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Conserved domains on  [gi|374253821|ref|NP_001243389|]
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integrator complex subunit 11 isoform 3 [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; ...
 1-175 9.18e-140

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: 402.79  E-value: 9.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd16291   25 MFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGA 160
Cdd:cd16291  105 IAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGA 184

                        170
                 ....*....|....*
gi 374253821 161 AWIDKCRPNLLITES 175
Cdd:cd16291  185 AWIDRLRPDLLITES 199
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-417 2.91e-104

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: 321.69  E-value: 2.91e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEmvGYDGPIYMTHPTQAICPILL 75
Cdd:COG1782   27 LLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY--GYRGPIYCTPPTRDLMALLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  76 EDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE- 142
Cdd:COG1782   97 LDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNAGHILGSAIVHLHIGDGl 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 143 -SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCI 221
Cdd:COG1782  177 hNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILY 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 222 LLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFA 294
Cdd:COG1782  256 VLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIA 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 295 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLV 373
Cdd:COG1782  336 TSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWL 414

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 374253821 374 GQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 417
Cdd:COG1782  415 RRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 1-175 9.18e-140

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: 402.79  E-value: 9.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd16291   25 MFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGA 160
Cdd:cd16291  105 IAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGA 184

                        170
                 ....*....|....*
gi 374253821 161 AWIDKCRPNLLITES 175
Cdd:cd16291  185 AWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-417 2.91e-104

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: 321.69  E-value: 2.91e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEmvGYDGPIYMTHPTQAICPILL 75
Cdd:COG1782   27 LLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY--GYRGPIYCTPPTRDLMALLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  76 EDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE- 142
Cdd:COG1782   97 LDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNAGHILGSAIVHLHIGDGl 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 143 -SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCI 221
Cdd:COG1782  177 hNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILY 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 222 LLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFA 294
Cdd:COG1782  256 VLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIA 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 295 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLV 373
Cdd:COG1782  336 TSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWL 414

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 374253821 374 GQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 417
Cdd:COG1782  415 RRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 216-334 5.55e-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: 149.61  E-value: 5.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   216 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 288
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253821   289 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 334
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 ...
 216-332 6.24e-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: 6.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  216 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 294
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253821  295 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 332
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 1-172 5.23e-16

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 76.48  E-value: 5.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821    1 MLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPTQAICPI-LL 75
Cdd:pfam16661  10 LLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPVANLGRVsTY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   76 EDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNM 152
Cdd:pfam16661  84 DLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAVDWNH 163

                         170       180
                  ....*....|....*....|....*....
gi 374253821  153 TPDRHL-GAAWIDKC--------RPNLLI 172
Cdd:pfam16661 164 TKDSHLnGASLLDSTgkpleslvRPTALI 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-155 5.09e-11

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: 61.80  E-value: 5.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821     1 MLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQAicpiLLEDYRK 80
Cdd:smart00849  13 LIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTAE----LLKDLLA 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253821    81 IAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYTGDYNMTPD 155
Cdd:smart00849  79 LLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFTGDLLFAGG 142
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
32-178 1.76e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 52.50  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFTSqmikdcmkKVVAVHLHQ 111
Cdd:COG1234   53 IDAIFITHLHGDHIAGLPGLLSTRSLAGR---EKPLTIYGPPGTKEFLEALLKASGTDLDFPL--------EFHEIEPGE 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 112 TVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PNLLITESTYA 178
Cdd:COG1234  122 VFEIGG-FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 1-175 9.18e-140

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: 402.79  E-value: 9.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd16291   25 MFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGA 160
Cdd:cd16291  105 IAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGA 184

                        170
                 ....*....|....*
gi 374253821 161 AWIDKCRPNLLITES 175
Cdd:cd16291  185 AWIDRLRPDLLITES 199
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-417 2.91e-104

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: 321.69  E-value: 2.91e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRfpdfsyitQNGRLTDF----LDCVIISHFHLDHCGALPY-FSEmvGYDGPIYMTHPTQAICPILL 75
Cdd:COG1782   27 LLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPLlVKY--GYRGPIYCTPPTRDLMALLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  76 EDYRKIA------VDKKGEAN------FFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE- 142
Cdd:COG1782   97 LDSAKIQeeeaeyANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYNAGHILGSAIVHLHIGDGl 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 143 -SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCI 221
Cdd:COG1782  177 hNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILY 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 222 LLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFA 294
Cdd:COG1782  256 VLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIA 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 295 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLV 373
Cdd:COG1782  336 TSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWL 414

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 374253821 374 GQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTL 417
Cdd:COG1782  415 RRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-387 6.45e-104

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 319.05  E-value: 6.45e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFnDDRRFPDFSYitqngRLTDfLDCVIISHFHLDHCGALPYFSEMvGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:COG1236   27 LIDCGLFQGG-KERNWPPFPF-----RPSD-VDAVVLTHAHLDHSGALPLLVKE-GFRGPIYATPATADLARILLGDSAK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDR-HLG 159
Cdd:COG1236   99 IQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPlLAP 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 160 AAWIDKCrpNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE-LCILLETFWERMNLKVPIYF 238
Cdd:COG1236  178 PEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQElLYLLRELKKEGRLPDIPIYV 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 239 StGLTEKANHYYKLFIPWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGN 314
Cdd:COG1236  256 S-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWD 328

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374253821 315 EKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLVGQAE-PESVLLVHGE 387
Cdd:COG1236  329 PRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 1-175 4.55e-85

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: 262.65  E-value: 4.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDrrfpdFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd07734   24 LLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGA 160
Cdd:cd07734   99 SAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPA 178

                        170
                 ....*....|....*
gi 374253821 161 AWIDKCRPNLLITES 175
Cdd:cd07734  179 ASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 1-175 5.05e-55

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: 184.33  E-value: 5.05e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRFPDFSYITqngrlTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd16292   27 MLDCGIHPGYSGLASLPFFDEID-----LSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYVR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IAvDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGA 160
Cdd:cd16292  102 VS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPA 179

                        170
                 ....*....|....*
gi 374253821 161 AWIDKCRPNLLITES 175
Cdd:cd16292  180 AEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 1-175 1.67e-47

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: 164.55  E-value: 1.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFNDDRRFPDFSYITQNGRLtdflDCVIISHFHLDHCGALPYFSEMvGYDGPIYMTHPTQAICPILLEDYRK 80
Cdd:cd16295   25 LLDCGLFQGGKELEELNNEPFPFDPKEI----DAVILTHAHLDHSGRLPLLVKE-GFRGPIYATPATKDLAELLLLDSAK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  81 IA---VDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE-SVVYTGDYNMTPDR 156
Cdd:cd16295  100 IQeeeAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGkRILFSGDLGRKNTP 179

                        170       180
                 ....*....|....*....|
gi 374253821 157 HLGA-AWIDKCrpNLLITES 175
Cdd:cd16295  180 LLRDpAPPPEA--DYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 216-334 5.55e-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: 149.61  E-value: 5.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   216 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 288
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253821   289 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 334
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 ...
 216-332 6.24e-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: 6.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  216 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 294
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253821  295 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 332
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 1-175 7.10e-27

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: 107.99  E-value: 7.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGmhmgFNDDRRFPDFSYITqngRLTDFLDCVIISHFHLDHCGALPYfseMVGYDG---PIYMTHPTQAICPI-LLE 76
Cdd:cd16293   25 LLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPY---LVGKLGltcPVYATLPVHKMGRMfMYD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  77 DYRKiavdKKGEANF--FTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYN 151
Cdd:cd16293   95 LYQS----RGLEEDFnlFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGHTLGGTIWKITKDSEDIVYAVDWN 170

                        170       180
                 ....*....|....*....|....*..
gi 374253821 152 MTPDRHL-GAAWIDKC--RPNLLITES 175
Cdd:cd16293  171 HKKERHLnGAVLDSFGglRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 1-172 5.23e-16

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 76.48  E-value: 5.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821    1 MLDCGmhmgFNDDRRFPDFSYITQNgrLTDFLDCVIISHFHLDHCGALPY----FSEMVGYDGPIYMTHPTQAICPI-LL 75
Cdd:pfam16661  10 LLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATLPVANLGRVsTY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   76 EDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNM 152
Cdd:pfam16661  84 DLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAVDWNH 163

                         170       180
                  ....*....|....*....|....*....
gi 374253821  153 TPDRHL-GAAWIDKC--------RPNLLI 172
Cdd:pfam16661 164 TKDSHLnGASLLDSTgkpleslvRPTALI 192
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 349-409 4.59e-15

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 69.57  E-value: 4.59e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253821  349 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 409
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-174 7.73e-14

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: 70.33  E-value: 7.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEmvgyDGPIYMTHPTQAIcpilLEDYRKIAVDKKGEANFFtsqmikdcmkKVVAvhLHQ 111
Cdd:cd07732   76 VDAVLLSHAHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNI----------RVFE--SGK 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253821 112 TVQVDDeLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 174
Cdd:cd07732  136 SFTIGD-FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-155 5.09e-11

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: 61.80  E-value: 5.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821     1 MLDCGMHMGFNDDRRFPDFSYITqngrltdfLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQAicpiLLEDYRK 80
Cdd:smart00849  13 LIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTAE----LLKDLLA 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253821    81 IAVDKKGeanfftsqmIKDCMKKVVAVHLHQTVQVDDElEIKAYYA-GHVLGAAMFqiKVGSESVVYTGDYNMTPD 155
Cdd:smart00849  79 LLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFTGDLLFAGG 142
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 1-150 1.20e-09

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: 58.96  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMHMGFND----DRRFPDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQAICPILLE 76
Cdd:cd07714   24 IIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLLPE--LNVPIYATPLTLALIKKKLE 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374253821  77 DYRKIavdkkGEANFftsqmikdcmkkvVAVHLHQTVQVDDeLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDY 150
Cdd:cd07714   99 EFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPDSVGLAIKTPEGTIVHTGDF 154
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
32-178 1.76e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 52.50  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFTSqmikdcmkKVVAVHLHQ 111
Cdd:COG1234   53 IDAIFITHLHGDHIAGLPGLLSTRSLAGR---EKPLTIYGPPGTKEFLEALLKASGTDLDFPL--------EFHEIEPGE 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821 112 TVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PNLLITESTYA 178
Cdd:COG1234  122 VFEIGG-FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-175 2.24e-07

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 51.11  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  24 QNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPiymTHPTQAICPI-LLEDYRKIavdkkgeanFFTSQMIKDCMK 102
Cdd:cd16272   43 KAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGR---KKPLTIYGPKgIKEFLEKL---------LNFPVEILPLGF 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374253821 103 KVVAVHL--HQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpNLLITES 175
Cdd:cd16272  111 PLEIEELeeGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 1-146 2.34e-07

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: 50.96  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMhmGFNDDRRFPDFSYItqngrltdflDCVIISHFHldHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDyrk 80
Cdd:cd16294   25 MLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGRLLMEE--- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253821  81 iavdkkgeanfftsqmIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVY 146
Cdd:cd16294   88 ----------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISY 137
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-177 4.03e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 51.43  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGmhmgfnddrrfPDFSYITQNGRLT-DFLDCVIISHFHLDHCGALPYFSEMVGYDG-PIYMTHPTQAicpILLEDY 78
Cdd:COG1235   48 LIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLE---ALERRF 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  79 RKIAVDKKGEANFFTsqmikdcmkkvvaVHLHQTVQVDDeLEIKAY----YAGHVLGaamFQIKVGSESVVYTGDYNMTP 154
Cdd:COG1235  114 PYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGGKKLAYATDTGYIP 176

                        170       180
                 ....*....|....*....|...
gi 374253821 155 DRHLgaAWIDKCRpnLLITESTY 177
Cdd:COG1235  177 EEVL--ELLRGAD--LLILDATY 195
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 32-149 6.70e-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: 49.98  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEMvgYDGPIYMTHPTQAicpiLLEDyrkiavdkKGEANFFTSQMIKDCMKKVVAVHLHQ 111
Cdd:cd06262   46 IKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADAE----LLED--------PELNLAFFGGGPLPPPEPDILLEDGD 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 374253821 112 TVQVDDeLEIKAYYA-GHVLGAAMFqiKVGSESVVYTGD 149
Cdd:cd06262  112 TIELGG-LELEVIHTpGHTPGSVCF--YIEEEGVLFTGD 147
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-149 1.28e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.29  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821    1 MLDCGMhmgfndDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEmvgydgpiymTHPTQAICPILLEDYRK 80
Cdd:pfam00753  19 LIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVPVIVVAEEARELL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374253821   81 IAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTvqVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGD 149
Cdd:pfam00753  83 DEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGD 149
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-64 1.62e-06

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 50.83  E-value: 1.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821   1 MLDCGMhmGFNDDRRF------PDFSYITQNGrltDFLDCVIISHFHLDHCGALPYFSEMVgyDGPIYMT 64
Cdd:COG0595   32 IVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDHIGALPYLLKEL--NVPVYGT 94
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 38-149 1.00e-05

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: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  38 SHFHLDHCGAL-PYFSEmvgydGPIYMTHPTQaicpILLEDyrKIAVDKkgeanfftsqmikdcmKKVVAVHLHQTVQVD 116
Cdd:cd16273   43 SHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVKL--KLKVDE----------------EYIVVLPMNTPVEID 95

                         90       100       110
                 ....*....|....*....|....*....|....
gi 374253821 117 DELEIKAYYAGHVLGAAMFQIKV-GSESVVYTGD 149
Cdd:cd16273   96 GDVSVTLLDANHCPGAVMFLFELpDGRRILHTGD 129
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 16-156 5.70e-05

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: 44.89  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  16 FPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDG----PIYMTHPTqaicpilledyrkIAVDKK----G 87
Cdd:cd07735   50 DILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPLLSPNDGGQRgspkTIYGLPET-------------IDALKKhifnW 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253821  88 EA--NFFTSQMIKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDynMTPDR 156
Cdd:cd07735  117 VIwpDFTSIPSGKYPYLRLEPIEPEYPIALTG-LSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 32-175 1.22e-04

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: 42.81  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHC---GALPYFSEMVGYDGPiymTHPTQAICPILLEDYRKIAVDKKGEANFFtsqmikdcmkkvvAVH 108
Cdd:cd07716   51 LDAVVLSHLHPDHCadlGVLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIE 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374253821 109 LHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PNLLITES 175
Cdd:cd07716  115 PGEPLEIGP-FTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 32-66 1.30e-04

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 44.15  E-value: 1.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEMVGyDGPIYMtHP 66
Cdd:cd07713   56 IDAVVLSHGHYDHTGGLKALLELNP-KAPVYA-HP 88
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 32-149 1.70e-04

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: 43.14  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEmvGYDGPIYMTHPTQAicpilledyrkiAVDKKGEANFFTSQMIKDcmkkVVAVHLHQ 111
Cdd:COG0491   52 IKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAE------------ALEAPAAGALFGREPVPP----DRTLEDGD 113

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 374253821 112 TVQVDDeLEIKAYYA-GHVLGAAMFQIKvgSESVVYTGD 149
Cdd:COG0491  114 TLELGG-PGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD 149
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
32-66 9.37e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.41  E-value: 9.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 374253821  32 LDCVIISHFHLDHCGALPYFSEMVGyDGPIYMtHP 66
Cdd:COG1237   58 IDAVVLSHGHYDHTGGLPALLELNP-KAPVYA-HP 90
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 32-51 1.58e-03

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 40.28  E-value: 1.58e-03
                         10        20
                 ....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYF 51
Cdd:cd07729   89 IDYVILSHLHFDHAGGLDLF 108
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-51 8.80e-03

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 37.62  E-value: 8.80e-03
                         10        20
                 ....*....|....*....|
gi 374253821  32 LDCVIISHFHLDHCGALPYF 51
Cdd:cd07740   50 IDAIFITHLHGDHFGGLPFF 69
 
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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