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Conserved domains on  [gi|1012443553|ref|NP_001308765|]
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cleavage and polyadenylation specificity factor subunit 3 isoform d [Homo sapiens]

Protein Classification

CPSF3/YSH1 family protein( domain architecture ID 11441009)

CPSF3/YSH1 family protein is a component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition; belongs to the metallo-beta-lactamase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 22-209 3.83e-144

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


:

Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.83e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  22 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 101
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 181
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 1012443553 182 GDFSRQEDRHLMAAEIPNIKPDILIIES 209
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 18-460 8.61e-120

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


The actual alignment was detected with superfamily member COG1782:

Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 365.61  E-value: 8.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTS 92
Cdd:COG1782     4 TFLGAAR-EVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  93 FKGRTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCY 158
Cdd:COG1782    78 YRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 159 HAGHVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIV 234
Cdd:COG1782   158 NAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 235 NRGGRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHIS 313
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLH 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 314 NLKSMDHFDDI----GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLK 389
Cdd:COG1782   314 YVESVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVR 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012443553 390 MSVDYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 460
Cdd:COG1782   393 AEVETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 483-686 3.74e-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: 3.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 483 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 561
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 562 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443553 638 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 686
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; ...
 22-209 3.83e-144

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.83e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  22 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 101
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 181
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 1012443553 182 GDFSRQEDRHLMAAEIPNIKPDILIIES 209
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 18-460 8.61e-120

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


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 365.61  E-value: 8.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTS 92
Cdd:COG1782     4 TFLGAAR-EVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  93 FKGRTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCY 158
Cdd:COG1782    78 YRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 159 HAGHVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIV 234
Cdd:COG1782   158 NAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 235 NRGGRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHIS 313
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLH 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 314 NLKSMDHFDDI----GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLK 389
Cdd:COG1782   314 YVESVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVR 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012443553 390 MSVDYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 460
Cdd:COG1782   393 AEVETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 483-686 3.74e-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: 3.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 483 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 561
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 562 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443553 638 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 686
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 ...
 481-687 3.65e-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: 3.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  481 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 554
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  555 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 631
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443553  632 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 687
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 ...
 250-371 1.03e-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: 1.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  250 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 324
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1012443553  325 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 371
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 ...
 250-369 1.18e-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: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 250 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 329
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1012443553 330 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 369
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
30-222 2.48e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.94  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 103
Cdd:COG1234    20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 104 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 178
Cdd:COG1234    94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1012443553 179 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 222
Cdd:COG1234   154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-199 3.61e-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: 3.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553   30 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 109
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  110 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 188
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 1012443553  189 DRHLMAAEIPN 199
Cdd:smart00849 142 GDGRTLVDGGD 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
30-199 4.04e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 109
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 110 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 189
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 1012443553 190 RHLMAAEIPN 199
Cdd:pfam00753 156 IGRLDLPLGG 165
PRK00055 PRK00055
ribonuclease Z; Reviewed
 30-97 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 1012443553  30 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 97
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 ...
 30-97 6.36e-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: 6.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012443553  30 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 97
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; ...
 22-209 3.83e-144

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.83e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  22 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 101
Cdd:cd16292     7 GAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 ATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 181
Cdd:cd16292    87 PTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYT 166

                         170       180
                  ....*....|....*....|....*...
gi 1012443553 182 GDFSRQEDRHLMAAEIPNIKPDILIIES 209
Cdd:cd16292   167 GDYSREEDRHLPAAEIPPIKPDVLIVES 194
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 18-460 8.61e-120

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


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 365.61  E-value: 8.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTS 92
Cdd:COG1782     4 TFLGAAR-EVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  93 FKGRTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCY 158
Cdd:COG1782    78 YRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 159 HAGHVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIV 234
Cdd:COG1782   158 NAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 235 NRGGRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHIS 313
Cdd:COG1782   235 ERGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLH 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 314 NLKSMDHFDDI----GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLK 389
Cdd:COG1782   314 YVESVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVR 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012443553 390 MSVDYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 460
Cdd:COG1782   393 AEVETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 18-425 2.60e-119

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 362.20  E-value: 2.60e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 97
Cdd:COG1236     4 TFLGAAG-EVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  98 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 176
Cdd:COG1236    80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 177 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 256
Cdd:COG1236   160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 257 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 333
Cdd:COG1236   239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 334 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 412
Cdd:COG1236   311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                         410
                  ....*....|....
gi 1012443553 413 LKPP-HVILVHGEQ 425
Cdd:COG1236   390 TGKPeRVFLVHGEP 403
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 22-209 2.98e-91

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 281.91  E-value: 2.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  22 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTH 101
Cdd:cd07734     4 GGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 ATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAGVKLL 179
Cdd:cd07734    84 PTVALGRLLLEDYVKSAERIGQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGEKLV 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1012443553 180 YTGDFSRQEDRHLMAAEIPNIKPDILIIES 209
Cdd:cd07734   164 YTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 483-686 3.74e-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: 3.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 483 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 561
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 562 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443553 638 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 686
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 22-209 2.88e-68

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293849  Cd Length: 199  Bit Score: 222.14  E-value: 2.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  22 GAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAE-----IDLLLISHFHLDHCGALPWFLQKTSFKGR 96
Cdd:cd16291     5 GAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGpftehIDCVIISHFHLDHCGALPYFTEVVGYDGP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  97 TFMTHATKAIYRWLLSDYVKVS-NISADDMLYTETDLEESMDKIETINFHEVKEV-AGIKFWCYHAGHVLGAAMFMIEIA 174
Cdd:cd16291    85 IYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFYVRVG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1012443553 175 GVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 209
Cdd:cd16291   165 DESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 481-687 3.65e-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: 3.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  481 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 554
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  555 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 631
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443553  632 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 687
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 18-209 3.02e-61

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 203.07  E-value: 3.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL-IDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGR 96
Cdd:cd16295     2 TFLGAAR-EVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  97 TFMTHATKAIYRWLLSDYVKVSNISADDM----LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMI 171
Cdd:cd16295    80 IYATPATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVEL 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1012443553 172 EI-AGVKLLYTGDFSRQEDRhLMAAEIPNIKPDILIIES 209
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 ...
 250-371 1.03e-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: 1.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  250 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 324
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1012443553  325 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 371
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 ...
 250-369 1.18e-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: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 250 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 329
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1012443553 330 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 369
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
30-222 2.48e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.94  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 103
Cdd:COG1234    20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 104 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 178
Cdd:COG1234    94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1012443553 179 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 222
Cdd:COG1234   154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 21-209 1.80e-18

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: 84.11  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  21 GGAGQEvGRSCIILEFKGRKIMLDCG--IHPGLEGMDALPYIdlidPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTF 98
Cdd:cd16293     5 SGAGDE-SPLCYLLEIDDVTILLDCGwdESFDMEYLESLKRI----APTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  99 MTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVA----GIKFWCYHAGHVLGAAMFMIEIA 174
Cdd:cd16293    80 ATLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWKITKD 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1012443553 175 GVKLLYTGDFSRQEDRHLMAAEIPNI---KPDILIIES 209
Cdd:cd16293   160 SEDIVYAVDWNHKKERHLNGAVLDSFgglRPSLLITDA 197
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-208 1.24e-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: 78.81  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  18 TFKGGAGqEVGRSCIILEFKGRKIMLDCG-----------------IHPGLEGMDALPYIDLI-------DPAEIDLLLI 73
Cdd:cd07732     3 TIHRGTN-EIGGNCIEVETGGTRILLDFGlpldpeskyfdevldflELGLLPDIVGLYRDPLLlgglrseEDPSVDAVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  74 SHFHLDHCGALPWFLQKTSFkgrtFMTHATKAIYRWLLSDYVKVSNISADdmlytetdleesmdkIETINFHEVKEVAGI 153
Cdd:cd07732    82 SHAHLDHYGLLNYLRPDIPV----YMGEATKRILKALLPFFGEGDPVPRN---------------IRVFESGKSFTIGDF 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 154 KFWCYHAGH-VLGAAMFMIEIAGVKLLYTGDF----SRQEDRHLMAAEIPNiKPDILIIE 208
Cdd:cd07732   143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELTEAFVEKAPK-NIDVLLME 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-199 3.61e-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: 3.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553   30 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 109
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  110 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 188
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 1012443553  189 DRHLMAAEIPN 199
Cdd:smart00849 142 GDGRTLVDGGD 152
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 21-209 5.11e-16

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: 76.53  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  21 GGAGQEVGR--SCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGR 96
Cdd:cd16272     7 GGAVPSLTRntSSYLLETGGTRILLDCGegTVYRLLKAG-------VDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  97 T-----FMTHATKAIYRWLLSDYVKVSnisaddmlytetDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMI 171
Cdd:cd16272    80 KkpltiYGPKGIKEFLEKLLNFPVEIL------------PLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRI 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1012443553 172 EIAGVKLLYTGDfsrqedrhlmAAEIPNIKP-----DILIIES 209
Cdd:cd16272   148 EAEGKSIVYSGD----------TGPCENLVElakgaDLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
30-199 4.04e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 109
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 110 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 189
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 1012443553 190 RHLMAAEIPN 199
Cdd:pfam00753 156 IGRLDLPLGG 165
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 33-206 1.58e-13

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 69.55  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  33 ILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPaEIDLLLISHFHLDHCGALPWFLQKtsfKGRTFMTH----ATKAIY- 107
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYLEKILP-EVDLILLSHPTLEHLGAYPLLYYK---FGSHLGSNipvyATLPVAn 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 108 --RWLLSDYVKVSNISA--DDMLYTETDLEESMDKIETINFHEVKEV----AGIKFWCYHAGHVLGAAMFMIEIAGVKLL 179
Cdd:pfam16661  77 lgRVSTYDLYASRGILGpyDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIV 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1012443553 180 YTGDFSRQEDRHLMAAEIPN---------IKPDILI 206
Cdd:pfam16661 157 YAVDWNHTKDSHLNGASLLDstgkpleslVRPTALI 192
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 21-221 9.57e-13

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: 68.59  E-value: 9.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  21 GGAGqEVGRSCIILEFKGRKIMLDCGIHPGLEGMdalPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK- 90
Cdd:cd07714     4 GGLG-EIGKNMYVVEYDDDIIIIDCGLKFPDEDM---PGVDYIIPdfsyleenkDKIKGIFITHGHEDHIGALPYLLPEl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  91 ------TSFkgrtfmthaTKAIYRWLLSDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGH-V 163
Cdd:cd07714    80 nvpiyaTPL---------TLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHsI 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443553 164 LGAAMFMIEIAGVKLLYTGDF--------SRQEDRHLMaAEIPNIKPDILIIESTYGTHiHEKREE 221
Cdd:cd07714   134 PDSVGLAIKTPEGTIVHTGDFkfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 29-172 1.91e-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: 65.98  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  29 RSCIILEFKGRKIMLDCGIhpglegmDALPYIDLIDPAEIDLLLISHFHldHCGALPWFLQKTSFKGRTFMTHATKAIYR 108
Cdd:cd16294    12 LPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1012443553 109 WLLSDYVkvsnisaddmlytetdleESMDKIETINFHEVKEVAG-IKFWCYHAGHVLGAAMFMIE 172
Cdd:cd16294    83 LLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQ 129
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 385-452 1.95e-11

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 59.56  E-value: 1.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443553 385 KLPLKMSVDYIS-FSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNP 452
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL------GIEVFVP 63
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 31-184 3.66e-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: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  31 CIILEFKGRK-IMLDcgihPGLEGMDALpyIDLID--PAEIDLLLISHFHLDHCGALPWFLQKTSFKgrtfmTHATKAIY 107
Cdd:cd06262    12 CYLVSDEEGEaILID----PGAGALEKI--LEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAP-----VYIHEADA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012443553 108 RWLLSDyvkvsnisADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGDF 184
Cdd:cd06262    81 ELLEDP--------ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEGV--LFTGDT 148
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 29-211 4.03e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 61.06  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  29 RSCIILEFKGRKIMLDCGihPGL-EGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG-RTFMTHATKAi 106
Cdd:COG1235    35 RSSILVEADGTRLLIDAG--PDLrEQLLRLG----LDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLE- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 107 yrwllsdyvkvsniSADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCY---H-AGHVLGaamFMIEIAGVKLLYTG 182
Cdd:COG1235   108 --------------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFpvpHdAGDPVG---YRIEDGGKKLAYAT 170

                         170       180       190
                  ....*....|....*....|....*....|
gi 1012443553 183 DFSrqedrHLMAAEIPNIK-PDILIIESTY 211
Cdd:COG1235   171 DTG-----YIPEEVLELLRgADLLILDATY 195
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 30-212 7.90e-10

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 59.77  E-value: 7.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMT 100
Cdd:cd07717    18 SSIALRLEGELWLFDCG-----EGtqrqLLRAG----LSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTepltiYGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 101 HATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVKEVAGIKF-------WCYHAGHVLGAAMFMIEI 173
Cdd:cd07717    89 KGLKEFLETLL-------RLSASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYRFEE 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1012443553 174 aGVKLLYTGDfSRQEDRHLMAAEipniKPDILIIESTYG 212
Cdd:cd07717   149 -GRKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 27-207 7.14e-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: 57.17  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  27 VGR-SCIILEFKGRKIML-DCGIHPGLEGMDA--LPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH- 101
Cdd:COG2333     8 VGQgDAILIRTPDGKTILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA--FPVGRVLVSg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 --ATKAIYRWLLsDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGHVLGAAM--------FMI 171
Cdd:COG2333    86 ppDTSETYERLL-EALKEKGI-----------------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSdennnslvLRL 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1012443553 172 EIAGVKLLYTGDFSRQEDRHLMAAEiPNIKPDILII 207
Cdd:COG2333   148 TYGGFSFLLTGDAEAEAEAALLARG-PDLKADVLKV 182
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 27-221 1.23e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 56.08  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  27 VGRSCIILEFKGRKIMLDcgihPGLEGMDALPYIDLIDPAE---IDLLLISHFHLDHCGalpwflqktsfkgrtfmthat 103
Cdd:COG2220     9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLDPEDlpkIDAVLVTHDHYDHLD--------------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 104 KAIYRWLLSDYVKV-SNISADDMLytetdLEESMDKIETINFHEVKEVAGIKFWCYHAGH--------VLGAAMFMIEIA 174
Cdd:COG2220    64 DATLRALKRTGATVvAPLGVAAWL-----RAWGFPRVTELDWGESVELGGLTVTAVPARHssgrpdrnGGLWVGFVIETD 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1012443553 175 GVKLLYTGD------FSRQEDRHlmaaeipniKPDILIIEsTYGTHIHEKREE 221
Cdd:COG2220   139 GKTIYHAGDtgyfpeMKEIGERF---------PIDVALLP-IGAYPFTMGPEE 181
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
21-90 1.37e-08

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 57.76  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  21 GGAGqEVGRSCIILEFKGRKIMLDCGI-HPGlegmDALPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK 90
Cdd:COG0595    12 GGLG-EIGKNMYVYEYDDDIIIVDCGLkFPE----DEMPGVDLVIPdisyleenkDKIKGIVLTHGHEDHIGALPYLLKE 86
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 30-183 2.82e-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: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGihPGlegmdALPYI-DLIDPAEIDLLLISHFHLDHCGALPWFLqktsfkgrtfmthatkaiYR 108
Cdd:cd07716    19 SGYLLEADGFRILLDCG--SG-----VLSRLqRYIDPEDLDAVVLSHLHPDHCADLGVLQ------------------YA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 109 WLLSDYVKVSNI-------SADDMLYTETDLEESMDkIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 181
Cdd:cd07716    74 RRYHPRGARKPPlplygpaGPAERLAALYGLEDVFD-FHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYT 152


                  ..
gi 1012443553 182 GD 183
Cdd:cd07716   153 GD 154
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-88 4.11e-08

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 53.80  E-value: 4.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1012443553  22 GAGQEVG-----RSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFL 88
Cdd:cd07740     4 GSGDAFGsggrlNTCFHVASEAGRFLIDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-200 6.33e-08

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 53.54  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  31 CIILEFKGRKIMLDcgihPGLEGMDALPYIDLID--PAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHAT-KAIY 107
Cdd:COG0491    17 SYLIVGGDGAVLID----TGLGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEaEALE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 108 RWLLSDYVKVSNISADdmlytetdleesmdkiETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDfsr 186
Cdd:COG0491    91 APAAGALFGREPVPPD----------------RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD--- 149

                         170
                  ....*....|....
gi 1012443553 187 qedrHLMAAEIPNI 200
Cdd:COG0491   150 ----ALFSGGVGRP 159
PRK00055 PRK00055
ribonuclease Z; Reviewed
 30-97 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 1012443553  30 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 97
Cdd:PRK00055   21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 31-92 2.10e-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: 2.10e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012443553  31 CIILEFKGRKIMLDCGIHPGLEG-MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTS 92
Cdd:cd07713    22 SLLIETEGKKILFDTGQSGVLLHnAKKLG----IDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
31-149 5.51e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  31 CIILEFKGRKIMLDCGiHPG--LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKTsfKGRTFMTHatKAIYR 108
Cdd:COG1237    24 SALIETEGKRILFDTG-QSDvlLKNAEKL----GIDLSDIDAVVLSHGHYDHTGGLPALLELN--PKAPVYAH--PDAFE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1012443553 109 WLLSDYVKVSNISaddMLYTETDLEESMDkietiNFHEVKE 149
Cdd:COG1237    95 KRYSKRPGGKYIG---IPFSREELEKLGA-----RLILVKE 127
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 30-91 1.81e-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: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL------------------IDPAEIDLLLISHFHLDHCGAL------P 85
Cdd:cd07729    33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGLdlfpnaT 112


                  ....*.
gi 1012443553  86 WFLQKT 91
Cdd:cd07729   113 IIVQRA 118
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 30-183 4.33e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 48.70  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLD--CGIHPG------LEGMDALPYidliDPAEIDLLLISHFHLDHCGALpwflqKTSFKGRTF--- 98
Cdd:cd07720    50 NAFLVRTGGRLILVDtgAGGLFGptagklLANLAAAGI----DPEDIDDVLLTHLHPDHIGGL-----VDAGGKPVFpna 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  99 MTHATKAIYRWLLSDyvkvsNISADDMLYTETDLEESMDKIET----INFHEVKEVA-GIKFWcYHAGHVLGAAMFMIEI 173
Cdd:cd07720   121 EVHVSEAEWDFWLDD-----ANAAKAPEGAKRFFDAARDRLRPyaaaGRFEDGDEVLpGITAV-PAPGHTPGHTGYRIES 194

                         170
                  ....*....|
gi 1012443553 174 AGVKLLYTGD 183
Cdd:cd07720   195 GGERLLIWGD 204
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 30-97 6.36e-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: 6.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012443553  30 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 97
Cdd:TIGR02651  19 PSIALKLNGELWLFDCG-----EGtqrqmLRSG-----ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 30-183 8.81e-05

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 44.41  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCGIHPG----LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---- 101
Cdd:cd07726    17 ASYLLDGEGRPALIDTGPSSSvprlLAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEA--LPNAKVYVHprga 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 102 -----------ATKAIYRWLlsdyvkvsnisADDMLYTETDLEEsmDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMF 169
Cdd:cd07726    91 rhlidpsklwaSARAVYGDE-----------ADRLGGEILPVPE--ERVIVLEDGETLDLGGRTLEVIDTpGHAPHHLSF 157

                         170
                  ....*....|....
gi 1012443553 170 MIEIAGVklLYTGD 183
Cdd:cd07726   158 LDEESDG--LFTGD 169
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 30-211 9.89e-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: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDCG--IHP-GLEGMDALPyidlidPAEIDLLLiSHFHLDH-CGaLPWF--LQKTSFKGRTFMTHAT 103
Cdd:cd07715    24 SCVEVRAGGELLILDAGtgIRElGNELMKEGP------PGEAHLLL-SHTHWDHiQG-FPFFapAYDPGNRIHIYGPHKD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 104 KAIYRWLLSDYVKVSN--ISADDMLytetdleesmdkiETINFHEVKE-----VAGIKFWCYHAGHVLGAAMFMIEIAGV 176
Cdd:cd07715    96 GGSLEEVLRRQMSPPYfpVPLEELL-------------AAIEFHDLEPgepfsIGGVTVTTIPLNHPGGALGYRIEEDGK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1012443553 177 KLLYTGDFsrqEDRHLMAAEIPNIKP-----DILIIESTY 211
Cdd:cd07715   163 SVVYATDT---EHYPDDGESDEALLEfargaDLLIHDAQY 199
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 31-207 1.26e-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: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  31 CIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsfkgrtfmthatkaiyrwl 110
Cdd:cd07731    12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN-------------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 111 lsdyVKVSNISADDMLYTETDLEESMDKIET--INFHEVK-----EVAGIKFWCYHAGHVLGAAM------FMIEIAGVK 177
Cdd:cd07731    72 ----FPVKEVYMPGVTHTTKTYEDLLDAIKEkgIPVTPCKagdrwQLGGVSFEVLSPPKDDYDDLnnnscvLRLTYGGTS 147

                         170       180       190
                  ....*....|....*....|....*....|
gi 1012443553 178 LLYTGDFSRQEDRHLMAAEiPNIKPDILII 207
Cdd:cd07731   148 FLLTGDAEKEAEEELLASG-PDLLADVLKV 176
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 30-85 1.30e-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: 1.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1012443553  30 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALP 85
Cdd:cd07719    19 PSTLVVVGGRVYLVDAG--SGvVRRLAQAG----LPLGDLDAVFLTHLHSDHVADLP 69
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-82 1.70e-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: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1012443553  32 IILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCG 82
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 ...
 63-87 3.48e-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: 3.48e-04
                          10        20
                  ....*....|....*....|....*
gi 1012443553  63 IDPAEIDLLLISHFHLDHCGALPWF 87
Cdd:cd07730    79 IDPEDIDAVILSHLHWDHIGGLSDF 103
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-82 6.12e-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: 6.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1012443553  33 ILEFKGRKIMLDCGI-----HPGLEGMDAL--PYID-L----IDPAEIDLLLISHFHLDHCG 82
Cdd:cd16277    17 LVRTPGRTILVDTGIgndkpRPGPPAFHNLntPYLErLaaagVRPEDVDYVLCTHLHVDHVG 78
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 39-85 8.40e-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: 8.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1012443553  39 RKIMLDCGihpglEGMDalPYIDLI-------DPAEIDLLLISHFHLDHCGALP 85
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 ...
 39-211 8.64e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 41.14  E-value: 8.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  39 RKIMLDCGihPGLEGMDAL---PYIDLIDPaeIDLLLISHFHLDHCGALPwFLQktsfKGRTFMTHATKAIYRWLLSDYV 115
Cdd:pfam12706   1 RRILIDPG--PDLRQQALPalqPGRLRDDP--IDAVLLTHDHYDHLAGLL-DLR----EGRPRPLYAPLGVLAHLRRNFP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 116 KVSNISADDMLYTETDLEESM---DKIETINFHEVKEVAGIKFWcYHAGHVLGaamFMIEIAGVKLLYTGD---FSRQED 189
Cdd:pfam12706  72 YLFLLEHYGVRVHEIDWGESFtvgDGGLTVTATPARHGSPRGLD-PNPGDTLG---FRIEGPGKRVYYAGDtgyFPDEIG 147

                         170       180
                  ....*....|....*....|..
gi 1012443553 190 RHLMAAeipnikpDILIIESTY 211
Cdd:pfam12706 148 ERLGGA-------DLLLLDGGA 162
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 30-191 1.34e-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: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  30 SCIILEFKGRKIMLDcgihPGLEGMDALPYIDlIDPAEIDLLLISHFHLDHCGAlpwFLQKTSFKGRTFMtHATKAIYRW 109
Cdd:cd07738    16 SGFIIWINGRGIMVD----PPVNSTSYLRQNG-ISPRLVDHVILTHCHADHDAG---TFQKILEEEKITL-YTTRTINES 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553 110 LLSDYVKVSNISADdmlytetDLEESMDKIETINFHEVKeVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 189
Cdd:cd07738    87 FLRKYAALTGLPPD-------FLEELFDFRPVIIGEKTK-INGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTRYDPD 158


                  ..
gi 1012443553 190 RH 191
Cdd:cd07738   159 GL 160
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-183 3.82e-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: 39.79  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  31 CIILEFKGRKIMLDCGI----------HPGLEG----MDALPYIDLiDPAEIDLLLISHFHLDHC-GALPWF---LQKTS 92
Cdd:cd16281    45 CLLIETGGRNILIDTGIgdkqdpkfrsIYVQHSehslLKSLARLGL-SPEDITDVILTHLHFDHCgGATRADddgLVELL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  93 FKGRTFMTHatKAIYRWLLSDYV--KVSNISADDMLytetdLEESmDKIETINFHEVKEVAGIKFWCYHaGHVLGAAMFM 170
Cdd:cd16281   124 FPNATYWVQ--KRHWEWALNPNPreRASFLPENIEP-----LEES-GRLKLIDGSDAELGPGIRFHLSD-GHTPGQMLPE 194

                         170
                  ....*....|...
gi 1012443553 171 IEIAGVKLLYTGD 183
Cdd:cd16281   195 ISTPGGTVVFAAD 207
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 62-87 4.95e-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: 38.82  E-value: 4.95e-03
                          10        20
                  ....*....|....*....|....*.
gi 1012443553  62 LIDPAEIDLLLISHFHLDHCGALPWF 87
Cdd:cd07725    50 GLKPSDIDRVLLTHHHPDHIGLAGKL 75
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 31-91 6.01e-03

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 38.74  E-value: 6.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443553  31 CIILEFKGRKIMLDCGIhPG-----LEGMDALPYidliDPAEIDLLLISHFHLDHCGALPWFLQKT 91
Cdd:cd07721    13 AYLIEDDDGLTLIDTGL-PGsakriLKALRELGL----SPKDIRRILLTHGHIDHIGSLAALKEAP 73
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 32-183 7.53e-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: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  32 IILEFKGRKIMLDCGIHPGL--------EGMDALPYI--DL----IDPAEIDLLLISHFHLDHCGALpwflqkTSFKGRT 97
Cdd:cd07728    46 ILIQYQGKNYLIDAGIGNGKltekqkrnFGVTEESSIeeSLaelgLTPEDIDYVLMTHLHFDHASGL------TKVKGEQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443553  98 FM------THATKAIyRWllsDYVKVSNISAddmlyTETDLEESMDKIE--TINF-HEVKEVAGIKFWcyH-AGHVLGAA 167
Cdd:cd07728   120 LVsvfpnaTIYVSEI-EW---EEMRNPNIRS-----KNTYWKENWEPIEdqVKTFsDEIEIVPGITMI--HtGGHSDGHS 188

                         170
                  ....*....|....*.
gi 1012443553 168 MFMIEIAGVKLLYTGD 183
Cdd:cd07728   189 IIEIEQGGETAIHMAD 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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