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Conserved domains on  [gi|2075896323|gb|KAG8434346|]
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hypothetical protein GDO86_012649 [Hymenochirus boettgeri]

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 4.44e-163

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: 463.27  E-value: 4.44e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   6 VTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFH 165
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075896323 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITES 204
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 9.83e-120

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 9.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDeLEIKAYYAGHVLGAAMF 164
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 165 HIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDLLITESTYATTIRDSKRCRERDFLKKVHETVEKGGKVLIPVFALG 243
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIrktfvqRNMFEFKHIK----AFDRAFVDNPGP 318
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 319 MVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKILSGQRKLEMEGRqTLEVKMQVE-YMSFSAHADAKG 397
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDE 382

                         410       420
                  ....*....|....*....|
gi 2075896323 398 IMQLIRQAE-PSNVLLVHGE 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGE 402
 
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 4.44e-163

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: 463.27  E-value: 4.44e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   6 VTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFH 165
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075896323 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITES 204
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 9.83e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 9.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDeLEIKAYYAGHVLGAAMF 164
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 165 HIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDLLITESTYATTIRDSKRCRERDFLKKVHETVEKGGKVLIPVFALG 243
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIrktfvqRNMFEFKHIK----AFDRAFVDNPGP 318
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 319 MVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKILSGQRKLEMEGRqTLEVKMQVE-YMSFSAHADAKG 397
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDE 382

                         410       420
                  ....*....|....*....|
gi 2075896323 398 IMQLIRQAE-PSNVLLVHGE 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGE 402
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-363 6.62e-41

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: 144.60  E-value: 6.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  245 AQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFVDNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2075896323  318 PMVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKI 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 6.35e-29

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: 110.68  E-value: 6.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 245 AQELCILLETFWER-MNLKAPIYFSTGLTEKANHYYKLFITWTNQKIRKtfvqrnmfeFKHIKAFDRAFVDNPGPMVVFA 323
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2075896323 324 TPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGY 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 5.08e-18

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 82.26  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  21 LVSIGGKNLMLDCGmhmgYNDDRRFPDFSYITQNgrLTEFLDCVIISHFHLDHCGALPYM----SEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLLyykfGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  97 KAICPI-LLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQV---DDELEIKAYYAGHVLGAAMFHIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075896323 173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPDLLI 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 1.09e-14

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 72.59  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   18 SCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITqngrltefLDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTK 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   98 AicpiLLEDFRKITVDKKGetnfftsqmIKDCMKKVVAVNLHQTVQVDDElEIKAYYA-GHVLGAAMFHIKvgSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 2075896323  177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-207 5.01e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 72.15  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAG---QDVGR--SCILVSIGGKNLMLDCG-------MHMGYNDDRrfpdfsyitqngrltefLDCVIISHFHL 71
Cdd:COG1234     1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  72 DHCGALPYMSEMVGYDG-----PIYMTHPTKAIcpilLEDFRKITvdkKGETNFFTsqmikdcmkKVVAVNLHQTVQVDD 146
Cdd:COG1234    64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKAS---GTDLDFPL---------EFHEIEPGEVFEIGG 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075896323 147 eLEIKAYYAGHVLGAAMFHIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PDLLITESTYA 207
Cdd:COG1234   128 -FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-78 1.12e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 41.32  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAGQ---DVGR--SCILVSIGGKNLMLDCG-------MHMGYnddrRFPDFSYItqngrlteFldcviISHFHL 71
Cdd:PRK00055    2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----KPRKIDKI--------F-----ITHLHG 64


                  ....*..
gi 2075896323  72 DHCGALP 78
Cdd:PRK00055   65 DHIFGLP 71
 
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 4.44e-163

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: 463.27  E-value: 4.44e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   6 VTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFH 165
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075896323 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITES 204
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 9.83e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 9.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDeLEIKAYYAGHVLGAAMF 164
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 165 HIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDLLITESTYATTIRDSKRCRERDFLKKVHETVEKGGKVLIPVFALG 243
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIrktfvqRNMFEFKHIK----AFDRAFVDNPGP 318
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLRfvtsVEESKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 319 MVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKILSGQRKLEMEGRqTLEVKMQVE-YMSFSAHADAKG 397
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDE 382

                         410       420
                  ....*....|....*....|
gi 2075896323 398 IMQLIRQAE-PSNVLLVHGE 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGE 402
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 4-443 4.12e-115

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


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 350.58  E-value: 4.12e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRfpdfsyitQNGRLTEF----LDCVIISHFHLDHCGALPY 79
Cdd:COG1782     1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  80 MSEMvGYDGPIYMTHPTKAICPILLEDFRKI------TVDKKGETN------FFTSQMIKDCMKKVVAVNLHQTVQVDDE 147
Cdd:COG1782    73 LVKY-GYRGPIYCTPPTRDLMALLLLDSAKIqeeeaeYANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 148 LEIKAYYAGHVLGAAMFHIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPDLLITESTYATTIRDSKRCRERDFLKKV 225
Cdd:COG1782   152 IKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 226 HETVEKGGKVLIPVFALGRAQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKT-FVQRNMFEFK 303
Cdd:COG1782   231 NETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 304 HIKAFD-----RAFVDNPGPMVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKILSGQRKLEMEGrQTL 378
Cdd:COG1782   311 NLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFG-ETI 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075896323 379 EVKMQVEYM-SFSAHADAKGIMQLIRQAE--PSNVLLVHGEAKKMEFLKLKIEQEFHINCYMPLNGET 443
Cdd:COG1782   390 PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLET 457
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 7-204 1.88e-94

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: 287.69  E-value: 1.88e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   7 TPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDrrfpdFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVGY 86
Cdd:cd07734     1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  87 DGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFHI 166
Cdd:cd07734    76 RGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEI 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075896323 167 KVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITES 204
Cdd:cd07734   156 QIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 4-204 9.16e-72

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: 229.01  E-value: 9.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYItqngRLTEfLDCVIISHFHLDHCGALPYMSEM 83
Cdd:cd16292     1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEI----DLSE-IDLLLITHFHLDHCGALPYFLQK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  84 VGYDGPIYMTHPTKAICPILLEDFRKITvDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDeLEIKAYYAGHVLGAAM 163
Cdd:cd16292    76 TNFKGRVFMTHPTKAIYKWLLSDYVRVS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAM 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2075896323 164 FHIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITES 204
Cdd:cd16292   154 FMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 6-204 5.22e-64

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: 208.85  E-value: 5.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   6 VTPLGAGQDVGRSCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITQNGRltefLDCVIISHFHLDHCGALPYMSEMvG 85
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----IDAVILTHAHLDHSGRLPLLVKE-G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  86 YDGPIYMTHPTKAICPILLEDFRKI---TVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAA 162
Cdd:cd16295    76 FRGPIYATPATKDLAELLLLDSAKIqeeEAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2075896323 163 MFHIKVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpDLLITES 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 6.62e-41

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: 144.60  E-value: 6.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  245 AQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFVDNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2075896323  318 PMVVFATPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGYKI 363
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 1.23e-31

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: 121.47  E-value: 1.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   7 TPLGAGQDVGRSCILVSIGGKNLMLDCGmhmgYNDDRRFPDFSYITqngRLTEFLDCVIISHFHLDHCGALPYMsemVGY 86
Cdd:cd16293     2 TPLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPYL---VGK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  87 DG---PIYMTHPTKAICPILLEDF---RKITvdkkGETNFFTSQMIKDCMKKVVAVNLHQTVQV---DDELEIKAYYAGH 157
Cdd:cd16293    72 LGltcPVYATLPVHKMGRMFMYDLyqsRGLE----EDFNLFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2075896323 158 VLGAAMFHIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--RPDLLITES 204
Cdd:cd16293   148 TLGGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-361 6.35e-29

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: 110.68  E-value: 6.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 245 AQELCILLETFWER-MNLKAPIYFSTGLTEKANHYYKLFITWTNQKIRKtfvqrnmfeFKHIKAFDRAFVDNPGPMVVFA 323
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2075896323 324 TPGMLHAGQSLLIFRRWAGDEKNMVIMPGYCVQGTVGY 361
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-203 8.16e-20

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: 88.05  E-value: 8.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLGAGQDVGRSCILVSIGGKNLMLDCGM-----------HMGYNDDRRFPDFS------YITQNGRLTE--FLDCVI 65
Cdd:cd07732     1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLpldpeskyfdeVLDFLELGLLPDIVglyrdpLLLGGLRSEEdpSVDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  66 ISHFHLDHCGALPYMSEmvgyDGPIYMTHPTKAIcpilLEDFRKITVDKKGETNFFTsqmikdcmkkvvAVNLHQTVQVD 145
Cdd:cd07732    81 LSHAHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNIR------------VFESGKSFTIG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075896323 146 DeLEIKAYYAGH-VLGAAMFHIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PDLLITE 203
Cdd:cd07732   141 D-FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 21-201 5.08e-18

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 82.26  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  21 LVSIGGKNLMLDCGmhmgYNDDRRFPDFSYITQNgrLTEFLDCVIISHFHLDHCGALPYM----SEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLLyykfGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  97 KAICPI-LLEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQV---DDELEIKAYYAGHVLGAAMFHIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075896323 173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPDLLI 201
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 377-438 9.66e-16

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: 71.88  E-value: 9.66e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075896323 377 TLEVKMQVEYMS-FSAHADAKGIMQLIRQAEPSNVLLVHGEAKKMEFLKLKIEQEFHINCYMP 438
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-179 2.33e-15

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: 75.91  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   7 TPLGaGQD-VGRSCILVSIGGKNLMLDCGMHMGYND----DRRFPDFSYITQNGrltEFLDCVIISHFHLDHCGALPYMS 81
Cdd:cd07714     1 IPLG-GLGeIGKNMYVVEYDDDIIIIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  82 EMvgYDGPIYMTHPTKAICPILLEDFRKItvdkkGETNFftsqmikdcmkkvVAVNLHQTVQVDDeLEIKAYYAGH-VLG 160
Cdd:cd07714    77 PE--LNVPIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPD 135

                         170
                  ....*....|....*....
gi 2075896323 161 AAMFHIKVGSESVVYTGDY 179
Cdd:cd07714   136 SVGLAIKTPEGTIVHTGDF 154
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-184 1.09e-14

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 72.59  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   18 SCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSYITqngrltefLDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTK 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   98 AicpiLLEDFRKITVDKKGetnfftsqmIKDCMKKVVAVNLHQTVQVDDElEIKAYYA-GHVLGAAMFHIKvgSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 2075896323  177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-204 2.01e-14

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: 71.53  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   6 VTPLGAG-----QDVGRSCILVSIGGKNLMLDCG-------MHMGYNDDRrfpdfsyitqngrltefLDCVIISHFHLDH 73
Cdd:cd16272     1 LTFLGTGgavpsLTRNTSSYLLETGGTRILLDCGegtvyrlLKAGVDPDK-----------------LDAIFLSHFHLDH 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  74 CGALPYMSEMVGYDGPiymTHPTKAICPILLEDFRKITVDKKGETNFFTSQMikdcmkKVVAVNLHQTVQVDDELEIKAY 153
Cdd:cd16272    64 IGGLPTLLFARRYGGR---KKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPL------EIEELEEGGEVLELGDLKVEAF 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2075896323 154 YAGHVLGAAMFHIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpDLLITES 204
Cdd:cd16272   135 PVKHSVESLGYRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-207 5.01e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 72.15  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAG---QDVGR--SCILVSIGGKNLMLDCG-------MHMGYNDDRrfpdfsyitqngrltefLDCVIISHFHL 71
Cdd:COG1234     1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  72 DHCGALPYMSEMVGYDG-----PIYMTHPTKAIcpilLEDFRKITvdkKGETNFFTsqmikdcmkKVVAVNLHQTVQVDD 146
Cdd:COG1234    64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKAS---GTDLDFPL---------EFHEIEPGEVFEIGG 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075896323 147 eLEIKAYYAGHVLGAAMFHIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PDLLITESTYA 207
Cdd:COG1234   128 -FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 17-206 1.17e-13

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 71.08  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  17 RSCILVSIGGKNLMLDCGmhmgynddrrfPDFSYITQNGRLT-EFLDCVIISHFHLDHCGALPYMSEMVGYDG-PIYMTH 94
Cdd:COG1235    35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  95 PTKAicpILLEDFRKITVDKKGETNFFTsqmikdcmkkvvaVNLHQTVQVDDeLEIKAY----YAGHVLGaamFHIKVGS 170
Cdd:COG1235   104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2075896323 171 ESVVYTGDYNMTPDRHLgaAWIDKCrpDLLITESTY 206
Cdd:COG1235   164 KKLAYATDTGYIPEEVL--ELLRGA--DLLILDATY 195
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-204 5.25e-11

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: 61.69  E-value: 5.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLG-----AGQDVGRSCILVSIGGKNLMLDCGmhmgynddrrfpdfsyitqNG---RLTEF-----LDCVIISHFHL 71
Cdd:cd07716     1 KLTVLGcsgsyPGPGGACSGYLLEADGFRILLDCG-------------------SGvlsRLQRYidpedLDAVVLSHLHP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  72 DHC---GALPYMSEMVGYDGPiymTHPTKAICPILLEDFRKITVDKKGETNFFtsqmikdcmkkvvAVNLHQTVQVDDeL 148
Cdd:cd07716    62 DHCadlGVLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIEPGEPLEIGP-F 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2075896323 149 EIKAYYAGHVLGAAMFHIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PDLLITES 204
Cdd:cd07716   125 TITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-93 5.30e-11

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 65.47  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   1 MPEIKVTPLGaGQD-VGRSCILVSIGGKNLMLDCGMhmGYNDDRRF------PDFSYITQNGrltEFLDCVIISHFHLDH 73
Cdd:COG0595     3 KDKLRIIPLG-GLGeIGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDH 76

                          90       100
                  ....*....|....*....|
gi 2075896323  74 CGALPYMSEMVgyDGPIYMT 93
Cdd:COG0595    77 IGALPYLLKEL--NVPVYGT 94
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-178 2.19e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.46  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  18 SCILVSIGGKNLMLDCGMhmgyndDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEmvgydgpiymTHPTK 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  98 AICPIllEDFRKITVDKKGETNFFTSQMIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFHIKVGSESVVYTG 177
Cdd:pfam00753  71 VIVVA--EEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 2075896323 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 4.97e-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: 55.58  E-value: 4.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  12 GQDVGRSCILVSIGGKNLMLDCGMhmGYNDDRRFPDFSYItqngrlteflDCVIISHFHldHCGALPYMSEMVGYDGPIY 91
Cdd:cd16294     7 SGHPTLPCNVLKFKSTTIMLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  92 MTHPTKAICPILLEDfrkitvdkkgetnfftsqmIKDCMKKVVAVNLHQTVQVDDELEIKAYYAGHVLGAAMFHIKVGSE 171
Cdd:cd16294    73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                  ....
gi 2075896323 172 SVVY 175
Cdd:cd16294   134 KISY 137
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 5-185 6.75e-08

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: 54.14  E-value: 6.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   5 KVTPLGA--GQDVGR-SCILVSIGGKN--LMLDCG------MHMGYNDDRRFPDfsyITQNGRLTEFLDCVIISHFHLDH 73
Cdd:cd07735     2 ELVVLGCsgGPDEGNtSSFLLDPAGSDgdILLDAGtgvgalSLEEMFNDILFPS---QKAAYELYQRIRHYLITHAHLDH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  74 CGALPYMSEMVGYDGpiymtHPTKAICPIlledfrKITVDKKGETNF-------FTSQMIKDCMKKVVAVNLHQTVQVDD 146
Cdd:cd07735    79 IAGLPLLSPNDGGQR-----GSPKTIYGL------PETIDALKKHIFnwviwpdFTSIPSGKYPYLRLEPIEPEYPIALT 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2075896323 147 ELEIKAYYAGH-VLGAAMFHIKVGSESVVYTGDynMTPDR 185
Cdd:cd07735   148 GLSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 18-207 4.38e-07

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: 51.30  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  18 SCILVSIGGKNLMLDCG-------MHMGYnddrRFPDfsyitqngrltefLDCVIISHFHLDHCGALP----YMSeMVGY 86
Cdd:cd07717    18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SPSK-------------IDRIFITHLHGDHILGLPgllsTMS-LLGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  87 DGP--IYMTHPTKAIcpilLEDFRKITvdkKGETNFFTsqmikdcmkKVVAVNLHQTVQVDDE-LEIKAYYAGHVLGAAM 163
Cdd:cd07717    80 TEPltIYGPKGLKEF----LETLLRLS---ASRLPYPI---------EVHELEPDPGLVFEDDgFTVTAFPLDHRVPCFG 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2075896323 164 FHIKVGSeSVVYTGDyNMTPDRHLGAAWidkcRPDLLITESTYA 207
Cdd:cd07717   144 YRFEEGR-KIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 61-178 4.49e-07

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 50.36  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  61 LDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTKAicpiLLEDfrkitvdkKGETNFFTSQMIKDCMKKVVAVNLHQ 140
Cdd:cd06262    46 IKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADAE----LLED--------PELNLAFFGGGPLPPPEPDILLEDGD 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2075896323 141 TVQVDDeLEIKAYYA-GHVLGAAMFHIKvgSESVVYTGD 178
Cdd:cd06262   112 TIELGG-LELEVIHTpGHTPGSVCFYIE--EEGVLFTGD 147
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 67-206 2.19e-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: 47.92  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  67 SHFHLDHcgalpYMsemvGYD-----GPIYMTHPTKaicpILLEDfrKITVDKKgetnfftsqmikdcmkKVVAVNLHQT 141
Cdd:cd16273    43 SHFHSDH-----YG----GLTkswshGPIYCSEITA----NLVKL--KLKVDEE----------------YIVVLPMNTP 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075896323 142 VQVDDELEIKAYYAGHVLGAAMFHIKV-GSESVVYTGDYNMTPDRHLGAAWIDKCRPDLLITESTY 206
Cdd:cd16273    92 VEIDGDVSVTLLDANHCPGAVMFLFELpDGRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTTY 157
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-78 1.36e-05

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: 45.97  E-value: 1.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075896323   5 KVTPLGAG---QDVGR--SCILVSIGGKNLMLDCGMHMGynddRRFpdfsyiTQNGRLTEFLDCVIISHFHLDHCGALP 78
Cdd:cd07719     1 RVTLLGTGgpiPDPDRagPSTLVVVGGRVYLVDAGSGVV----RRL------AQAGLPLGDLDAVFLTHLHSDHVADLP 69
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 14-79 2.00e-05

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: 46.39  E-value: 2.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075896323  14 DVGR-SCILV-SIGGKNLMLDCGmhmgynddrrfPDFSYITQNGRLTEFL--------DCVIISHFHLDHCGALPY 79
Cdd:COG2333     7 DVGQgDAILIrTPDGKTILIDTG-----------PRPSFDAGERVVLPYLralgirrlDLLVLTHPDADHIGGLAA 71
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-79 2.06e-05

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: 45.20  E-value: 2.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075896323  14 DVGRS-CILVSIGGKNLMLDCGMHMGYNDDRRFPdfsYITQNGRLTefLDCVIISHFHLDHCGALPY 79
Cdd:cd07731     6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGIKK--LDYLILTHPDADHIGGLDA 67
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-178 4.76e-05

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 45.07  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  19 CILVSIGGKNLMLDCGMhmGYNDDRRFPDfsYITQNGRLtefLDCVIISHFHLDHCGALPYMSEmvGYDGPIYMTHPTKA 98
Cdd:COG0491    17 SYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALGLD---IKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  99 IcpilledfrkitVDKKGETNFFTSQMIKDcmkkVVAVNLHQTVQVDDeLEIKAYYA-GHVLGAAMFHIKvgSESVVYTG 177
Cdd:COG0491    88 A------------LEAPAAGALFGREPVPP----DRTLEDGDTLELGG-PGLEVIHTpGHTPGHVSFYVP--DEKVLFTG 148


                  .
gi 2075896323 178 D 178
Cdd:COG0491   149 D 149
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-79 1.44e-04

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: 43.74  E-value: 1.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075896323  18 SCILVSIGGKNLMLDCGMHMGYNDDRRFPDFSY---ITQNGRLTEFL----------DCVIISHFHLDHCGALPY 79
Cdd:cd07729    33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgVTEEQTLEEQLarlgldpediDYVILSHLHFDHAGGLDL 107
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-96 1.88e-04

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: 42.85  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  17 RSCILVSIGGKNLMLDCGmhmgynddrrfPDFSY------ITQngrltefLDCVIISHFHLDHCGALP---YMSEMVGYD 87
Cdd:cd16279    35 RSSILIETGGKNILIDTG-----------PDFRQqalragIRK-------LDAVLLTHAHADHIHGLDdlrPFNRLQQRP 96


                  ....*....
gi 2075896323  88 GPIYMTHPT 96
Cdd:cd16279    97 IPVYASEET 105
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 19-95 2.69e-04

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 42.99  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  19 CILVSIGGKNLMLDCGM---------HMGYNDDRrfpdfsyitqngrltefLDCVIISHFHLDHCGALPYMSEMVGyDGP 89
Cdd:cd07713    22 SLLIETEGKKILFDTGQsgvllhnakKLGIDLSD-----------------IDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                  ....*.
gi 2075896323  90 IYMtHP 95
Cdd:cd07713    84 VYA-HP 88
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-78 1.12e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 41.32  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323   4 IKVTPLGAGQ---DVGR--SCILVSIGGKNLMLDCG-------MHMGYnddrRFPDFSYItqngrlteFldcviISHFHL 71
Cdd:PRK00055    2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----KPRKIDKI--------F-----ITHLHG 64


                  ....*..
gi 2075896323  72 DHCGALP 78
Cdd:PRK00055   65 DHIFGLP 71
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 18-186 6.73e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 38.04  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  18 SCILVSIGGKNLMLDCGMHMGynddrrfpdfSYITQNGRLTEFLDCVIISHFHLDHCGALPYMsemvgydgpiymthptk 97
Cdd:cd07738    16 SGFIIWINGRGIMVDPPVNST----------SYLRQNGISPRLVDHVILTHCHADHDAGTFQK----------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  98 aicpILLEDfrKITVdkkgetnfFTSQMIKDC-MKKVVAVNL-----------HQTVQVDDELEI-----KAYYAGHVLG 160
Cdd:cd07738    69 ----ILEEE--KITL--------YTTRTINESfLRKYAALTGlppdfleelfdFRPVIIGEKTKIngaefEFDYSFHSIP 134

                         170       180
                  ....*....|....*....|....*.
gi 2075896323 161 AAMFHIKVGSESVVYTGDYNMTPDRH 186
Cdd:cd07738   135 TIRFKVSYGGKSIAYSGDTRYDPDGL 160
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
61-95 8.31e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 38.33  E-value: 8.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2075896323  61 LDCVIISHFHLDHCGALPYMSEMVGyDGPIYMtHP 95
Cdd:COG1237    58 IDAVVLSHGHYDHTGGLPALLELNP-KAPVYA-HP 90
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 61-208 8.60e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 37.67  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  61 LDCVIISHFHLDHCGALPYMSEmvGYDGPIYMTHPTKAicpILLEDFRKITVDKKGETNfftsqmikdcmkkVVAVNLHQ 140
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLRE--GRPRPLYAPLGVLA---HLRRNFPYLFLLEHYGVR-------------VHEIDWGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323 141 TVQVDDE-LEIKA------------YYAGHVLGaamFHIKVGSESVVYTGDYNMTPD---RHLGAAwidkcrpDLLITES 204
Cdd:pfam12706  91 SFTVGDGgLTVTAtparhgsprgldPNPGDTLG---FRIEGPGKRVYYAGDTGYFPDeigERLGGA-------DLLLLDG 160


                  ....
gi 2075896323 205 TYAT 208
Cdd:pfam12706 161 GAWR 164
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 18-206 8.66e-03

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: 37.86  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  18 SCILVSIGGKNLMLDCGMHMgynddRRFPDfsYITQNGRLTEFLdcVIISHFHLDH-CGaLPYMsemvgydGPIYMTHpt 96
Cdd:cd07715    24 SCVEVRAGGELLILDAGTGI-----RELGN--ELMKEGPPGEAH--LLLSHTHWDHiQG-FPFF-------APAYDPG-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075896323  97 kaicpilledfRKITV-----DKKGETNFFTSQM--------IKDCMKKVVAVNL--HQTVQVDDeLEIKAYYAGHVLGA 161
Cdd:cd07715    85 -----------NRIHIygphkDGGSLEEVLRRQMsppyfpvpLEELLAAIEFHDLepGEPFSIGG-VTVTTIPLNHPGGA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2075896323 162 AMFHIKVGSESVVYTGDYNMTP-DRHLGAAWIDKCR-PDLLITESTY 206
Cdd:cd07715   153 LGYRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
 
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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