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Conserved domains on  [gi|15219848|ref|NP_176297|]
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cleavage and polyadenylation specificity factor 73-I [Arabidopsis thaliana]

Protein Classification

MBL fold metallo-hydrolase; INTS11 family MBL fold metallo-hydrolase( domain architecture ID 11611285)

uncharacterized member of the MBL fold metallo-hydrolase superfamily similar to Thermus thermophilus ribonuclease TTHA0252, which exhibits endoribonuclease activity towards 23S and 16S rRNA in vitro and may function in RNA degradation; 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
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 22-215 1.21e-141

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: 411.59  E-value: 1.21e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  22 LIVTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNG 101
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 102 RVFMTHATKAIYKLLLTDYVKVSKVSVEDMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAG 181
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 15219848 182 VRILYTGDYSREEDRHLRAAELPQFSPDICIIES 215
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 24-430 4.18e-114

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 349.10  E-value: 4.18e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYfdEIDPSSIDVLLITHFHIDHAASLPYfLEKTTFNGRV 103
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 104 FMTHATKAIYKLLLTDYVKVSKVSVEDM-LFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAGV 182
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 183 RILYTGDYSREEDRHLRAAELPQfSPDICIIESTSGVQLHQSRHIREKRFTDVIHSTVAQGGRVLIPAFALGRAQELLLI 262
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 263 LDEYWANHpDLHNIPIyYASPLAKKCMAVYQTYILSMNDRIRnqfansNPFVFKHISPLNSIDD---FNDVGPSVVMATP 339
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 340 GGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTIINEPKEVTLMnGLTAPLNMQVH-YISFSAHADYAQTSTFLKE 418
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIF-GEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|...
gi 15219848 419 L-MPPNIILVHGE 430
Cdd:COG1236 390 TgKPERVFLVHGE 402
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-687 1.05e-68

Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.


:

Pssm-ID: 463330  Cd Length: 204  Bit Score: 223.53  E-value: 1.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   486 DTVSGILVKKGFTYQIMAPDELHVFSQLSTATVTQRITIPFVGAFGVIKHRLEKIFESVEFSTDEEsGLPALKVHERVTV 565
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKE-GKPTLRVMGCVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   566 KQEsEKHISLQWSSDPISDMVSDSIVALILNISREvPKIVMEEEDAVKSEEENGKKVE--KVIYALLVSLFGDVKLGE-- 641
Cdd:pfam11718  80 TVE-KGEVTLEWEGNPVNDMIADSVLAVLLSVESS-PASVKLSELPLRNPHAESDPEEriERLIMLLEAQFGEDCVIElp 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15219848   642 -NGKLVIRVDGNVAQLDKESGEVESEHSGLKERVRVAFERIQSAVKP 687
Cdd:pfam11718 158 kVPGLEVTVDGKVANIDLETLEVECEDEVLKDRVETVVERAVEAVAP 204
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 22-215 1.21e-141

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: 411.59  E-value: 1.21e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  22 LIVTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNG 101
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 102 RVFMTHATKAIYKLLLTDYVKVSKVSVEDMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAG 181
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 15219848 182 VRILYTGDYSREEDRHLRAAELPQFSPDICIIES 215
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 24-430 4.18e-114

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 349.10  E-value: 4.18e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYfdEIDPSSIDVLLITHFHIDHAASLPYfLEKTTFNGRV 103
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 104 FMTHATKAIYKLLLTDYVKVSKVSVEDM-LFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAGV 182
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 183 RILYTGDYSREEDRHLRAAELPQfSPDICIIESTSGVQLHQSRHIREKRFTDVIHSTVAQGGRVLIPAFALGRAQELLLI 262
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 263 LDEYWANHpDLHNIPIyYASPLAKKCMAVYQTYILSMNDRIRnqfansNPFVFKHISPLNSIDD---FNDVGPSVVMATP 339
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 340 GGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTIINEPKEVTLMnGLTAPLNMQVH-YISFSAHADYAQTSTFLKE 418
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIF-GEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|...
gi 15219848 419 L-MPPNIILVHGE 430
Cdd:COG1236 390 TgKPERVFLVHGE 402
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-687 1.05e-68

Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.


Pssm-ID: 463330  Cd Length: 204  Bit Score: 223.53  E-value: 1.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   486 DTVSGILVKKGFTYQIMAPDELHVFSQLSTATVTQRITIPFVGAFGVIKHRLEKIFESVEFSTDEEsGLPALKVHERVTV 565
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKE-GKPTLRVMGCVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   566 KQEsEKHISLQWSSDPISDMVSDSIVALILNISREvPKIVMEEEDAVKSEEENGKKVE--KVIYALLVSLFGDVKLGE-- 641
Cdd:pfam11718  80 TVE-KGEVTLEWEGNPVNDMIADSVLAVLLSVESS-PASVKLSELPLRNPHAESDPEEriERLIMLLEAQFGEDCVIElp 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15219848   642 -NGKLVIRVDGNVAQLDKESGEVESEHSGLKERVRVAFERIQSAVKP 687
Cdd:pfam11718 158 kVPGLEVTVDGKVANIDLETLEVECEDEVLKDRVETVVERAVEAVAP 204
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 484-688 4.18e-51

This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins; The exact function of this domain is not known.


Pssm-ID: 215023  Cd Length: 212  Bit Score: 176.45  E-value: 4.18e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    484 VGDTVSGILVKKGFTYQIMAPDELHVFSQLSTATVTQRITIPFVGAFGVIKHRLEKIFESVEFSTD----EESGLPALKV 559
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPSSASLLLVLLELMFEFGFVEEDvdeeEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    560 HERVTVKQESEKHIsLQWSSDPISDMVSDSIVALILNISREVPKIVMEEEDAVKSEEENGKKVE-KVIYALLVSLFGD-- 636
Cdd:smart01098  81 MGDVTVTYSGHMLV-LEWESSPVNDMDADSDSAIILLISSEPSPAKVKSSSKSKHHHHNDEEFReKLIEILLKEQFGDgv 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15219848    637 VKLGENGKLVIRVDGNVAQLDKESGEV-ESEHSGLKERVRVAFERIQSAVKPI 688
Cdd:smart01098 160 VNVEEGEDLKVTVDGKTANIDLETLKVvEEDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 256-377 9.60e-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: 144.99  E-value: 9.60e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    256 AQELLLILDEYWANHpDLHNIPIYYASPLAKKCMAVYQTYILSMNDRIRNQFANS-NPFVFKHISPLNSIDDF----NDV 330
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGrNPFDFKNLKFVKSLEESkrlnDYK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 15219848    331 GPSVVMATPGGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTI 377
Cdd:smart01027  80 GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 256-375 7.01e-33

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: 122.24  E-value: 7.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   256 AQELLLILDEYWANHPdLHNIPIYYASPLAKKCMAVYQTYILSMNDRIRNQFANSNpfvfkhisplNSIDDFNDVGPSVV 335
Cdd:pfam10996   1 AQELLYLLDELWREGR-LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKS----------ESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15219848   336 MATPGGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAK 375
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
24-261 1.99e-17

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 82.55  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGR-----SCVYMSFRGKNILFDCGihpaySG-MAALPYFDeIDPSSIDVLLITHFHIDHAASLPYFLEKT 97
Cdd:COG1234   3 LTFLGTGGAVPTpgratSSYLLEAGGERLLIDCG-----EGtQRQLLRAG-LDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  98 TFNGR-----VFMTHATKAIYKLLLtdyvkvsKVSVEDMLFDeqdinksmdkIEVIDFH--QTVEVNGIKFWCYTAGHVL 170
Cdd:COG1234  77 SLAGRekpltIYGPPGTKEFLEALL-------KASGTDLDFP----------LEFHEIEpgEVFEIGGFTVTAFPLDHPV 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 171 GAAMFMVDIAGVRILYTGD--YSREEDRHLRAAelpqfspDICIIESTSgvqLHQSRHIREKRFtdviHSTVAQGGRVLi 248
Cdd:COG1234 140 PAYGYRFEEPGRSLVYSGDtrPCEALVELAKGA-------DLLIHEATF---LDEEAELAKETG----HSTAKEAAELA- 204

                       250
                ....*....|...
gi 15219848 249 pafALGRAQELLL 261
Cdd:COG1234 205 ---AEAGVKRLVL 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-189 3.08e-17

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: 79.90  E-value: 3.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848     36 SCVYMSFRGKNILFDCGIHPAysgMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKttFNGRVFMTHATKAIYKL 115
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA---EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219848    116 LLTDYVKVSkvsvedmlfdeqDINKSMDKIEVIDFHQTVEVNGIKFWC-YTAGHVLGAAMFMVDiaGVRILYTGD 189
Cdd:smart00849  76 LLALLGELG------------AEAEPAPPDRTLKDGDELDLGGGELEViHTPGHTPGSIVLYLP--EGKILFTGD 136
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-196 5.59e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    36 SCVYMSFRGKNILFDCGIHPAYSGMAALpYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNGRVFMTHATKAIYKL 115
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLL-AALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   116 LLTDYvkvskvsvedMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAGVRILYTGD--YSRE 193
Cdd:pfam00753  86 LGLAA----------SRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllFAGE 155


                  ...
gi 15219848   194 EDR 196
Cdd:pfam00753 156 IGR 158
PRK00055 PRK00055
ribonuclease Z; Reviewed
 24-261 2.65e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 49.41  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   24 VTPLGAGSEV---GR--SCVYMSFRGKNILFDCGihpaySG----MAALPyfdeIDPSSIDVLLITHFHIDHAASLPYFL 94
Cdd:PRK00055   4 LTFLGTGSGVptpTRnvSSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   95 EKTTFNGRvfmTHATKAIYKLLLTDYVKVSKVSVEDM--LFDEQDIN--------KSMDKIEVIDFHQ-----TVEVNGi 159
Cdd:PRK00055  75 STRSLSGR---TEPLTIYGPKGIKEFVETLLRASGSLgyRIAEKDKPgkldaeklKALGVPPGPLFGKlkrgeDVTLED- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  160 kfwcytaGHVLGAAMFM-VDIAGVRILYTGD--YSREEDRHLRAAelpqfspDICIIESTSGvqlHQSRHIREKRFtdvi 236
Cdd:PRK00055 151 -------GRIINPADVLgPPRKGRKVAYCGDtrPCEALVELAKGA-------DLLVHEATFG---DEDEELAKEYG---- 209

                        250       260
                 ....*....|....*....|....*.
gi 15219848  237 HSTVAQGGRVlipafAL-GRAQELLL 261
Cdd:PRK00055 210 HSTARQAAEI-----AKeAGVKRLIL 230
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 22-215 1.21e-141

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: 411.59  E-value: 1.21e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  22 LIVTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNG 101
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 102 RVFMTHATKAIYKLLLTDYVKVSKVSVEDMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAG 181
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 15219848 182 VRILYTGDYSREEDRHLRAAELPQFSPDICIIES 215
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 24-430 4.18e-114

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 349.10  E-value: 4.18e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYfdEIDPSSIDVLLITHFHIDHAASLPYfLEKTTFNGRV 103
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 104 FMTHATKAIYKLLLTDYVKVSKVSVEDM-LFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAGV 182
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 183 RILYTGDYSREEDRHLRAAELPQfSPDICIIESTSGVQLHQSRHIREKRFTDVIHSTVAQGGRVLIPAFALGRAQELLLI 262
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 263 LDEYWANHpDLHNIPIyYASPLAKKCMAVYQTYILSMNDRIRnqfansNPFVFKHISPLNSIDD---FNDVGPSVVMATP 339
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 340 GGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTIINEPKEVTLMnGLTAPLNMQVH-YISFSAHADYAQTSTFLKE 418
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIF-GEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|...
gi 15219848 419 L-MPPNIILVHGE 430
Cdd:COG1236 390 TgKPERVFLVHGE 402
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 24-463 1.72e-109

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: 339.03  E-value: 1.72e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHP-----AYSGMAALPyfdeIDPSSIDVLLITHFHIDHAASLPYfLEKTT 98
Cdd:COG1782   3 ITFLGAAREVTGSCHLLETGESRILLDCGLFQggreeRERNNDAFP----FDPEELDAVVLTHAHLDHSGLLPL-LVKYG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  99 FNGRVFMTHATKAIYKLLLTDYVKV-------------SKVSVEDMLFDEQDINKSMDKIEVIDFHQTVEVN-GIKFWCY 164
Cdd:COG1782  78 YRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 165 TAGHVLGAAMFMVDIAG--VRILYTGDYSREEDRHLRAaelPQFSP--DICIIESTSGVQLHQSRHIREKRFTDVIHSTV 240
Cdd:COG1782 158 NAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTPLLRP---PTPFPraDTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 241 AQGGRVLIPAFALGRAQELLLILDEYWANHpDLHNIPIYYASPLAKKCMAVYQTYILSMNDRIRNQ-FANSNPFVFKHIS 319
Cdd:COG1782 235 ERGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLH 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 320 PLNSIDD----FNDVGPSVVMATPGGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTIINEPKEVTlMNGLTAPLN 395
Cdd:COG1782 314 YVESVEEskeiNDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVK-IFGETIPVR 392

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219848 396 MQVHYI-SFSAHADYAQTSTFLKELMPP--NIILVHGEANEMMRLKQKLLTEFpdgNTKIMTPKNCESVEM 463
Cdd:COG1782 393 AEVETIdGFSGHADRNELLNWLRRLKPKpkKVFLVHGEPEAAEALASSIRKKL---GIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 25-215 1.05e-72

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: 233.38  E-value: 1.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  25 TPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNGRVF 104
Cdd:cd07734   1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 105 MTHATKAIYKLLLTDYVKVSKVSVEDM-LFDEQDINKSMDKIEVIDFHQTVEVN-GIKFWCYTAGHVLGAAMFMVDIAGV 182
Cdd:cd07734  81 ATHPTVALGRLLLEDYVKSAERIGQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGE 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15219848 183 RILYTGDYSREEDRHLRAAELPQFSPDICIIES 215
Cdd:cd07734 161 KLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 24-215 3.16e-71

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: 229.84  E-value: 3.16e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPS-----SIDVLLITHFHIDHAASLPYFLEKTT 98
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNgpfteHIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  99 FNGRVFMTHATKAIYKLLLTDYVKVS-KVSVEDMLFDEQDINKSMDKIEVIDFHQTVEV-NGIKFWCYTAGHVLGAAMFM 176
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15219848 177 VDIAGVRILYTGDYSREEDRHLRAAELPQFSPDICIIES 215
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-687 1.05e-68

Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.


Pssm-ID: 463330  Cd Length: 204  Bit Score: 223.53  E-value: 1.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   486 DTVSGILVKKGFTYQIMAPDELHVFSQLSTATVTQRITIPFVGAFGVIKHRLEKIFESVEFSTDEEsGLPALKVHERVTV 565
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKE-GKPTLRVMGCVTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   566 KQEsEKHISLQWSSDPISDMVSDSIVALILNISREvPKIVMEEEDAVKSEEENGKKVE--KVIYALLVSLFGDVKLGE-- 641
Cdd:pfam11718  80 TVE-KGEVTLEWEGNPVNDMIADSVLAVLLSVESS-PASVKLSELPLRNPHAESDPEEriERLIMLLEAQFGEDCVIElp 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15219848   642 -NGKLVIRVDGNVAQLDKESGEVESEHSGLKERVRVAFERIQSAVKP 687
Cdd:pfam11718 158 kVPGLEVTVDGKVANIDLETLEVECEDEVLKDRVETVVERAVEAVAP 204
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 24-215 8.20e-55

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: 186.13  E-value: 8.20e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGMAALPYFD-EIDPSSIDVLLITHFHIDHAASLPYfLEKTTFNGR 102
Cdd:cd16295   1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPfPFDPKEIDAVILTHAHLDHSGRLPL-LVKEGFRGP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 103 VFMTHATKAIYKLLLTDYVKVSKVSVEDM----LFDEQDINKSMDKIEVIDFHQTVEVN-GIKFWCYTAGHVLGAAMFMV 177
Cdd:cd16295  80 IYATPATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVEL 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15219848 178 DI-AGVRILYTGDYSREEDRHLRAAELPQFsPDICIIES 215
Cdd:cd16295 160 EIgGGKRILFSGDLGRKNTPLLRDPAPPPE-ADYLIMES 197
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 484-688 4.18e-51

This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins; The exact function of this domain is not known.


Pssm-ID: 215023  Cd Length: 212  Bit Score: 176.45  E-value: 4.18e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    484 VGDTVSGILVKKGFTYQIMAPDELHVFSQLSTATVTQRITIPFVGAFGVIKHRLEKIFESVEFSTD----EESGLPALKV 559
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPSSASLLLVLLELMFEFGFVEEDvdeeEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    560 HERVTVKQESEKHIsLQWSSDPISDMVSDSIVALILNISREVPKIVMEEEDAVKSEEENGKKVE-KVIYALLVSLFGD-- 636
Cdd:smart01098  81 MGDVTVTYSGHMLV-LEWESSPVNDMDADSDSAIILLISSEPSPAKVKSSSKSKHHHHNDEEFReKLIEILLKEQFGDgv 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15219848    637 VKLGENGKLVIRVDGNVAQLDKESGEV-ESEHSGLKERVRVAFERIQSAVKPI 688
Cdd:smart01098 160 VNVEEGEDLKVTVDGKTANIDLETLKVvEEDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 256-377 9.60e-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: 144.99  E-value: 9.60e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    256 AQELLLILDEYWANHpDLHNIPIYYASPLAKKCMAVYQTYILSMNDRIRNQFANS-NPFVFKHISPLNSIDDF----NDV 330
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGrNPFDFKNLKFVKSLEESkrlnDYK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 15219848    331 GPSVVMATPGGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAKTI 377
Cdd:smart01027  80 GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 256-375 7.01e-33

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: 122.24  E-value: 7.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   256 AQELLLILDEYWANHPdLHNIPIYYASPLAKKCMAVYQTYILSMNDRIRNQFANSNpfvfkhisplNSIDDFNDVGPSVV 335
Cdd:pfam10996   1 AQELLYLLDELWREGR-LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKS----------ESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15219848   336 MATPGGLQSGLSRQLFDSWCSDKKNACIIPGYMVEGTLAK 375
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
24-261 1.99e-17

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 82.55  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGR-----SCVYMSFRGKNILFDCGihpaySG-MAALPYFDeIDPSSIDVLLITHFHIDHAASLPYFLEKT 97
Cdd:COG1234   3 LTFLGTGGAVPTpgratSSYLLEAGGERLLIDCG-----EGtQRQLLRAG-LDPRDIDAIFITHLHGDHIAGLPGLLSTR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  98 TFNGR-----VFMTHATKAIYKLLLtdyvkvsKVSVEDMLFDeqdinksmdkIEVIDFH--QTVEVNGIKFWCYTAGHVL 170
Cdd:COG1234  77 SLAGRekpltIYGPPGTKEFLEALL-------KASGTDLDFP----------LEFHEIEpgEVFEIGGFTVTAFPLDHPV 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 171 GAAMFMVDIAGVRILYTGD--YSREEDRHLRAAelpqfspDICIIESTSgvqLHQSRHIREKRFtdviHSTVAQGGRVLi 248
Cdd:COG1234 140 PAYGYRFEEPGRSLVYSGDtrPCEALVELAKGA-------DLLIHEATF---LDEEAELAKETG----HSTAKEAAELA- 204

                       250
                ....*....|...
gi 15219848 249 pafALGRAQELLL 261
Cdd:COG1234 205 ---AEAGVKRLVL 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-189 3.08e-17

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: 79.90  E-value: 3.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848     36 SCVYMSFRGKNILFDCGIHPAysgMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKttFNGRVFMTHATKAIYKL 115
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA---EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219848    116 LLTDYVKVSkvsvedmlfdeqDINKSMDKIEVIDFHQTVEVNGIKFWC-YTAGHVLGAAMFMVDiaGVRILYTGD 189
Cdd:smart00849  76 LLALLGELG------------AEAEPAPPDRTLKDGDELDLGGGELEViHTPGHTPGSIVLYLP--EGKILFTGD 136
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 25-215 1.16e-16

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: 78.72  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  25 TPLGAGSEVGRSCVYMSFRGKNILFDCGihpaYSGMAALPYFDEIDP--SSIDVLLITHFHIDHAASLPYFLEKTTFNGR 102
Cdd:cd16293   2 TPLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLKRiaPTIDAVLLSHPDLEHLGALPYLVGKLGLTCP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 103 VFMTHATKAIYKLLLTDYVKvSKVSVEDM-LFDEQDINKSMDKIEVIDFHQTVEV----NGIKFWCYTAGHVLGAAMFMV 177
Cdd:cd16293  78 VYATLPVHKMGRMFMYDLYQ-SRGLEEDFnLFTLDDVDEAFDRITQLKYSQPVNLrgkgDGLTITAYNAGHTLGGTIWKI 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15219848 178 DIAGVRILYTGDYSREEDRHLRAAELPQFS---PDICIIES 215
Cdd:cd16293 157 TKDSEDIVYAVDWNHKKERHLNGAVLDSFGglrPSLLITDA 197
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
36-196 5.59e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    36 SCVYMSFRGKNILFDCGIHPAYSGMAALpYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNGRVFMTHATKAIYKL 115
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLL-AALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   116 LLTDYvkvskvsvedMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGHVLGAAMFMVDIAGVRILYTGD--YSRE 193
Cdd:pfam00753  86 LGLAA----------SRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllFAGE 155


                  ...
gi 15219848   194 EDR 196
Cdd:pfam00753 156 IGR 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 35-216 6.34e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 75.32  E-value: 6.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  35 RSCVYMSFRGKNILFDCGIhpaysGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNG-RVFMTHATKAiy 113
Cdd:COG1235  35 RSSILVEADGTRLLIDAGP-----DLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLE-- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 114 kllltdyvkvskvSVEDMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWCYTAGH-VLGAAMFMVDIAGVRILY---TGD 189
Cdd:COG1235 108 -------------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHdAGDPVGYRIEDGGKKLAYatdTGY 174

                       170       180
                ....*....|....*....|....*..
gi 15219848 190 YSREEDRHLRAAelpqfspDICIIEST 216
Cdd:COG1235 175 IPEEVLELLRGA-------DLLILDAT 194
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 24-203 3.53e-13

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: 68.44  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEV-----GRSCVYMSFRGKNILFDCGIHPAYSGMAALpyfdeIDPSSIDVLLITHFHIDHAASLPYFLEKTT 98
Cdd:cd16272   1 LTFLGTGGAVpsltrNTSSYLLETGGTRILLDCGEGTVYRLLKAG-----VDPDKLDAIFLSHFHLDHIGGLPTLLFARR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  99 FNGR-----VFMTHATKAIYKLLLTDYVKVSKVSvEDMLFDEQDINksmdkievidfHQTVEVNGIKFWCYTAGHVLGAA 173
Cdd:cd16272  76 YGGRkkpltIYGPKGIKEFLEKLLNFPVEILPLG-FPLEIEELEEG-----------GEVLELGDLKVEAFPVKHSVESL 143

                       170       180       190
                ....*....|....*....|....*....|..
gi 15219848 174 MFMVDIAGVRILYTGD--YSREEDRHLRAAEL 203
Cdd:cd16272 144 GYRIEAEGKSIVYSGDtgPCENLVELAKGADL 175
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-190 9.68e-13

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: 67.64  E-value: 9.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEVGRSCVYMSFRGKNILFDCG------------------------IHPAYSGMAALPYFDEIDPSSIDVLLI 79
Cdd:cd07732   2 ITIHRGTNEIGGNCIEVETGGTRILLDFGlpldpeskyfdevldflelgllpdIVGLYRDPLLLGGLRSEEDPSVDAVLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  80 THFHIDHAASLPYFLEKTTfngrVFMTHATKAIYKLLLTdyvkvskvsvedmLFDEQDINKSmdKIEVIDFHQTVEVNGI 159
Cdd:cd07732  82 SHAHLDHYGLLNYLRPDIP----VYMGEATKRILKALLP-------------FFGEGDPVPR--NIRVFESGKSFTIGDF 142

                       170       180       190
                ....*....|....*....|....*....|..
gi 15219848 160 KFWCYTAGH-VLGAAMFMVDIAGVRILYTGDY 190
Cdd:cd07732 143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDF 174
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 40-203 1.46e-12

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 66.85  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    40 MSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSsIDVLLITHFHIDHAASLPYFLEKttFNGRVFMT---HATKAIYKL- 115
Cdd:pfam16661   2 LEFDNVRILLDPGWDGSFSYESDLKYLEKILPE-VDLILLSHPTLEHLGAYPLLYYK--FGSHLGSNipvYATLPVANLg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   116 ---LLTDYVKVSKV-SVEDMLFDEQDINKSMDKIEVIDFHQTVEV----NGIKFWCYTAGHVLGAAMFMVDIAGVRILYT 187
Cdd:pfam16661  79 rvsTYDLYASRGILgPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIVYA 158

                         170
                  ....*....|....*.
gi 15219848   188 GDYSREEDRHLRAAEL 203
Cdd:pfam16661 159 VDWNHTKDSHLNGASL 174
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 391-445 1.38e-11

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: 59.94  E-value: 1.38e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219848   391 TAPLNMQVHYIS-FSAHADYAQTSTFLKELMPPNIILVHGEANEMMRLKQKLLTEF 445
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL 56
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 30-186 6.75e-11

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: 61.36  E-value: 6.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  30 GSEVGRSCVYMSFRGKNILFDCGIhpaysgmAALPYFDEIDPSSIDVLLITHFHidHAASLPYFLEKTTFNGRVFMTHAT 109
Cdd:cd16294   7 SGHPTLPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPT 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219848 110 KAIYKLLLTDYVkvskvsvedmlfdeqdinKSMDKIEVIDFHQTVEVNG-IKFWCYTAGHVLGAAMFMVDIAGVRILY 186
Cdd:cd16294  78 VQIGRLLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQSHYEKISY 137
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 44-189 2.19e-10

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: 60.38  E-value: 2.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  44 GKNILFDCGIHPAYSGMAALpyfdEIDPSSIDVLLITHFHIDHAASLPYFLEKttFNGRVFMTHATKAiyklLLTDyvkv 123
Cdd:cd06262  20 GEAILIDPGAGALEKILEAI----EELGLKIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADAE----LLED---- 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219848 124 skvSVEDMLFDEQDINKSMDKIEVIDFHQTVEVNGIKFWC-YTAGHVLGAAMFMVDIAGVriLYTGD 189
Cdd:cd06262  86 ---PELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEViHTPGHTPGSVCFYIEEEGV--LFTGD 147
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 19-214 3.56e-10

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 60.70  E-value: 3.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  19 GDQLIVTPLGAgsevgrSCVYMSFRGKNILFDCGIHPAYSGMAALPY-FDEIDPssIDVLLITHFHIDHA--ASLPYFLE 95
Cdd:COG2220   1 PGGMKITWLGH------ATFLIETGGKRILIDPVFSGRASPVNPLPLdPEDLPK--IDAVLVTHDHYDHLddATLRALKR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  96 KTTfngRVFMTHATKAIykllltdyvkvskvsvedmlFDEQDInksmDKIEVIDFHQTVEVNGIKFWCYTAGH------- 168
Cdd:COG2220  73 TGA---TVVAPLGVAAW--------------------LRAWGF----PRVTELDWGESVELGGLTVTAVPARHssgrpdr 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15219848 169 -VLGAAMFMVDIAGVRILYTGD--YSREEDRHLRaaelpQFSPDICIIE 214
Cdd:COG2220 126 nGGLWVGFVIETDGKTIYHAGDtgYFPEMKEIGE-----RFPIDVALLP 169
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-102 4.87e-10

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: 59.58  E-value: 4.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  27 LGAGSEVG-----RSCVYMSFRGKNILFDCGIhpaySGMAALPYFDeIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNG 101
Cdd:cd07740   3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGA----SSLIALKRAG-IDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVA 77


                .
gi 15219848 102 R 102
Cdd:cd07740  78 K 78
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 43-201 1.97e-08

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: 55.63  E-value: 1.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  43 RGKNILFDCGIHPAYSGMAA--LPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFnGRVFM---THATKAIYKLLl 117
Cdd:COG2333  20 DGKTILIDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFPV-GRVLVsgpPDTSETYERLL- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 118 tdyvkvskvsvedmlfdeQDINKSMDKIEVIDFHQTVEVNGIKFwcytagHVLGAAM--------------FMVDIAGVR 183
Cdd:COG2333  98 ------------------EALKEKGIPVRPCRAGDTWQLGGVRF------EVLWPPEdllegsdennnslvLRLTYGGFS 153

                       170
                ....*....|....*...
gi 15219848 184 ILYTGDYSREEDRHLRAA 201
Cdd:COG2333 154 FLLTGDAEAEAEAALLAR 171
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 44-189 2.81e-08

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: 54.70  E-value: 2.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  44 GKNILFDCGIHPAySGMAALPYFDEIDpSSIDVLLITHFHIDHAASLPYFLEKttFNGRVFMTHATKAIYKLLLTDYVKV 123
Cdd:COG0491  24 DGAVLIDTGLGPA-DAEALLAALAALG-LDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEAEALEAPAAGALFG 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219848 124 SKVSVEDMLFDEQDinksmdkievidfhqTVEVNGIKFWC-YTAGHVLGAAMFMVDiaGVRILYTGD 189
Cdd:COG0491 100 REPVPPDRTLEDGD---------------TLELGGPGLEViHTPGHTPGHVSFYVP--DEKVLFTGD 149
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 25-190 8.28e-08

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: 53.95  E-value: 8.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  25 TPLGAGSEVGRSCVYMSFRGKNILFDCGIHPAYSGM----AALPYFDEIDPSSIDV--LLITHFHIDHAASLPYFLEKtt 98
Cdd:cd07714   1 IPLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDMpgvdYIIPDFSYLEENKDKIkgIFITHGHEDHIGALPYLLPE-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  99 FNGRVFMTHATKAIYKLLLTDYVKVSKVsvedmlfdeqdinksmdKIEVIDFHQTVEVNGIKFWCYTAGH-VLGAAMFMV 177
Cdd:cd07714  79 LNVPIYATPLTLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHsIPDSVGLAI 141

                       170
                ....*....|...
gi 15219848 178 DIAGVRILYTGDY 190
Cdd:cd07714 142 KTPEGTIVHTGDF 154
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 37-97 1.77e-07

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: 53.01  E-value: 1.77e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219848  37 CVYMSFRGKNILFDCGihpaYSG-----MAALpyfdEIDPSSIDVLLITHFHIDHAASLPYFLEKT 97
Cdd:cd07713  22 SLLIETEGKKILFDTG----QSGvllhnAKKL----GIDLSDIDAVVLSHGHYDHTGGLKALLELN 79
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 37-118 5.07e-07

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: 50.21  E-value: 5.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  37 CVYMSFRGKNILFDCGIHPAYSGMAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEKttFN-GRVFM---THATKAI 112
Cdd:cd07731  12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN--FPvKEVYMpgvTHTTKTY 89


                ....*.
gi 15219848 113 YKLLLT 118
Cdd:cd07731  90 EDLLDA 95
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 44-189 1.04e-06

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: 49.82  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  44 GKNILFDCGiHPAYSGMAALpyfdEIDPSSIDVLLITHFHIDHAASLPYFLeKTT-FNGR-----VF-------MTHATK 110
Cdd:cd07719  27 GRVYLVDAG-SGVVRRLAQA----GLPLGDLDAVFLTHLHSDHVADLPALL-LTAwLAGRktplpVYgppgtraLVDGLL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 111 AIYKLlltDYVKVSKVSVEDMLFDEqdinksmDKIEVIDFHQTV---EVNGIKFWCYTAGH--VLGAAMFMVDIAGVRIL 185
Cdd:cd07719 101 AAYAL---DIDYRARIGDEGRPDPG-------ALVEVHEIAAGGvvyEDDGVKVTAFLVDHgpVPPALAYRFDTPGRSVV 170


                ....
gi 15219848 186 YTGD 189
Cdd:cd07719 171 FSGD 174
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 44-93 2.36e-06

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: 49.14  E-value: 2.36e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219848  44 GKNILFDCGIHPAYSGMAALPYFDE------------------IDPSSIDVLLITHFHIDHAASLPYF 93
Cdd:cd07729  41 EGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGLDLF 108
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 24-102 2.48e-06

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: 49.37  E-value: 2.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  24 VTPLGAGSEV---GR--SCVYMSFRGKNILFDCGihpaysgmaalpyfdE----------IDPSSIDVLLITHFHIDHAA 88
Cdd:cd07717   1 LTFLGTGSAVptpERnlSSIALRLEGELWLFDCG---------------EgtqrqllragLSPSKIDRIFITHLHGDHIL 65

                        90
                ....*....|....
gi 15219848  89 SLPYFLEKTTFNGR 102
Cdd:cd07717  66 GLPGLLSTMSLLGR 79
PRK00055 PRK00055
ribonuclease Z; Reviewed
 24-261 2.65e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 49.41  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   24 VTPLGAGSEV---GR--SCVYMSFRGKNILFDCGihpaySG----MAALPyfdeIDPSSIDVLLITHFHIDHAASLPYFL 94
Cdd:PRK00055   4 LTFLGTGSGVptpTRnvSSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   95 EKTTFNGRvfmTHATKAIYKLLLTDYVKVSKVSVEDM--LFDEQDIN--------KSMDKIEVIDFHQ-----TVEVNGi 159
Cdd:PRK00055  75 STRSLSGR---TEPLTIYGPKGIKEFVETLLRASGSLgyRIAEKDKPgkldaeklKALGVPPGPLFGKlkrgeDVTLED- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  160 kfwcytaGHVLGAAMFM-VDIAGVRILYTGD--YSREEDRHLRAAelpqfspDICIIESTSGvqlHQSRHIREKRFtdvi 236
Cdd:PRK00055 151 -------GRIINPADVLgPPRKGRKVAYCGDtrPCEALVELAKGA-------DLLVHEATFG---DEDEELAKEYG---- 209

                        250       260
                 ....*....|....*....|....*.
gi 15219848  237 HSTVAQGGRVlipafAL-GRAQELLL 261
Cdd:PRK00055 210 HSTARQAAEI-----AKeAGVKRLIL 230
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 43-114 7.15e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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 annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 48.03  E-value: 7.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  43 RGKNILFDCGIHPAYS--------GMAALPYFDE-------------IDPSSIDVLLITHFHIDHAASLPYFlekttFNG 101
Cdd:cd07730  32 TGGKILFDLGYRKDFEeytprvpeRLYRTPVPLEveedvaeqlaaggIDPEDIDAVILSHLHWDHIGGLSDF-----PNA 106

                        90
                ....*....|...
gi 15219848 102 RVFMTHATKAIYK 114
Cdd:cd07730 107 RLIVGPGAKEALR 119
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 44-105 1.67e-05

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 46.14  E-value: 1.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219848  44 GKNILFDCGIHPAYSGMAALPYFDE--IDPSSIDVLLITHFHIDHAASLPYFLEKttFNGRVFM 105
Cdd:cd07725  24 DETTLIDTGLATEEDAEALWEGLKElgLKPSDIDRVLLTHHHPDHIGLAGKLQEK--SGATVYI 85
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 46-262 1.81e-05

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: 46.15  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848    46 NILFDCGihPAYSG-MAALPYFDEIDPSSIDVLLITHFHIDHAASLPYFLEkttfnGRVFMTHATKAIYKLLltdyvkvS 124
Cdd:pfam12706   2 RILIDPG--PDLRQqALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLRE-----GRPRPLYAPLGVLAHL-------R 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848   125 KVSVEDMLFDEQDINksmdkIEVIDFHQTVEVN--GIKFWCYTAGH------------VLGaamFMVDIAGVRILYTGD- 189
Cdd:pfam12706  68 RNFPYLFLLEHYGVR-----VHEIDWGESFTVGdgGLTVTATPARHgsprgldpnpgdTLG---FRIEGPGKRVYYAGDt 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219848   190 --YSREEDRHLRAAelpqfspDICIIESTSgvqlhqsrhIREKRFTDVIHSTVAQGGRvlipAFALGRAQELLLI 262
Cdd:pfam12706 140 gyFPDEIGERLGGA-------DLLLLDGGA---------WRDDEMIHMGHMTPEEAVE----AAADLGARRKVLI 194
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 44-212 5.93e-05

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. 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. 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 44.79  E-value: 5.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  44 GKNILFDCGIHPAY----SGMAALpyfdEIDPSSIDVLLITHFHIDHAASLPYFLEKTTfNGRVFmTH------------ 107
Cdd:cd07726  25 GRPALIDTGPSSSVprllAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEALP-NAKVY-VHprgarhlidpsk 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848 108 ---ATKAIYKLLLtdyvkvskvsvEDMLFDEQDINKsmDKIEVIDFHQTVEVNG--IKFWcYTAGHVLGAAMFMVDIAGV 182
Cdd:cd07726  99 lwaSARAVYGDEA-----------DRLGGEILPVPE--ERVIVLEDGETLDLGGrtLEVI-DTPGHAPHHLSFLDEESDG 164

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15219848 183 riLYTGD----YSREEDRHLRA-AELPQFSPDICI 212
Cdd:cd07726 165 --LFTGDaagvRYPELDVVGPPsTPPPDFDPEAWL 197
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 25-90 6.87e-05

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. 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. 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 43.41  E-value: 6.87e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219848  25 TPLGAGSEvGrSCVYMSFRGKNILFDCGIhpaySGMAALPYFDEI--DPSSIDVLLITHFHIDHAASL 90
Cdd:cd07733   1 SVLASGSK-G-NCTYLETEDGKLLIDAGL----SGRKITGRLAEIgrDPEDIDAILVTHEHADHIKGL 62
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 44-87 1.57e-04

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 44.08  E-value: 1.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15219848  44 GKNILFDCG---IHPAYSG-----MAALpyfdEIDPSSIDVLLITHFHIDHA 87
Cdd:cd07720  58 GRLILVDTGaggLFGPTAGkllanLAAA----GIDPEDIDDVLLTHLHPDHI 105
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 36-93 8.04e-04

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 41.33  E-value: 8.04e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219848  36 SCVYMSFRGKNILFDCGihpaySGMAALPyfDEIDPSSIDV---LLITHFHIDHAASLPYF 93
Cdd:cd07715  24 SCVEVRAGGELLILDAG-----TGIRELG--NELMKEGPPGeahLLLSHTHWDHIQGFPFF 77
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-86 8.66e-04

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) 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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 41.35  E-value: 8.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15219848  44 GKNILFDCGI-------HPAYSGMAALPYFDE-----IDPSSIDVLLITHFHIDH 86
Cdd:cd16277  22 GRTILVDTGIgndkprpGPPAFHNLNTPYLERlaaagVRPEDVDYVLCTHLHVDH 76
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 43-197 9.85e-04

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: 40.74  E-value: 9.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  43 RGKNILFDCgihPAYSGMAALPYfdEIDPSSIDVLLITHFHIDHAASlpyFLEKTTFNGRVFMtHATKAIYKLLLTDYVK 122
Cdd:cd07738  23 NGRGIMVDP---PVNSTSYLRQN--GISPRLVDHVILTHCHADHDAG---TFQKILEEEKITL-YTTRTINESFLRKYAA 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219848 123 VSKvsvedmlFDEQDINKSMDKIEVIDFHQTvEVNGIKFWCYTAGHVLGAAMFMVDIAGVRILYTGDYSREEDRH 197
Cdd:cd07738  94 LTG-------LPPDFLEELFDFRPVIIGEKT-KINGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTRYDPDGL 160
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 78-190 1.70e-03

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. 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: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 39.81  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  78 LITHFHIDHAASLpyflekttfngrvfMTHATKAIYKLLLTDYVKVSKVSVEdmlfdEQDINK-SMDKiEVIdfhqtveV 156
Cdd:cd16298  41 FLTHFHSDHYCGL--------------TKKFKFPIYCSKITGNLVKSKLKVE-----EQYINVlPMNT-ECI-------V 93

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15219848 157 NGIKFWCYTAGHVLGAAM-FMVDIAGVRILYTGDY 190
Cdd:cd16298  94 NGVKVVLLDANHCPGAVMiLFRLPSGTLVLHTGDF 128
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 47-97 1.85e-03

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. 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. 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: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 40.28  E-value: 1.85e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15219848  47 ILFDCGihpaYSGMAA--LPYFDEI--DPSSIDVLLITHFHIDHAASLPYFLEKT 97
Cdd:cd07721  23 TLIDTG----LPGSAKriLKALRELglSPKDIRRILLTHGHIDHIGSLAALKEAP 73
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 37-90 2.33e-03

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 39.53  E-value: 2.33e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15219848  37 CVYMSFRGKNILFDCGIHPAYsgmaalpyfDEIDPSSIDVLLITHFHIDHAASL 90
Cdd:cd07736  39 SALIEVDGERILLDAGLTDLA---------ERFPPGSIDAILLTHFHMDHVQGL 83
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 43-123 3.99e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 39.11  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219848  43 RGKNILFDCGIHPAY----SGMAALpyfdEIDPSSIDVLLITHFHIDHAASLPYFLEKTTFNGRV-----FMTHATKAIY 113
Cdd:cd07711  30 GGKNILVDTGTPWDRdlllKALAEH----GLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDicgdsYDDHSLEEGD 105

                        90
                ....*....|
gi 15219848 114 KLLLTDYVKV 123
Cdd:cd07711 106 GYEIDENVEV 115
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 44-97 4.26e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 39.39  E-value: 4.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219848  44 GKNILFDCGIHPaysgmaalpYFDE--------IDPSSIDVLLITHFHIDHAASLPYFLEKT 97
Cdd:cd07709  40 EKTALIDTVKEP---------FFDEflenleevIDPRKIDYIVVNHQEPDHSGSLPELLELA 92
NorV COG0426
Flavorubredoxin [Energy production and conversion];
44-98 8.23e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.04  E-value: 8.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15219848  44 GKNILFDCGIHPAYSgmaalPYFDE----IDPSSIDVLLITHFHIDHAASLPYFLEKTT 98
Cdd:COG0426  42 EKTALIDTVGESFFE-----EFLENlskvIDPKKIDYIIVNHQEPDHSGSLPELLELAP 95
PRK02126 PRK02126
ribonuclease Z; Provisional
 37-86 8.73e-03

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 38.74  E-value: 8.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15219848   37 CVYMSFR--GKNILFDCGihpaysGMAALPyFDEIdpSSIDVLLITHFHIDH 86
Cdd:PRK02126  18 GLYVDFLfeRRALLFDLG------DLHHLP-PREL--LRISHIFVSHTHMDH 60
 
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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