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Conserved domains on  [gi|7706427|ref|NP_057291|]
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cleavage and polyadenylation specificity factor subunit 3 isoform a [Homo sapiens]

Protein Classification

CPSF3-like_MBL-fold and YSH1 domain-containing protein( domain architecture ID 11611285)

protein containing domains CPSF3-like_MBL-fold, YSH1, and CPSF73-100_C

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; ...
 12-205 7.46e-148

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: 427.39  E-value: 7.46e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 7706427  172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 5.87e-121

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.43  E-value: 5.87e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  330 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|....
gi 7706427  409 LKPP-HVILVHGEQ 421
Cdd:COG1236 390 TGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 3.83e-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: 276.69  E-value: 3.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 7706427    634 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 682
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; ...
 12-205 7.46e-148

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: 427.39  E-value: 7.46e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 7706427  172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 5.87e-121

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.43  E-value: 5.87e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  330 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|....
gi 7706427  409 LKPP-HVILVHGEQ 421
Cdd:COG1236 390 TGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 3.83e-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: 276.69  E-value: 3.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 7706427    634 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 682
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 ...
 477-683 3.35e-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: 208.81  E-value: 3.35e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     477 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 550
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     551 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 627
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7706427     628 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 683
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 ...
 246-367 1.06e-45

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: 158.47  E-value: 1.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 320
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 7706427     321 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 367
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 ...
 246-365 1.38e-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: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 325
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 7706427    326 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 365
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
26-218 3.24e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.56  E-value: 3.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 99
Cdd:COG1234  20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  100 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 174
Cdd:COG1234  94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 7706427  175 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 218
Cdd:COG1234 154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-195 3.99e-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: 3.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427      26 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     106 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 184
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 7706427     185 DRHLMAAEIPN 195
Cdd:smart00849 142 GDGRTLVDGGD 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-195 4.86e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 105
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    106 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 7706427    186 RHLMAAEIPN 195
Cdd:pfam00753 156 IGRLDLPLGG 165
PRK00055 PRK00055
ribonuclease Z; Reviewed
 26-93 1.23e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706427    26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
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 ...
 26-93 5.82e-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: 5.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7706427     26 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
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; ...
 12-205 7.46e-148

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: 427.39  E-value: 7.46e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 7706427  172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 5.87e-121

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.43  E-value: 5.87e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236   3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236  80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236 160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236 239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  330 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236 311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                       410
                ....*....|....
gi 7706427  409 LKPP-HVILVHGEQ 421
Cdd:COG1236 390 TGKPeRVFLVHGEP 403
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 17-456 3.19e-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: 366.76  E-value: 3.19e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   17 LGAGQEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTSFKG 91
Cdd:COG1782   6 LGAAREVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYGYRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   92 RTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAG 157
Cdd:COG1782  81 PIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFYNAG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  158 HVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIVNRG 233
Cdd:COG1782 161 HILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  234 GRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHISNLK 312
Cdd:COG1782 238 GKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHYVE 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  313 SMDHFDDI----GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSV 388
Cdd:COG1782 317 SVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRAEV 395

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706427  389 DYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 456
Cdd:COG1782 396 ETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 15-205 1.12e-92

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: 285.38  E-value: 1.12e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   15 RPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTF 94
Cdd:cd07734   1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   95 MTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:cd07734  81 ATHPTVALGRLLLEDYVKSAERIGQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGE 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 7706427  173 KLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd07734 161 KLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 3.83e-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: 276.69  E-value: 3.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 7706427    634 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 682
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 14-205 1.59e-70

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: 227.91  E-value: 1.59e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAE-----IDLLLISHFHLDHCGALPWFLQKTS 88
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGpftehIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   89 FKGRTFMTHATKAIYRWLLSDYVKVS-NISADDMLYTETDLEESMDKIETINFHEVKEV-AGIKFWCYHAGHVLGAAMFM 166
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7706427  167 IEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 477-683 3.35e-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: 208.81  E-value: 3.35e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     477 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 550
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     551 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 627
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7706427     628 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 683
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 14-205 1.09e-62

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: 206.93  E-value: 1.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL-IDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGR 92
Cdd:cd16295   1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   93 TFMTHATKAIYRWLLSDYVKVSNISADDM----LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMI 167
Cdd:cd16295  80 IYATPATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVEL 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7706427  168 EI-AGVKLLYTGDFSRQEDRhLMAAEIPNIKPDILIIES 205
Cdd:cd16295 160 EIgGGKRILFSGDLGRKNTP-LLRDPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 246-367 1.06e-45

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: 158.47  E-value: 1.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 320
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 7706427     321 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 367
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 ...
 246-365 1.38e-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: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 325
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 7706427    326 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 365
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
26-218 3.24e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.56  E-value: 3.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 99
Cdd:COG1234  20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  100 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 174
Cdd:COG1234  94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 7706427  175 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 218
Cdd:COG1234 154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 16-205 9.34e-19

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: 84.88  E-value: 9.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   16 PLGAGQEVGRSCIILEFKGRKIMLDCG--IHPGLEGMDALPYIdlidPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:cd16293   3 PLSGAGDESPLCYLLEIDDVTILLDCGwdESFDMEYLESLKRI----APTIDAVLLSHPDLEHLGALPYLVGKLGLTCPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   94 FMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVA----GIKFWCYHAGHVLGAAMFMIEI 169
Cdd:cd16293  79 YATLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWKITK 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7706427  170 AGVKLLYTGDFSRQEDRHLMAAEIPNI---KPDILIIES 205
Cdd:cd16293 159 DSEDIVYAVDWNHKKERHLNGAVLDSFgglRPSLLITDA 197
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-195 3.99e-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: 3.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427      26 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     106 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 184
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 7706427     185 DRHLMAAEIPN 195
Cdd:smart00849 142 GDGRTLVDGGD 152
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-204 9.35e-16

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: 76.50  E-value: 9.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEVGRSCIILEFKGRKIMLDCG-----------------IHPGLEGMDALPYIDLI-------DPAEIDLLLI 69
Cdd:cd07732   2 ITIHRGTNEIGGNCIEVETGGTRILLDFGlpldpeskyfdevldflELGLLPDIVGLYRDPLLlgglrseEDPSVDAVLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   70 SHFHLDHCGALPWFLQKTSFkgrtFMTHATKAIYRWLLSDYVKVSNISADdmlytetdleesmdkIETINFHEVKEVAGI 149
Cdd:cd07732  82 SHAHLDHYGLLNYLRPDIPV----YMGEATKRILKALLPFFGEGDPVPRN---------------IRVFESGKSFTIGDF 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  150 KFWCYHAGH-VLGAAMFMIEIAGVKLLYTGDF----SRQEDRHLMAAEIPNiKPDILIIE 204
Cdd:cd07732 143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELTEAFVEKAPK-NIDVLLME 201
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-205 2.36e-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: 2.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   14 IRPLGAGQEV-----GRSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFLQK 86
Cdd:cd16272   1 LTFLGTGGAVpsltrNTSSYLLETGGTRILLDCGegTVYRLLKAG-------VDPDKLDAIFLSHFHLDHIGGLPTLLFA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   87 TSFKGRT-----FMTHATKAIYRWLLSDYVKVSnisaddmlytetDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLG 161
Cdd:cd16272  74 RRYGGRKkpltiYGPKGIKEFLEKLLNFPVEIL------------PLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVE 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7706427  162 AAMFMIEIAGVKLLYTGDfsrqedrhlmAAEIPNIKP-----DILIIES 205
Cdd:cd16272 142 SLGYRIEAEGKSIVYSGD----------TGPCENLVElakgaDLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-195 4.86e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 105
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    106 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 7706427    186 RHLMAAEIPN 195
Cdd:pfam00753 156 IGRLDLPLGG 165
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 29-202 1.95e-13

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 69.16  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     29 ILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPaEIDLLLISHFHLDHCGALPWFLQKtsfKGRTFMTH----ATKAIY- 103
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYLEKILP-EVDLILLSHPTLEHLGAYPLLYYK---FGSHLGSNipvyATLPVAn 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    104 --RWLLSDYVKVSNISA--DDMLYTETDLEESMDKIETINFHEVKEV----AGIKFWCYHAGHVLGAAMFMIEIAGVKLL 175
Cdd:pfam16661  77 lgRVSTYDLYASRGILGpyDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIV 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 7706427    176 YTGDFSRQEDRHLMAAEIPN---------IKPDILI 202
Cdd:pfam16661 157 YAVDWNHTKDSHLNGASLLDstgkpleslVRPTALI 192
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 16-217 1.35e-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: 68.20  E-value: 1.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   16 PLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMdalPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK 86
Cdd:cd07714   2 PLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDM---PGVDYIIPdfsyleenkDKIKGIFITHGHEDHIGALPYLLPE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   87 -------TSFkgrtfmthaTKAIYRWLLSDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGH- 158
Cdd:cd07714  79 lnvpiyaTPL---------TLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHs 132

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706427  159 VLGAAMFMIEIAGVKLLYTGDF--------SRQEDRHLMaAEIPNIKPDILIIESTYGTHiHEKREE 217
Cdd:cd07714 133 IPDSVGLAIKTPEGTIVHTGDFkfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 25-168 2.23e-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: 65.59  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   25 RSCIILEFKGRKIMLDCGIhpglegmDALPYIDLIDPAEIDLLLISHFHldHCGALPWFLQKTSFKGRTFMTHATKAIYR 104
Cdd:cd16294  12 LPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGR 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7706427  105 WLLSDYVkvsnisaddmlytetdleESMDKIETINFHEVKEVAG-IKFWCYHAGHVLGAAMFMIE 168
Cdd:cd16294  83 LLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQ 129
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 381-448 2.13e-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: 2.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7706427    381 KLPLKMSVDYIS-FSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNP 448
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL------GIEVFVP 63
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 27-180 3.96e-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: 3.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   27 CIILEFKGRK-IMLDcgihPGLEGMDALpyIDLID--PAEIDLLLISHFHLDHCGALPWFLQKTSFKgrtfmTHATKAIY 103
Cdd:cd06262  12 CYLVSDEEGEaILID----PGAGALEKI--LEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAP-----VYIHEADA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706427  104 RWLLSDyvkvsnisADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGDF 180
Cdd:cd06262  81 ELLEDP--------ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEGV--LFTGDT 148
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 4-207 4.34e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 60.68  E-value: 4.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    4 IPAEESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGihPGL-EGMDALPyidlIDPAEIDLLLISHFHLDHCGALPW 82
Cdd:COG1235  14 VPQIGCDCPVCASTDPRYGRTRSSILVEADGTRLLIDAG--PDLrEQLLRLG----LDPSKIDAILLTHEHADHIAGLDD 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   83 FLQKTSFKG-RTFMTHATKAiyrwllsdyvkvsniSADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCY---H-AG 157
Cdd:COG1235  88 LRPRYGPNPiPVYATPGTLE---------------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFpvpHdAG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7706427  158 HVLGaamFMIEIAGVKLLYTGDFSrqedrHLMAAEIPNIK-PDILIIESTY 207
Cdd:COG1235 153 DPVG---YRIEDGGKKLAYATDTG-----YIPEEVLELLRgADLLILDATY 195
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 26-208 8.13e-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: 8.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMT 96
Cdd:cd07717  18 SSIALRLEGELWLFDCG-----EGtqrqLLRAG----LSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTepltiYGP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   97 HATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVKEVAGIKF-------WCYHAGHVLGAAMFMIEI 169
Cdd:cd07717  89 KGLKEFLETLL-------RLSASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYRFEE 148

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7706427  170 aGVKLLYTGDfSRQEDRHLMAAEipniKPDILIIESTYG 208
Cdd:cd07717 149 -GRKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
10-86 6.85e-09

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 58.92  E-value: 6.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   10 DQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGI-HPGlegmDALPYIDLIDP---------AEIDLLLISHFHLDHCGA 79
Cdd:COG0595   4 DKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLkFPE----DEMPGVDLVIPdisyleenkDKIKGIVLTHGHEDHIGA 79


                ....*..
gi 7706427   80 LPWFLQK 86
Cdd:COG0595  80 LPYLLKE 86
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 23-203 8.84e-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: 8.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   23 VGR-SCIILEFKGRKIML-DCGIHPGLEGMDA--LPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH- 97
Cdd:COG2333   8 VGQgDAILIRTPDGKTILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA--FPVGRVLVSg 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   98 --ATKAIYRWLLsDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGHVLGAAM--------FMI 167
Cdd:COG2333  86 ppDTSETYERLL-EALKEKGI-----------------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSdennnslvLRL 147

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7706427  168 EIAGVKLLYTGDFSRQEDRHLMAAEiPNIKPDILII 203
Cdd:COG2333 148 TYGGFSFLLTGDAEAEAEAALLARG-PDLKADVLKV 182
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-84 1.06e-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: 55.73  E-value: 1.06e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7706427   17 LGAGQEVG-----RSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFL 84
Cdd:cd07740   3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 23-217 1.56e-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: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   23 VGRSCIILEFKGRKIMLDcgihPGLEGMDALPYIDLIDPAE---IDLLLISHFHLDHCGalpwflqktsfkgrtfmthat 99
Cdd:COG2220   9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLDPEDlpkIDAVLVTHDHYDHLD--------------------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  100 KAIYRWLLSDYVKV-SNISADDMLytetdLEESMDKIETINFHEVKEVAGIKFWCYHAGH--------VLGAAMFMIEIA 170
Cdd:COG2220  64 DATLRALKRTGATVvAPLGVAAWL-----RAWGFPRVTELDWGESVELGGLTVTAVPARHssgrpdrnGGLWVGFVIETD 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7706427  171 GVKLLYTGD------FSRQEDRHlmaaeipniKPDILIIEsTYGTHIHEKREE 217
Cdd:COG2220 139 GKTIYHAGDtgyfpeMKEIGERF---------PIDVALLP-IGAYPFTMGPEE 181
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 26-179 2.80e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 53.99  E-value: 2.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGihPGlegmdALPYI-DLIDPAEIDLLLISHFHLDHCGALPWFLqktsfkgrtfmthatkaiYR 104
Cdd:cd07716  19 SGYLLEADGFRILLDCG--SG-----VLSRLqRYIDPEDLDAVVLSHLHPDHCADLGVLQ------------------YA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  105 WLLSDYVKVSNI-------SADDMLYTETDLEESMDkIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 177
Cdd:cd07716  74 RRYHPRGARKPPlplygpaGPAERLAALYGLEDVFD-FHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYT 152


                ..
gi 7706427  178 GD 179
Cdd:cd07716 153 GD 154
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-179 8.47e-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: 53.16  E-value: 8.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   27 CIILEFKGRKIMLDcgihPGLEGMDALPYIDLID--PAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHAT-KAIY 103
Cdd:COG0491  17 SYLIVGGDGAVLID----TGLGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEaEALE 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706427  104 RWLLSDYVKVSNISADdmlytetdleesmdkiETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGD 179
Cdd:COG0491  91 APAAGALFGREPVPPD----------------RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD 149
PRK00055 PRK00055
ribonuclease Z; Reviewed
 26-93 1.23e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706427    26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:PRK00055  21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 27-88 2.03e-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: 2.03e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7706427   27 CIILEFKGRKIMLDCGIHPGLEG-MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTS 88
Cdd:cd07713  22 SLLIETEGKKILFDTGQSGVLLHnAKKLG----IDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
27-145 5.13e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 5.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   27 CIILEFKGRKIMLDCGiHPG--LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKTsfKGRTFMTHatKAIYR 104
Cdd:COG1237  24 SALIETEGKRILFDTG-QSDvlLKNAEKL----GIDLSDIDAVVLSHGHYDHTGGLPALLELN--PKAPVYAH--PDAFE 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7706427  105 WLLSDYVKVSNISaddMLYTETDLEESMDkietiNFHEVKE 145
Cdd:COG1237  95 KRYSKRPGGKYIG---IPFSREELEKLGA-----RLILVKE 127
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 26-87 2.26e-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: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL------------------IDPAEIDLLLISHFHLDHCGAL------P 81
Cdd:cd07729  33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGLdlfpnaT 112


                ....*.
gi 7706427   82 WFLQKT 87
Cdd:cd07729 113 IIVQRA 118
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 3-179 3.85e-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: 3.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    3 AIPAEESDQLLIRPLGAGQ-EVGRSCIILEFKGRKIMLD--CGIHPG------LEGMDALPYidliDPAEIDLLLISHFH 73
Cdd:cd07720  26 GAAPEAEAALLAAFLPPDPvETSVNAFLVRTGGRLILVDtgAGGLFGptagklLANLAAAGI----DPEDIDDVLLTHLH 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   74 LDHCGALpwflqKTSFKGRTF---MTHATKAIYRWLLSDyvkvsNISADDMLYTETDLEESMDKIET----INFHEVKEV 146
Cdd:cd07720 102 PDHIGGL-----VDAGGKPVFpnaEVHVSEAEWDFWLDD-----ANAAKAPEGAKRFFDAARDRLRPyaaaGRFEDGDEV 171

                       170       180       190
                ....*....|....*....|....*....|....
gi 7706427  147 A-GIKFWcYHAGHVLGAAMFMIEIAGVKLLYTGD 179
Cdd:cd07720 172 LpGITAV-PAPGHTPGHTGYRIESGGERLLIWGD 204
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 26-93 5.82e-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: 5.82e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7706427     26 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
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 ...
 26-207 9.73e-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: 9.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCG--IHP-GLEGMDALPyidlidPAEIDLLLiSHFHLDH-CGaLPWF--LQKTSFKGRTFMTHAT 99
Cdd:cd07715  24 SCVEVRAGGELLILDAGtgIRElGNELMKEGP------PGEAHLLL-SHTHWDHiQG-FPFFapAYDPGNRIHIYGPHKD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  100 KAIYRWLLSDYVKVSN--ISADDMLytetdleesmdkiETINFHEVKE-----VAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:cd07715  96 GGSLEEVLRRQMSPPYfpVPLEELL-------------AAIEFHDLEPgepfsIGGVTVTTIPLNHPGGALGYRIEEDGK 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7706427  173 KLLYTGDFsrqEDRHLMAAEIPNIKP-----DILIIESTY 207
Cdd:cd07715 163 SVVYATDT---EHYPDDGESDEALLEfargaDLLIHDAQY 199
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-179 1.23e-04

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: 43.64  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDCGIHPG----LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---- 97
Cdd:cd07726  17 ASYLLDGEGRPALIDTGPSSSvprlLAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEA--LPNAKVYVHprga 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   98 -----------ATKAIYRWLlsdyvkvsnisADDMLYTETDLEEsmDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMF 165
Cdd:cd07726  91 rhlidpsklwaSARAVYGDE-----------ADRLGGEILPVPE--ERVIVLEDGETLDLGGRTLEVIDTpGHAPHHLSF 157

                       170
                ....*....|....
gi 7706427  166 MIEIAGVklLYTGD 179
Cdd:cd07726 158 LDEESDG--LFTGD 169
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 26-81 1.29e-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: 1.29e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7706427   26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALP 81
Cdd:cd07719  19 PSTLVVVGGRVYLVDAG--SGvVRRLAQAG----LPLGDLDAVFLTHLHSDHVADLP 69
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 27-203 1.36e-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: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   27 CIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsfkgrtfmthatkaiyrwl 106
Cdd:cd07731  12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN-------------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  107 lsdyVKVSNISADDMLYTETDLEESMDKIET--INFHEVK-----EVAGIKFWCYHAGHVLGAAM------FMIEIAGVK 173
Cdd:cd07731  72 ----FPVKEVYMPGVTHTTKTYEDLLDAIKEkgIPVTPCKagdrwQLGGVSFEVLSPPKDDYDDLnnnscvLRLTYGGTS 147

                       170       180       190
                ....*....|....*....|....*....|
gi 7706427  174 LLYTGDFSRQEDRHLMAAEiPNIKPDILII 203
Cdd:cd07731 148 FLLTGDAEKEAEEELLASG-PDLLADVLKV 176
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-78 1.63e-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: 1.63e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 7706427   28 IILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCG 78
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 ...
 59-83 3.65e-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: 3.65e-04
                        10        20
                ....*....|....*....|....*
gi 7706427   59 IDPAEIDLLLISHFHLDHCGALPWF 83
Cdd:cd07730  79 IDPEDIDAVILSHLHWDHIGGLSDF 103
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-78 6.31e-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: 6.31e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706427   29 ILEFKGRKIMLDCGI-----HPGLEGMDAL--PYID-L----IDPAEIDLLLISHFHLDHCG 78
Cdd:cd16277  17 LVRTPGRTILVDTGIgndkpRPGPPAFHNLntPYLErLaaagVRPEDVDYVLCTHLHVDHVG 78
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 35-81 8.50e-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: 8.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 7706427   35 RKIMLDCGihpglEGMDalPYIDLI-------DPAEIDLLLISHFHLDHCGALP 81
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 ...
 35-207 1.09e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 40.76  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427     35 RKIMLDCGihPGLEGMDAL---PYIDLIDPaeIDLLLISHFHLDHCGALPwFLQktsfKGRTFMTHATKAIYRWLLSDYV 111
Cdd:pfam12706   1 RRILIDPG--PDLRQQALPalqPGRLRDDP--IDAVLLTHDHYDHLAGLL-DLR----EGRPRPLYAPLGVLAHLRRNFP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427    112 KVSNISADDMLYTETDLEESM---DKIETINFHEVKEVAGIKFWcYHAGHVLGaamFMIEIAGVKLLYTGD---FSRQED 185
Cdd:pfam12706  72 YLFLLEHYGVRVHEIDWGESFtvgDGGLTVTATPARHGSPRGLD-PNPGDTLG---FRIEGPGKRVYYAGDtgyFPDEIG 147

                         170       180
                  ....*....|....*....|..
gi 7706427    186 RHLMAAeipnikpDILIIESTY 207
Cdd:pfam12706 148 ERLGGA-------DLLLLDGGA 162
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 26-187 1.23e-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: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   26 SCIILEFKGRKIMLDcgihPGLEGMDALPYIDlIDPAEIDLLLISHFHLDHCGAlpwFLQKTSFKGRTFMtHATKAIYRW 105
Cdd:cd07738  16 SGFIIWINGRGIMVD----PPVNSTSYLRQNG-ISPRLVDHVILTHCHADHDAG---TFQKILEEEKITL-YTTRTINES 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427  106 LLSDYVKVSNISADdmlytetDLEESMDKIETINFHEVKeVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:cd07738  87 FLRKYAALTGLPPD-------FLEELFDFRPVIIGEKTK-INGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTRYDPD 158


                ..
gi 7706427  186 RH 187
Cdd:cd07738 159 GL 160
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-179 4.22e-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: 4.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   27 CIILEFKGRKIMLDCGI----------HPGLEG----MDALPYIDLiDPAEIDLLLISHFHLDHC-GALPWF---LQKTS 88
Cdd:cd16281  45 CLLIETGGRNILIDTGIgdkqdpkfrsIYVQHSehslLKSLARLGL-SPEDITDVILTHLHFDHCgGATRADddgLVELL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   89 FKGRTFMTHatKAIYRWLLSDYV--KVSNISADDMLytetdLEESmDKIETINFHEVKEVAGIKFWCYHaGHVLGAAMFM 166
Cdd:cd16281 124 FPNATYWVQ--KRHWEWALNPNPreRASFLPENIEP-----LEES-GRLKLIDGSDAELGPGIRFHLSD-GHTPGQMLPE 194

                       170
                ....*....|...
gi 7706427  167 IEIAGVKLLYTGD 179
Cdd:cd16281 195 ISTPGGTVVFAAD 207
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 58-83 5.34e-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: 5.34e-03
                        10        20
                ....*....|....*....|....*.
gi 7706427   58 LIDPAEIDLLLISHFHLDHCGALPWF 83
Cdd:cd07725  50 GLKPSDIDRVLLTHHHPDHIGLAGKL 75
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 28-179 6.48e-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: 6.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   28 IILEFKGRKIMLDCGIHPGL--------EGMDALPYI--DL----IDPAEIDLLLISHFHLDHCGALpwflqkTSFKGRT 93
Cdd:cd07728  46 ILIQYQGKNYLIDAGIGNGKltekqkrnFGVTEESSIeeSLaelgLTPEDIDYVLMTHLHFDHASGL------TKVKGEQ 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706427   94 FM------THATKAIyRWllsDYVKVSNISAddmlyTETDLEESMDKIE--TINF-HEVKEVAGIKFWcyH-AGHVLGAA 163
Cdd:cd07728 120 LVsvfpnaTIYVSEI-EW---EEMRNPNIRS-----KNTYWKENWEPIEdqVKTFsDEIEIVPGITMI--HtGGHSDGHS 188

                       170
                ....*....|....*.
gi 7706427  164 MFMIEIAGVKLLYTGD 179
Cdd:cd07728 189 IIEIEQGGETAIHMAD 204
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 27-87 6.66e-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: 38.36  E-value: 6.66e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7706427   27 CIILEFKGRKIMLDCGIhPG-----LEGMDALPYidliDPAEIDLLLISHFHLDHCGALPWFLQKT 87
Cdd:cd07721  13 AYLIEDDDGLTLIDTGL-PGsakriLKALRELGL----SPKDIRRILLTHGHIDHIGSLAALKEAP 73
 
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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