkkgeanfftsqmIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE 171
Cdd:cd16294  73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                ....
gi 33300633 172 SVVY 175
Cdd:cd16294 134 KISY 137
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-204 2.24e-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: 53.99  E-value: 2.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   5 RVTPLG-----AGQDVGRSCILVSIAGKNVMLDCGmhmgfnddrrfpdfsyitqNG------RLTDF--LDCVIISHFHL 71
Cdd:cd07716   1 KLTVLGcsgsyPGPGGACSGYLLEADGFRILLDCG-------------------SGvlsrlqRYIDPedLDAVVLSHLHP 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  72 DHC---GALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFtsqmikdcmkkvvAVHLHQTVQVDDeL 148
Cdd:cd07716  62 DHCadlGVLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIEPGEPLEIGP-F 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33300633 149 EIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PNLLITES 204
Cdd:cd07716 125 TITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 5-185 3.44e-07

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: 51.83  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   5 RVTPLGA--GQDVGR-SCILVSIAGKN--VMLDCGMHMG---FNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGA 76
Cdd:cd07735   2 ELVVLGCsgGPDEGNtSSFLLDPAGSDgdILLDAGTGVGalsLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  77 LPYFSEMVGYDG----PIYMTHPTqaicpilledyrkIAVDKK----GEA--NFFTSQMIKDCMKKVVAVHLHQTVQVDD 146
Cdd:cd07735  82 LPLLSPNDGGQRgspkTIYGLPET-------------IDALKKhifnWVIwpDFTSIPSGKYPYLRLEPIEPEYPIALTG 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33300633 147 eLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDynMTPDR 185
Cdd:cd07735 149 -LSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-178 3.51e-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: 3.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  19 CILVSI-AGKNVMLDCGMhmgfnddrrfPDFSYITQNGRLTDF-LDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPT 96
Cdd:cd06262  12 CYLVSDeEGEAILIDPGA----------GALEKILEAIEELGLkIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  97 QAicpiLLEDyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAMFqiKVGSESVVY 175
Cdd:cd06262  80 AE----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELGG-LELEVIHTpGHTPGSVCF--YIEEEGVLF 144


                ...
gi 33300633 176 TGD 178
Cdd:cd06262 145 TGD 147
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-79 7.25e-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: 7.25e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33300633  14 DVGRS-CILVSIAGKNVMLDCGMHMGFNDDRRFPdfsYITQNGRLTdfLDCVIISHFHLDHCGALPY 79
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; ...
 17-98 7.80e-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: 7.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  17 RSCILVSIAGKNVMLDCGmhmgfnddrrfPDFSY-ITQNGrlTDFLDCVIISHFHLDHCGALP---YFSEMVGYDGPIYM 92
Cdd:cd16279  35 RSSILIETGGKNILIDTG-----------PDFRQqALRAG--IRKLDAVLLTHAHADHIHGLDdlrPFNRLQQRPIPVYA 101


                ....*.
gi 33300633  93 THPTQA 98
Cdd:cd16279 102 SEETLD 107
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 14-79 8.67e-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: 8.67e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33300633  14 DVGR-SCILV-SIAGKNVMLDCGMHMGFNDDRRFPDfSYITQNGRltDFLDCVIISHFHLDHCGALPY 79
Cdd:COG2333   7 DVGQgDAILIrTPDGKTILIDTGPRPSFDAGERVVL-PYLRALGI--RRLDLLVLTHPDADHIGGLAA 71
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 67-178 8.89e-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: 8.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  67 SHFHLDHCGAL-PYFSEmvgydGPIYMTHPTQaicpILLEDyrKIAVDKkgeanfftsqmikdcmKKVVAVHLHQTVQVD 145
Cdd:cd16273  43 SHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVKL--KLKVDE----------------EYIVVLPMNTPVEID 95

                        90       100       110
                ....*....|....*....|....*....|....
gi 33300633 146 DELEIKAYYAGHVLGAAMFQIKV-GSESVVYTGD 178
Cdd:cd16273  96 GDVSVTLLDANHCPGAVMFLFELpDGRRILHTGD 129
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-80 1.59e-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: 1.59e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33300633  18 SCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDF-------------LDCVIISHFHLDHCGALPYF 80
Cdd:cd07729  33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEEQTLeeqlarlgldpedIDYVILSHLHFDHAGGLDLF 108
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 19-95 1.83e-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: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  19 CILVSIAGKNVMLDCGM---------HMGFNDDRrfpdfsyitqngrltdfLDCVIISHFHLDHCGALPYFSEMVGyDGP 89
Cdd:cd07713  22 SLLIETEGKKILFDTGQsgvllhnakKLGIDLSD-----------------IDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                ....*.
gi 33300633  90 IYMtHP 95
Cdd:cd07713  84 VYA-HP 88
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-80 5.47e-05

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: 44.56  E-value: 5.47e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33300633   9 LGAGQDVG-----RSCILVSIAGKNVMLDCGMHmgfnddrrfpdfSYITQN--GRLTDFLDCVIISHFHLDHCGALPYF 80
Cdd:cd07740   3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGAS------------SLIALKraGIDPNAIDAIFITHLHGDHFGGLPFF 69
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 18-207 5.89e-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: 5.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  18 SCILVSIAGKNVMLDCG-------MHMGFnddrRFPDfsyitqngrltdfLDCVIISHFHLDHCGALPYF---SEMVGYD 87
Cdd:cd07717  18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SPSK-------------IDRIFITHLHGDHILGLPGLlstMSLLGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  88 GPIYMTHPtqaicpilledyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLH------QTVQVDDELEIKAYYAGHVLGA 161
Cdd:cd07717  81 EPLTIYGP-------------------KGLKEFLETLLRLSASRLPYPIEVHelepdpGLVFEDDGFTVTAFPLDHRVPC 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33300633 162 AMFQIKVGSeSVVYTGDyNMTPDRHLGAAWidkcRPNLLITESTYA 207
Cdd:cd07717 142 FGYRFEEGR-KIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-178 6.10e-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: 44.68  E-value: 6.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  19 CILVSIAGKNVMLDCGMhmGFNDDRRFPDfsYITQNGRLtdfLDCVIISHFHLDHCGALPYFSEmvGYDGPIYMTHPTQA 98
Cdd:COG0491  17 SYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALGLD---IKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  99 icpilledyrkiAVDKKGEANFFTSQMIKDcmkkVVAVHLHQTVQVDDeLEIKAYYA-GHVLGAAMFQIKvgSESVVYTG 177
Cdd:COG0491  88 ------------ALEAPAAGALFGREPVPP----DRTLEDGDTLELGG-PGLEVIHTpGHTPGHVSFYVP--DEKVLFTG 148


                .
gi 33300633 178 D 178
Cdd:COG0491 149 D 149
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-178 1.42e-04

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: 43.27  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633   5 RVTPLGAG---QDVGR--SCILVSIAGKNVMLDCGMHMGfnddRRFpdfsyiTQNGRLTDFLDCVIISHFHLDHCGALP- 78
Cdd:cd07719   1 RVTLLGTGgpiPDPDRagPSTLVVVGGRVYLVDAGSGVV----RRL------AQAGLPLGDLDAVFLTHLHSDHVADLPa 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  79 --YFSEMVGYDGP--IYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCmkKVVAVHLHQTVQVDDELEIKAYY 154
Cdd:cd07719  71 llLTAWLAGRKTPlpVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALV--EVHEIAAGGVVYEDDGVKVTAFL 148

                       170       180
                ....*....|....*....|....*.
gi 33300633 155 AGH--VLGAAMFQIKVGSESVVYTGD 178
Cdd:cd07719 149 VDHgpVPPALAYRFDTPGRSVVFSGD 174
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 18-206 5.42e-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: 41.71  E-value: 5.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  18 SCILVSIAGKNVMLDCGMhmGFnddRRFPDfsYITQNGRLTDFLdcVIISHFHLDH-CGaLPYFsemvgydGPIYMthPT 96
Cdd:cd07715  24 SCVEVRAGGELLILDAGT--GI---RELGN--ELMKEGPPGEAH--LLLSHTHWDHiQG-FPFF-------APAYD--PG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  97 QAI---CPILledyrkiavDKKGEANFFTSQM--------IKDCMKKVVAVHL--HQTVQVDDeLEIKAYYAGHVLGAAM 163
Cdd:cd07715  85 NRIhiyGPHK---------DGGSLEEVLRRQMsppyfpvpLEELLAAIEFHDLepGEPFSIGG-VTVTTIPLNHPGGALG 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 33300633 164 FQIKVGSESVVYTGDYNMTP-DRHLGAAWIDKCR-PNLLITESTY 206
Cdd:cd07715 155 YRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
61-95 1.01e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.41  E-value: 1.01e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 33300633  61 LDCVIISHFHLDHCGALPYFSEMVGyDGPIYMtHP 95
Cdd:COG1237  58 IDAVVLSHGHYDHTGGLPALLELNP-KAPVYA-HP 90
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 18-205 2.64e-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: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  18 SCILVSIAGK-NVMLDCG------MHmgfnddRRFPDFsyiTQNGRLTDfLDCVIISHFHLDHCGALPY-----FSEMVG 85
Cdd:cd07718  18 SGILLRIPGDgSILLDCGegtlgqLR------RHYGPE---EADEVLRN-LKCIFISHLHADHHLGLIRllaerKKLFKP 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33300633  86 YDGPIYMTHPTQ---------AICPILLEDYRKIAV---DKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDdeleikay 153
Cdd:cd07718  88 PSPPLYVVAPRQlrrwlreysSLEDLGLHDISFISNrvsQSLPESDDPLSRDLLSNLLEELGLKSIETVPVI-------- 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33300633 154 yagHVLGAAMFQIKVGSE-SVVYTGDynmtpdrhlgaawidkCRPN-----------LLITEST 205
Cdd:cd07718 160 ---HCPDAYGIVLTHEDGwKIVYSGD----------------TRPCealveagkgadLLIHEAT 204
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 21-82 3.13e-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: 3.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33300633  21 LVSIAGKNVMLDCGMHMgfNDDRRFPdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSE 82
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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