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Conserved domains on  [gi|2217328862|ref|XP_047300701|]
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cleavage and polyadenylation specificity factor subunit 3 isoform X1 [Homo sapiens]

Protein Classification

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; ...
 8-195 3.04e-144

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: 417.76  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 87
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 167
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 2217328862 168 GDFSRQEDRHLMAAEIPNIKPDILIIES 195
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-411 1.25e-120

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 365.28  E-value: 1.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQPCsGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFK 80
Cdd:COG1236     1 MKLTFL-GAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  81 GRTFMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEI 159
Cdd:COG1236    77 GPIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 160 AGVKLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQEL 239
Cdd:COG1236   157 GGKRIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQEL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 240 LLILDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVM 316
Cdd:COG1236   236 LYLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIII 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 317 ASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEF 395
Cdd:COG1236   308 APSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEW 386

                         410
                  ....*....|....*..
gi 2217328862 396 IRALKPP-HVILVHGEQ 411
Cdd:COG1236   387 IKATGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 469-672 1.94e-89

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: 277.08  E-value: 1.94e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 469 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 547
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 548 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 623
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217328862 624 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 672
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 8-195 3.04e-144

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: 417.76  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 87
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 167
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 2217328862 168 GDFSRQEDRHLMAAEIPNIKPDILIIES 195
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-411 1.25e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 365.28  E-value: 1.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQPCsGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFK 80
Cdd:COG1236     1 MKLTFL-GAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  81 GRTFMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEI 159
Cdd:COG1236    77 GPIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 160 AGVKLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQEL 239
Cdd:COG1236   157 GGKRIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQEL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 240 LLILDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVM 316
Cdd:COG1236   236 LYLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIII 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 317 ASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEF 395
Cdd:COG1236   308 APSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEW 386

                         410
                  ....*....|....*..
gi 2217328862 396 IRALKPP-HVILVHGEQ 411
Cdd:COG1236   387 IKATGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 469-672 1.94e-89

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: 277.08  E-value: 1.94e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 469 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 547
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 548 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 623
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217328862 624 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 672
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 467-673 1.75e-63

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: 209.58  E-value: 1.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  467 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 540
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  541 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 617
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328862  618 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 673
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 236-357 8.06e-46

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: 158.86  E-value: 8.06e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  236 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 310
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217328862  311 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 357
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 ...
 236-355 1.08e-35

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: 129.94  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 236 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 315
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217328862 316 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 355
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-208 6.40e-20

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 89.48  E-value: 6.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQP--CSGAGQEVGR--SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQ 75
Cdd:COG1234     1 MKLTFlgTGGAVPTPGRatSSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  76 KTSFKGRT-----FMTHATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYH 145
Cdd:COG1234    75 TRSLAGREkpltiYGPPGTKEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFP 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328862 146 AGHVLGAAMFMIEIAGVKLLYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 208
Cdd:COG1234   135 LDHPVPAYGYRFEEPGRSLVYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 16-185 3.52e-16

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: 76.82  E-value: 3.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   16 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 95
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   96 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 174
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 2217328862  175 DRHLMAAEIPN 185
Cdd:smart00849 142 GDGRTLVDGGD 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
16-185 4.22e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 95
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  96 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 175
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 2217328862 176 RHLMAAEIPN 185
Cdd:pfam00753 156 IGRLDLPLGG 165
PRK00055 PRK00055
ribonuclease Z; Reviewed
 16-83 1.08e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  16 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 83
Cdd:PRK00055   21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 16-83 5.13e-06

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 48.75  E-value: 5.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  16 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 83
Cdd:TIGR02651  19 PSIALKLNGELWLFDCG-----EGtqrqMLRSG----ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 8-195 3.04e-144

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: 417.76  E-value: 3.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 87
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 167
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 2217328862 168 GDFSRQEDRHLMAAEIPNIKPDILIIES 195
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-411 1.25e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 365.28  E-value: 1.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQPCsGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFK 80
Cdd:COG1236     1 MKLTFL-GAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  81 GRTFMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEI 159
Cdd:COG1236    77 GPIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 160 AGVKLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQEL 239
Cdd:COG1236   157 GGKRIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQEL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 240 LLILDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVM 316
Cdd:COG1236   236 LYLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIII 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 317 ASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEF 395
Cdd:COG1236   308 APSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEW 386

                         410
                  ....*....|....*..
gi 2217328862 396 IRALKPP-HVILVHGEQ 411
Cdd:COG1236   387 IKATGKPeRVFLVHGEP 403
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-446 2.61e-120

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: 366.38  E-value: 2.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQpCSGAGQEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQ 75
Cdd:COG1782     1 MRIT-FLGAAREVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  76 KTSFKGRTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKF 141
Cdd:COG1782    75 KYGYRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 142 WCYHAGHVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVH 217
Cdd:COG1782   155 TFYNAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVIN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 218 DIVNRGGRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFK 296
Cdd:COG1782   232 ETIERGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 297 HISNLKSMDHFDDI----GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKL 372
Cdd:COG1782   311 NLHYVESVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETI 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217328862 373 PLKMSVDYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 446
Cdd:COG1782   390 PVRAEVETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 8-195 3.24e-91

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: 281.53  E-value: 3.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 87
Cdd:cd07734     4 GGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 ATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAGVKLL 165
Cdd:cd07734    84 PTVALGRLLLEDYVKSAERIGQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGEKLV 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217328862 166 YTGDFSRQEDRHLMAAEIPNIKPDILIIES 195
Cdd:cd07734   164 YTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 469-672 1.94e-89

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: 277.08  E-value: 1.94e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 469 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 547
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 548 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 623
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217328862 624 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 672
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 8-195 2.67e-68

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: 221.75  E-value: 2.67e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAE-----IDLLLISHFHLDHCGALPWFLQKTSFKGR 82
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGpftehIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  83 TFMTHATKAIYRWLLSDYVKVS-NISADDMLYTETDLEESMDKIETINFHEVKEV-AGIKFWCYHAGHVLGAAMFMIEIA 160
Cdd:cd16291    85 IYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFYVRVG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217328862 161 GVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 195
Cdd:cd16291   165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 467-673 1.75e-63

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: 209.58  E-value: 1.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  467 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 540
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  541 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 617
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328862  618 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 673
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 8-195 3.44e-61

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 202.69  E-value: 3.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL-IDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGRTFMT 86
Cdd:cd16295     5 GAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGPIYAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  87 HATKAIYRWLLSDYVKVSNISADDM----LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEI-A 160
Cdd:cd16295    84 PATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVELEIgG 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217328862 161 GVKLLYTGDFSRQEDRhLMAAEIPNIKPDILIIES 195
Cdd:cd16295   164 GKRILFSGDLGRKNTP-LLRDPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 236-357 8.06e-46

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: 158.86  E-value: 8.06e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  236 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 310
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217328862  311 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 357
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 ...
 236-355 1.08e-35

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: 129.94  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 236 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 315
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217328862 316 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 355
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 3-195 4.10e-20

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: 88.73  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   3 LQPCSGAGQEvGRSCIILEFKGRKIMLDCG--IHPGLEGMDALPYIdlidPAEIDLLLISHFHLDHCGALPWFLQKTSFK 80
Cdd:cd16293     1 FTPLSGAGDE-SPLCYLLEIDDVTILLDCGwdESFDMEYLESLKRI----APTIDAVLLSHPDLEHLGALPYLVGKLGLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  81 GRTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVA----GIKFWCYHAGHVLGAAMFM 156
Cdd:cd16293    76 CPVYATLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217328862 157 IEIAGVKLLYTGDFSRQEDRHLMAAEIPNI---KPDILIIES 195
Cdd:cd16293   156 ITKDSEDIVYAVDWNHKKERHLNGAVLDSFgglRPSLLITDA 197
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-208 6.40e-20

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 89.48  E-value: 6.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQP--CSGAGQEVGR--SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQ 75
Cdd:COG1234     1 MKLTFlgTGGAVPTPGRatSSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  76 KTSFKGRT-----FMTHATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYH 145
Cdd:COG1234    75 TRSLAGREkpltiYGPPGTKEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFP 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328862 146 AGHVLGAAMFMIEIAGVKLLYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 208
Cdd:COG1234   135 LDHPVPAYGYRFEEPGRSLVYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 16-185 3.52e-16

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: 76.82  E-value: 3.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   16 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 95
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   96 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 174
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 2217328862  175 DRHLMAAEIPN 185
Cdd:smart00849 142 GDGRTLVDGGD 152
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-194 1.19e-15

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: 76.11  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  12 EVGRSCIILEFKGRKIMLDCG-----------------IHPGLEGMDALPYIDLI-------DPAEIDLLLISHFHLDHC 67
Cdd:cd07732    10 EIGGNCIEVETGGTRILLDFGlpldpeskyfdevldflELGLLPDIVGLYRDPLLlgglrseEDPSVDAVLLSHAHLDHY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  68 GALPWFLQKTSFkgrtFMTHATKAIYRWLLSDYVKVSNISADdmlytetdleesmdkIETINFHEVKEVAGIKFWCYHAG 147
Cdd:cd07732    90 GLLNYLRPDIPV----YMGEATKRILKALLPFFGEGDPVPRN---------------IRVFESGKSFTIGDFTVTPYLVD 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217328862 148 H-VLGAAMFMIEIAGVKLLYTGDF----SRQEDRHLMAAEIPNiKPDILIIE 194
Cdd:cd07732   151 HsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELTEAFVEKAPK-NIDVLLME 201
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 16-195 2.48e-15

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: 74.61  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHA 88
Cdd:cd16272    18 SSYLLETGGTRILLDCGegTVYRLLKAG-------VDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKkpltiYGPKG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  89 TKAIYRWLLSDYVKVSnisaddmlytetDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTG 168
Cdd:cd16272    91 IKEFLEKLLNFPVEIL------------PLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSG 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2217328862 169 DfsrqedrhlmAAEIPNIKP-----DILIIES 195
Cdd:cd16272   159 D----------TGPCENLVElakgaDLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
16-185 4.22e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 95
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  96 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 175
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 2217328862 176 RHLMAAEIPN 185
Cdd:pfam00753 156 IGRLDLPLGG 165
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 19-192 1.60e-13

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 69.55  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  19 ILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPaEIDLLLISHFHLDHCGALPWFLQKtsfKGRTFMTH----ATKAIY- 93
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYLEKILP-EVDLILLSHPTLEHLGAYPLLYYK---FGSHLGSNipvyATLPVAn 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  94 --RWLLSDYVKVSNISA--DDMLYTETDLEESMDKIETINFHEVKEV----AGIKFWCYHAGHVLGAAMFMIEIAGVKLL 165
Cdd:pfam16661  77 lgRVSTYDLYASRGILGpyDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIV 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217328862 166 YTGDFSRQEDRHLMAAEIPN---------IKPDILI 192
Cdd:pfam16661 157 YAVDWNHTKDSHLNGASLLDstgkpleslVRPTALI 192
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 1-158 1.27e-12

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: 66.36  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   1 MRLQPCSGagqEVGRSCIILEFKGRKIMLDCGIhpglegmDALPYIDLIDPAEIDLLLISHFHldHCGALPWFLQKTSFK 80
Cdd:cd16294     1 MKLYCLSG---HPTLPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFT 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328862  81 GRTFMTHATKAIYRWLLSDYVkvsnisaddmlytetdleESMDKIETINFHEVKEVAG-IKFWCYHAGHVLGAAMFMIE 158
Cdd:cd16294    69 GVVYATEPTVQIGRLLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQ 129
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 8-207 6.95e-12

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: 65.89  E-value: 6.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   8 GAGqEVGRSCIILEFKGRKIMLDCGIHPGLEGMdalPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK-- 76
Cdd:cd07714     5 GLG-EIGKNMYVVEYDDDIIIIDCGLKFPDEDM---PGVDYIIPdfsyleenkDKIKGIFITHGHEDHIGALPYLLPEln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  77 -----TSFkgrtfmthaTKAIYRWLLSDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGH-VL 150
Cdd:cd07714    81 vpiyaTPL---------TLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHsIP 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217328862 151 GAAMFMIEIAGVKLLYTGDF--------SRQEDRHLMaAEIPNIKPDILIIESTYGTHiHEKREE 207
Cdd:cd07714   135 DSVGLAIKTPEGTIVHTGDFkfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 371-438 1.85e-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: 59.56  E-value: 1.85e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328862 371 KLPLKMSVDYIS-FSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNP 438
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL------GIEVFVP 63
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 6-197 3.23e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 61.06  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   6 CSGAGQEVGR--SCIILEFKGRKIMLDCGihPGL-EGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG- 81
Cdd:COG1235    24 CASTDPRYGRtrSSILVEADGTRLLIDAG--PDLrEQLLRLG----LDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPi 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  82 RTFMTHATKAiyrwllsdyvkvsniSADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCY---H-AGHVLGaamFMI 157
Cdd:COG1235    98 PVYATPGTLE---------------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFpvpHdAGDPVG---YRI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217328862 158 EIAGVKLLYTGDFSrqedrHLMAAEIPNIK-PDILIIESTY 197
Cdd:COG1235   160 EDGGKKLAYATDTG-----YIPEEVLELLRgADLLILDATY 195
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 17-170 3.60e-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: 59.61  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  17 CIILEFKGRK-IMLDcgihPGLEGMDALpyIDLID--PAEIDLLLISHFHLDHCGALPWFLQKTSFKgrtfmTHATKAIY 93
Cdd:cd06262    12 CYLVSDEEGEaILID----PGAGALEKI--LEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAP-----VYIHEADA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217328862  94 RWLLSDyvkvsnisADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGDF 170
Cdd:cd06262    81 ELLEDP--------ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEGV--LFTGDT 148
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 16-198 7.41e-10

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: 59.77  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMT 86
Cdd:cd07717    18 SSIALRLEGELWLFDCG-----EGtqrqLLRAG----LSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTepltiYGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  87 HATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVKEVAGIKF-------WCYHAGHVLGAAMFMIEI 159
Cdd:cd07717    89 KGLKEFLETLL-------RLSASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYRFEE 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217328862 160 aGVKLLYTGDfSRQEDRHLMAAEipniKPDILIIESTYG 198
Cdd:cd07717   149 -GRKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 6-169 4.26e-09

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 56.30  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   6 CSGAGQEVGR--SCIILEFKGRKIMLDCGihPGlegmdALPYI-DLIDPAEIDLLLISHFHLDHCGALPWFLqktsfkgr 82
Cdd:cd07716     7 CSGSYPGPGGacSGYLLEADGFRILLDCG--SG-----VLSRLqRYIDPEDLDAVVLSHLHPDHCADLGVLQ-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  83 tfmthatkaiYRWLLSDYVKVSNI-------SADDMLYTETDLEESMDkIETINFHEVKEVAGIKFWCYHAGHVLGAAMF 155
Cdd:cd07716    72 ----------YARRYHPRGARKPPlplygpaGPAERLAALYGLEDVFD-FHPIEPGEPLEIGPFTITFFRTVHPVPCYAM 140

                         170
                  ....*....|....
gi 2217328862 156 MIEIAGVKLLYTGD 169
Cdd:cd07716   141 RIEDGGKVLVYTGD 154
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 13-193 7.91e-09

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: 56.79  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  13 VGR-SCIILEFKGRKIML-DCGIHPGLEGMDA--LPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH- 87
Cdd:COG2333     8 VGQgDAILIRTPDGKTILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA--FPVGRVLVSg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 --ATKAIYRWLLsDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGHVLGAAM--------FMI 157
Cdd:COG2333    86 ppDTSETYERLL-EALKEKGI-----------------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSdennnslvLRL 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217328862 158 EIAGVKLLYTGDFSRQEDRHLMAAEiPNIKPDILII 193
Cdd:COG2333   148 TYGGFSFLLTGDAEAEAEAALLARG-PDLKADVLKV 182
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 13-207 1.31e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 55.69  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  13 VGRSCIILEFKGRKIMLDcgihPGLEGMDALPYIDLIDPAE---IDLLLISHFHLDHCGalpwflqktsfkgrtfmthat 89
Cdd:COG2220     9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLDPEDlpkIDAVLVTHDHYDHLD--------------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  90 KAIYRWLLSDYVKV-SNISADDMLytetdLEESMDKIETINFHEVKEVAGIKFWCYHAGH--------VLGAAMFMIEIA 160
Cdd:COG2220    64 DATLRALKRTGATVvAPLGVAAWL-----RAWGFPRVTELDWGESVELGGLTVTAVPARHssgrpdrnGGLWVGFVIETD 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217328862 161 GVKLLYTGD------FSRQEDRHlmaaeipniKPDILIIEsTYGTHIHEKREE 207
Cdd:COG2220   139 GKTIYHAGDtgyfpeMKEIGERF---------PIDVALLP-IGAYPFTMGPEE 181
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-74 4.01e-08

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: 53.80  E-value: 4.01e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217328862   8 GAGQEVG-----RSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFL 74
Cdd:cd07740     4 GSGDAFGsggrlNTCFHVASEAGRFLIDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 17-186 7.03e-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: 53.54  E-value: 7.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  17 CIILEFKGRKIMLDcgihPGLEGMDALPYIDLID--PAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHAT-KAIY 93
Cdd:COG0491    17 SYLIVGGDGAVLID----TGLGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEaEALE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  94 RWLLSDYVKVSNISADdmlytetdleesmdkiETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDfsr 172
Cdd:COG0491    91 APAAGALFGREPVPPD----------------RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD--- 149

                         170
                  ....*....|....
gi 2217328862 173 qedrHLMAAEIPNI 186
Cdd:COG0491   150 ----ALFSGGVGRP 159
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
8-76 9.78e-08

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 55.07  E-value: 9.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217328862   8 GAGqEVGRSCIILEFKGRKIMLDCGI-HPGlegmDALPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK 76
Cdd:COG0595    13 GLG-EIGKNMYVYEYDDDIIIVDCGLkFPE----DEMPGVDLVIPdisyleenkDKIKGIVLTHGHEDHIGALPYLLKE 86
PRK00055 PRK00055
ribonuclease Z; Reviewed
 16-83 1.08e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  16 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 83
Cdd:PRK00055   21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 17-78 2.01e-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: 2.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217328862  17 CIILEFKGRKIMLDCGIHPGLEG-MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTS 78
Cdd:cd07713    22 SLLIETEGKKILFDTGQSGVLLHnAKKLG----IDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
16-135 4.81e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIIlEFKGRKIMLDCGiHPG--LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKTsfKGRTFMTHatKAIY 93
Cdd:COG1237    24 SALI-ETEGKRILFDTG-QSDvlLKNAEKL----GIDLSDIDAVVLSHGHYDHTGGLPALLELN--PKAPVYAH--PDAF 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217328862  94 RWLLSDYVKVSNISaddMLYTETDLEESMDkietiNFHEVKE 135
Cdd:COG1237    94 EKRYSKRPGGKYIG---IPFSREELEKLGA-----RLILVKE 127
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 16-77 2.04e-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: 49.52  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL------------------IDPAEIDLLLISHFHLDHCGAL------P 71
Cdd:cd07729    33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGLdlfpnaT 112


                  ....*.
gi 2217328862  72 WFLQKT 77
Cdd:cd07729   113 IIVQRA 118
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 16-169 4.22e-06

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: 48.70  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLD--CGIHPG------LEGMDALPYidliDPAEIDLLLISHFHLDHCGALpwflqKTSFKGRTF--- 84
Cdd:cd07720    50 NAFLVRTGGRLILVDtgAGGLFGptagklLANLAAAGI----DPEDIDDVLLTHLHPDHIGGL-----VDAGGKPVFpna 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  85 MTHATKAIYRWLLSDyvkvsNISADDMLYTETDLEESMDKIET----INFHEVKEVA-GIKFWcYHAGHVLGAAMFMIEI 159
Cdd:cd07720   121 EVHVSEAEWDFWLDD-----ANAAKAPEGAKRFFDAARDRLRPyaaaGRFEDGDEVLpGITAV-PAPGHTPGHTGYRIES 194

                         170
                  ....*....|
gi 2217328862 160 AGVKLLYTGD 169
Cdd:cd07720   195 GGERLLIWGD 204
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 16-83 5.13e-06

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 48.75  E-value: 5.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  16 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 83
Cdd:TIGR02651  19 PSIALKLNGELWLFDCG-----EGtqrqMLRSG----ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 5-197 9.13e-05

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: 44.02  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862   5 PCSGAGQevGR-----SCIILEFKGRKIMLDCG--IHP-GLEGMDALPyidlidPAEIDLLLiSHFHLDH-CGaLPWF-- 73
Cdd:cd07715    10 PVPGPDT--VRyggntSCVEVRAGGELLILDAGtgIRElGNELMKEGP------PGEAHLLL-SHTHWDHiQG-FPFFap 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  74 LQKTSFKGRTFMTHATKAIYRWLLSDYVKVSN--ISADDMLytetdleesmdkiETINFHEVKE-----VAGIKFWCYHA 146
Cdd:cd07715    80 AYDPGNRIHIYGPHKDGGSLEEVLRRQMSPPYfpVPLEELL-------------AAIEFHDLEPgepfsIGGVTVTTIPL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328862 147 GHVLGAAMFMIEIAGVKLLYTGDFsrqEDRHLMAAEIPNIKP-----DILIIESTY 197
Cdd:cd07715   147 NHPGGALGYRIEEDGKSVVYATDT---EHYPDDGESDEALLEfargaDLLIHDAQY 199
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 16-169 9.78e-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: 44.02  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDCGIHPG----LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---- 87
Cdd:cd07726    17 ASYLLDGEGRPALIDTGPSSSvprlLAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEA--LPNAKVYVHprga 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  88 -----------ATKAIYRWLlsdyvkvsnisADDMLYTETDLEEsmDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMF 155
Cdd:cd07726    91 rhlidpsklwaSARAVYGDE-----------ADRLGGEILPVPE--ERVIVLEDGETLDLGGRTLEVIDTpGHAPHHLSF 157

                         170
                  ....*....|....
gi 2217328862 156 MIEIAGVklLYTGD 169
Cdd:cd07726   158 LDEESDG--LFTGD 169
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 17-193 1.18e-04

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: 43.28  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  17 CIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsfkgrtfmthatkaiyrwl 96
Cdd:cd07731    12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN-------------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  97 lsdyVKVSNISADDMLYTETDLEESMDKIET--INFHEVK-----EVAGIKFWCYHAGHVLGAAM------FMIEIAGVK 163
Cdd:cd07731    72 ----FPVKEVYMPGVTHTTKTYEDLLDAIKEkgIPVTPCKagdrwQLGGVSFEVLSPPKDDYDDLnnnscvLRLTYGGTS 147

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217328862 164 LLYTGDFSRQEDRHLMAAEiPNIKPDILII 193
Cdd:cd07731   148 FLLTGDAEKEAEEELLASG-PDLLADVLKV 176
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 16-71 1.27e-04

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 43.27  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217328862  16 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALP 71
Cdd:cd07719    19 PSTLVVVGGRVYLVDAG--SGvVRRLAQAG----LPLGDLDAVFLTHLHSDHVADLP 69
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-68 1.59e-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) 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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 43.33  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  18 IILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCG 68
Cdd:cd07741    23 IWIELNGKNIHIDPG--PGaLVRMCRPK----LDPTKLDAIILSHRHLDHSN 68
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-73 3.49e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 42.64  E-value: 3.49e-04
                          10        20
                  ....*....|....*....|....*
gi 2217328862  49 IDPAEIDLLLISHFHLDHCGALPWF 73
Cdd:cd07730    79 IDPEDIDAVILSHLHWDHIGGLSDF 103
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-68 6.14e-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: 41.74  E-value: 6.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217328862  19 ILEFKGRKIMLDCGI-----HPGLEGMDAL--PYID-L----IDPAEIDLLLISHFHLDHCG 68
Cdd:cd16277    17 LVRTPGRTILVDTGIgndkpRPGPPAFHNLntPYLErLaaagVRPEDVDYVLCTHLHVDHVG 78
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 25-71 8.43e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 40.98  E-value: 8.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217328862  25 RKIMLDCGihpglEGMDalPYIDLI-------DPAEIDLLLISHFHLDHCGALP 71
Cdd:cd07722    28 RRILIDTG-----EGRP--SYIPLLksvldseGNATISDILLTHWHHDHVGGLP 74
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 25-197 9.51e-04

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: 40.76  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  25 RKIMLDCGihPGLEGMDAL---PYIDLIDPaeIDLLLISHFHLDHCGALPwFLQktsfKGRTFMTHATKAIYRWLLSDYV 101
Cdd:pfam12706   1 RRILIDPG--PDLRQQALPalqPGRLRDDP--IDAVLLTHDHYDHLAGLL-DLR----EGRPRPLYAPLGVLAHLRRNFP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862 102 KVSNISADDMLYTETDLEESM---DKIETINFHEVKEVAGIKFWcYHAGHVLGaamFMIEIAGVKLLYTGD---FSRQED 175
Cdd:pfam12706  72 YLFLLEHYGVRVHEIDWGESFtvgDGGLTVTATPARHGSPRGLD-PNPGDTLG---FRIEGPGKRVYYAGDtgyFPDEIG 147

                         170       180
                  ....*....|....*....|..
gi 2217328862 176 RHLMAAeipnikpDILIIESTY 197
Cdd:pfam12706 148 ERLGGA-------DLLLLDGGA 162
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 16-177 1.19e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293824  Cd Length: 189  Bit Score: 40.36  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  16 SCIILEFKGRKIMLDcgihPGLEGMDALPYIDlIDPAEIDLLLISHFHLDHCGAlpwFLQKTSFKGRTFMtHATKAIYRW 95
Cdd:cd07738    16 SGFIIWINGRGIMVD----PPVNSTSYLRQNG-ISPRLVDHVILTHCHADHDAG---TFQKILEEEKITL-YTTRTINES 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  96 LLSDYVKVSNISADdmlytetDLEESMDKIETINFHEVKeVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 175
Cdd:cd07738    87 FLRKYAALTGLPPD-------FLEELFDFRPVIIGEKTK-INGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTRYDPD 158


                  ..
gi 2217328862 176 RH 177
Cdd:cd07738   159 GL 160
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-169 3.90e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 293839  Cd Length: 252  Bit Score: 39.40  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  17 CIILEFKGRKIMLDCGI----------HPGLEG----MDALPYIDLiDPAEIDLLLISHFHLDHC-GALPWF---LQKTS 78
Cdd:cd16281    45 CLLIETGGRNILIDTGIgdkqdpkfrsIYVQHSehslLKSLARLGL-SPEDITDVILTHLHFDHCgGATRADddgLVELL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  79 FKGRTFMTHatKAIYRWLLSDYV--KVSNISADDMLytetdLEESmDKIETINFHEVKEVAGIKFWCYHaGHVLGAAMFM 156
Cdd:cd16281   124 FPNATYWVQ--KRHWEWALNPNPreRASFLPENIEP-----LEES-GRLKLIDGSDAELGPGIRFHLSD-GHTPGQMLPE 194

                         170
                  ....*....|...
gi 2217328862 157 IEIAGVKLLYTGD 169
Cdd:cd16281   195 ISTPGGTVVFAAD 207
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 48-73 4.92e-03

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 38.43  E-value: 4.92e-03
                          10        20
                  ....*....|....*....|....*.
gi 2217328862  48 LIDPAEIDLLLISHFHLDHCGALPWF 73
Cdd:cd07725    50 GLKPSDIDRVLLTHHHPDHIGLAGKL 75
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 17-77 6.03e-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: 38.74  E-value: 6.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217328862  17 CIILEFKGRKIMLDCGIhPG-----LEGMDALPYidliDPAEIDLLLISHFHLDHCGALPWFLQKT 77
Cdd:cd07721    13 AYLIEDDDGLTLIDTGL-PGsakriLKALRELGL----SPKDIRRILLTHGHIDHIGSLAALKEAP 73
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 18-169 6.20e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 38.78  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  18 IILEFKGRKIMLDCGIHPGL--------EGMDALPYI--DL----IDPAEIDLLLISHFHLDHCGALpwflqkTSFKGRT 83
Cdd:cd07728    46 ILIQYQGKNYLIDAGIGNGKltekqkrnFGVTEESSIeeSLaelgLTPEDIDYVLMTHLHFDHASGL------TKVKGEQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328862  84 FM------THATKAIyRWllsDYVKVSNISAddmlyTETDLEESMDKIE--TINF-HEVKEVAGIKFWcyH-AGHVLGAA 153
Cdd:cd07728   120 LVsvfpnaTIYVSEI-EW---EEMRNPNIRS-----KNTYWKENWEPIEdqVKTFsDEIEIVPGITMI--HtGGHSDGHS 188

                         170
                  ....*....|....*.
gi 2217328862 154 MFMIEIAGVKLLYTGD 169
Cdd:cd07728   189 IIEIEQGGETAIHMAD 204
 
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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