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Conserved domains on  [gi|1012443600|ref|NP_001308763|]
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cleavage and polyadenylation specificity factor subunit 3 isoform b [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; ...
 1-168 9.48e-127

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: 371.92  E-value: 9.48e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:cd16292    27 MLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYVRVSNIS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIK 160
Cdd:cd16292   107 SDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIK 186


                  ....*...
gi 1012443600 161 PDILIIES 168
Cdd:cd16292   187 PDVLIVES 194
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-419 2.70e-108

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: 334.79  E-value: 2.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGRTFMTHATKAIYRWLLSDYVK 75
Cdd:COG1782    27 LLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYGYRGPIYCTPPTRDLMALLLLDSAK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  76 V-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAG--VKLLY 139
Cdd:COG1782   102 IqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFYNAGHILGSAIVHLHIGDglHNIVF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 140 TGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILD 217
Cdd:COG1782   182 SGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLN 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 218 EYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHISNLKSMDHFDDI----GPSVVMASP 292
Cdd:COG1782   259 ELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHYVESVEESKEIndsdEPAIIIATS 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 293 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVDYI-SFSAHTDYQQTSEFIRA 371
Cdd:COG1782   338 GMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRAEVETIdGFSGHADRNELLNWLRR 416

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1012443600 372 L--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 419
Cdd:COG1782   417 LkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 442-645 2.29e-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: 276.31  E-value: 2.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 442 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 520
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 521 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 596
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443600 597 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 645
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; ...
 1-168 9.48e-127

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: 371.92  E-value: 9.48e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:cd16292    27 MLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYVRVSNIS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIK 160
Cdd:cd16292   107 SDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIK 186


                  ....*...
gi 1012443600 161 PDILIIES 168
Cdd:cd16292   187 PDVLIVES 194
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-419 2.70e-108

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: 334.79  E-value: 2.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGRTFMTHATKAIYRWLLSDYVK 75
Cdd:COG1782    27 LLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYGYRGPIYCTPPTRDLMALLLLDSAK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  76 V-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAG--VKLLY 139
Cdd:COG1782   102 IqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFYNAGHILGSAIVHLHIGDglHNIVF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 140 TGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILD 217
Cdd:COG1782   182 SGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLN 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 218 EYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHISNLKSMDHFDDI----GPSVVMASP 292
Cdd:COG1782   259 ELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHYVESVEESKEIndsdEPAIIIATS 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 293 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVDYI-SFSAHTDYQQTSEFIRA 371
Cdd:COG1782   338 GMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRAEVETIdGFSGHADRNELLNWLRR 416

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1012443600 372 L--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 419
Cdd:COG1782   417 LkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 442-645 2.29e-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: 276.31  E-value: 2.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 442 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 520
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 521 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 596
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443600 597 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 645
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 ...
 440-646 3.06e-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: 208.42  E-value: 3.06e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  440 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 513
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  514 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 590
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443600  591 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 646
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 ...
 209-330 7.26e-46

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 158.47  E-value: 7.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  209 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 283
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1012443600  284 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 330
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 ...
 209-328 1.11e-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: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 209 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 288
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1012443600 289 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 328
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-181 1.06e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 74.08  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHATKAIYRWLLsdyv 74
Cdd:COG1234    32 LIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGTKEFLEALL---- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  75 kvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDfSRqedr 149
Cdd:COG1234   102 ---KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD-TR---- 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1012443600 150 hLMAAEIPNIK-PDILIIESTYGTHIHEKREER 181
Cdd:COG1234   161 -PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-158 2.69e-13

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: 68.35  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600    1 MLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrwllsDYVKVSNIS 80
Cdd:smart00849  13 LIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA--------ELLKDLLAL 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600   81 ADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQEDRHLMAAEIPN 158
Cdd:smart00849  80 LGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAGGDGRTLVDGGD 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-158 4.10e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:pfam00753  19 LIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLAASRLGLPG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012443600  81 AddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPN 158
Cdd:pfam00753  98 P---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-56 2.23e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 40.55  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 56
Cdd:PRK00055   33 LFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 22-56 4.90e-03

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: 39.51  E-value: 4.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 56
Cdd:TIGR02651  47 ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 1-168 9.48e-127

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: 371.92  E-value: 9.48e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:cd16292    27 MLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYVRVSNIS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIK 160
Cdd:cd16292   107 SDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIK 186


                  ....*...
gi 1012443600 161 PDILIIES 168
Cdd:cd16292   187 PDVLIVES 194
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 1-419 2.70e-108

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: 334.79  E-value: 2.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGRTFMTHATKAIYRWLLSDYVK 75
Cdd:COG1782    27 LLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYGYRGPIYCTPPTRDLMALLLLDSAK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  76 V-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAG--VKLLY 139
Cdd:COG1782   102 IqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFYNAGHILGSAIVHLHIGDglHNIVF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 140 TGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILD 217
Cdd:COG1782   182 SGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLN 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 218 EYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHISNLKSMDHFDDI----GPSVVMASP 292
Cdd:COG1782   259 ELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHYVESVEESKEIndsdEPAIIIATS 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 293 GMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVDYI-SFSAHTDYQQTSEFIRA 371
Cdd:COG1782   338 GMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRAEVETIdGFSGHADRNELLNWLRR 416

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1012443600 372 L--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 419
Cdd:COG1782   417 LkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-384 7.05e-108

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 331.77  E-value: 7.05e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:COG1236    27 LIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPIYATPATADLARILLGDSAKIQEEE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNi 159
Cdd:COG1236   104 AEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVP- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 160 KPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIyYASSLAK 239
Cdd:COG1236   183 PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYLLRELKKEG-RLPDIPI-YVSGMAI 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 240 KCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASPGMMQSGLSRELFESWCTDKRNGVI 316
Cdd:COG1236   261 RATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTIL 334

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 317 IAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRALKPP-HVILVHGEQ 384
Cdd:COG1236   335 FVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKATGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 442-645 2.29e-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: 276.31  E-value: 2.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 442 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLCYQLQKLTGDVEELEIQEK-PALKVFKNITVI 520
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 521 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVS-VKDDS 596
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443600 597 ILSVTVDGKTANLNLETRTVECEegsedDESLREMVELAAQRLYEALTP 645
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 1-168 9.70e-79

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: 248.40  E-value: 9.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:cd07734    24 LLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDM-LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPN 158
Cdd:cd07734   104 GQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILP 183

                         170
                  ....*....|
gi 1012443600 159 IKPDILIIES 168
Cdd:cd07734   184 PRPDLLITES 193
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 440-646 3.06e-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: 208.42  E-value: 3.06e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  440 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFNLLCYQLQKLT---GDVEELEIQEKPALKV 513
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  514 FKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCV 590
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1012443600  591 SVKDDSILSVTVDGKTANLNLETRTVECeegsEDDESLREMVELAAQRLYEALTPV 646
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 1-168 2.80e-54

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: 184.00  E-value: 2.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPAE-----IDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVK 75
Cdd:cd16291    25 MFDCGMHMGYNDERRFPDFSYISQNGpftehIDCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPTKAICPILLEDYRK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  76 VS-NISADDMLYTETDLEESMDKIETINFHEVKEV-AGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMA 153
Cdd:cd16291   105 IAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGA 184

                         170
                  ....*....|....*
gi 1012443600 154 AEIPNIKPDILIIES 168
Cdd:cd16291   185 AWIDRLRPDLLITES 199
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 1-168 2.17e-48

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: 168.02  E-value: 2.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDL-IDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNI 79
Cdd:cd16295    25 LLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGPIYATPATKDLAELLLLDSAKIQEE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  80 SADDM----LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEI-AGVKLLYTGDFSRQEDRhLMA 153
Cdd:cd16295   104 EAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVELEIgGGKRILFSGDLGRKNTP-LLR 182

                         170
                  ....*....|....*
gi 1012443600 154 AEIPNIKPDILIIES 168
Cdd:cd16295   183 DPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 209-330 7.26e-46

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 158.47  E-value: 7.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  209 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 283
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1012443600  284 GPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 330
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 ...
 209-328 1.11e-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: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 209 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 288
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1012443600 289 MASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 328
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-181 1.06e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 74.08  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHATKAIYRWLLsdyv 74
Cdd:COG1234    32 LIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGTKEFLEALL---- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  75 kvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDfSRqedr 149
Cdd:COG1234   102 ---KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD-TR---- 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1012443600 150 hLMAAEIPNIK-PDILIIESTYGTHIHEKREER 181
Cdd:COG1234   161 -PCEALVELAKgADLLIHEATFLDEEAELAKET 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 1-168 2.00e-14

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: 72.17  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCG--IHPGLEGMDALPYIdlidPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSN 78
Cdd:cd16293    25 LLDCGwdESFDMEYLESLKRI----APTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLYQSRG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  79 ISADDMLYTETDLEESMDKIETINFHEVKEVA----GIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAA 154
Cdd:cd16293   101 LEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWKITKDSEDIVYAVDWNHKKERHLNGA 180

                         170
                  ....*....|....*..
gi 1012443600 155 EIPNI---KPDILIIES 168
Cdd:cd16293   181 VLDSFgglRPSLLITDA 197
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-158 2.69e-13

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: 68.35  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600    1 MLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrwllsDYVKVSNIS 80
Cdd:smart00849  13 LIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA--------ELLKDLLAL 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600   81 ADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQEDRHLMAAEIPN 158
Cdd:smart00849  80 LGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAGGDGRTLVDGGD 152
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-167 2.21e-12

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: 66.48  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   8 PGLEGMDALPYIDLI-DPAEIDLLLISHFHLDHCGALPWFLQKTSFkgrtFMTHATKAIYRWLLSDYVKVSNISADdmly 86
Cdd:cd07732    56 VGLYRDPLLLGGLRSeEDPSVDAVLLSHAHLDHYGLLNYLRPDIPV----YMGEATKRILKALLPFFGEGDPVPRN---- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  87 tetdleesmdkIETINFHEVKEVAGIKFWCYHAGH-VLGAAMFMIEIAGVKLLYTGDF----SRQEDRHLMAAEIPNiKP 161
Cdd:cd07732   128 -----------IRVFESGKSFTIGDFTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELTEAFVEKAPK-NI 195


                  ....*.
gi 1012443600 162 DILIIE 167
Cdd:cd07732   196 DVLLME 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-158 4.10e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNIS 80
Cdd:pfam00753  19 LIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLAASRLGLPG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012443600  81 AddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPN 158
Cdd:pfam00753  98 P---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 344-411 2.00e-11

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


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 59.56  E-value: 2.00e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600 344 KLPLKMSVDYIS-FSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNP 411
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL------GIEVFVP 63
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 1-168 1.44e-10

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: 60.74  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHATKAIYRWLLSDY 73
Cdd:cd16272    30 LLDCGegTVYRLLKAG-------VDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKkpltiYGPKGIKEFLEKLLNFP 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  74 VKVSnisaddmlytetDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDfsrqedrhlmA 153
Cdd:cd16272   103 VEIL------------PLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGD----------T 160

                         170       180
                  ....*....|....*....|
gi 1012443600 154 AEIPNIKP-----DILIIES 168
Cdd:cd16272   161 GPCENLVElakgaDLLIHEC 180
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 1-165 7.25e-10

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 58.76  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMDALPYIDLIDPaEIDLLLISHFHLDHCGALPWFLQKtsfKGRTFMTH----ATKAIY---RWLLSDY 73
Cdd:pfam16661  10 LLDPGWDGSFSYESDLKYLEKILP-EVDLILLSHPTLEHLGAYPLLYYK---FGSHLGSNipvyATLPVAnlgRVSTYDL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  74 VKVSNISA--DDMLYTETDLEESMDKIETINFHEVKEV----AGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQE 147
Cdd:pfam16661  86 YASRGILGpyDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIVYAVDWNHTK 165

                         170       180
                  ....*....|....*....|....*..
gi 1012443600 148 DRHLMAAEIPN---------IKPDILI 165
Cdd:pfam16661 166 DSHLNGASLLDstgkpleslVRPTALI 192
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 8-143 2.52e-09

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: 57.30  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   8 PGLEGMDALpyIDLID--PAEIDLLLISHFHLDHCGALPWFLQKTSFKgrtfmTHATKAIYRWLLSDyvkvsnisADDML 85
Cdd:cd06262    27 PGAGALEKI--LEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAP-----VYIHEADAELLEDP--------ELNLA 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600  86 YTETDLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGDF 143
Cdd:cd06262    92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEGV--LFTGDT 148
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 1-131 5.85e-08

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: 52.88  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIhpglegmDALPYIDLIDPAEIDLLLISHFHldHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVkvsnis 80
Cdd:cd16294    25 MLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELV------ 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1012443600  81 addmlytetdleESMDKIETINFHEVKEVAG-IKFWCYHAGHVLGAAMFMIE 131
Cdd:cd16294    90 ------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQ 129
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-47 5.63e-07

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: 50.34  E-value: 5.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1012443600   2 LDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFL 47
Cdd:cd07740    30 IDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-142 5.97e-07

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: 50.84  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   8 PGLEGMDALPYIDLID--PAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHAT-KAIYRWLLSDYVKVSNISADdm 84
Cdd:COG0491    31 TGLGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEaEALEAPAAGALFGREPVPPD-- 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600  85 lytetdleesmdkiETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGD 142
Cdd:COG0491   107 --------------RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD 149
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 1-180 8.87e-07

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: 50.48  E-value: 8.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGIHPGLEGMdalPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK-------TSFkgrtfmthaTKA 64
Cdd:cd07714    24 IIDCGLKFPDEDM---PGVDYIIPdfsyleenkDKIKGIFITHGHEDHIGALPYLLPElnvpiyaTPL---------TLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  65 IYRWLLSDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGH-VLGAAMFMIEIAGVKLLYTGDF 143
Cdd:cd07714    92 LIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHsIPDSVGLAIKTPEGTIVHTGDF 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1012443600 144 --------SRQEDRHLMaAEIPNIKPDILIIESTYGTHiHEKREE 180
Cdd:cd07714   155 kfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 1-166 4.54e-06

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: 48.70  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 ML-DCGIHPGLEGMDA--LPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---ATKAIYRWLLsDYV 74
Cdd:COG2333    24 ILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA--FPVGRVLVSgppDTSETYERLL-EAL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  75 KVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGHVLGAAM--------FMIEIAGVKLLYTGDFSRQ 146
Cdd:COG2333   101 KEKGI-----------------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSdennnslvLRLTYGGFSFLLTGDAEAE 163

                         170       180
                  ....*....|....*....|
gi 1012443600 147 EDRHLMAAEiPNIKPDILII 166
Cdd:COG2333   164 AEAALLARG-PDLKADVLKV 182
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 22-142 4.81e-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: 48.31  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALpwflqKTSFKGRTF---MTHATKAIYRWLLSDyvkvsNISADDMLYTETDLEESMDKI 98
Cdd:cd07720    87 IDPEDIDDVLLTHLHPDHIGGL-----VDAGGKPVFpnaEVHVSEAEWDFWLDD-----ANAAKAPEGAKRFFDAARDRL 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1012443600  99 ET----INFHEVKEVA-GIKFWcYHAGHVLGAAMFMIEIAGVKLLYTGD 142
Cdd:cd07720   157 RPyaaaGRFEDGDEVLpGITAV-PAPGHTPGHTGYRIESGGERLLIWGD 204
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 21-171 9.43e-06

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 47.44  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  21 LIDPAE---------------IDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHATKAIYRWLLsdyvkvsNIS 80
Cdd:cd07717    30 LFDCGEgtqrqllraglspskIDRIFITHLHGDHILGLPGLLSTMSLLGRTepltiYGPKGLKEFLETLL-------RLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  81 ADDMLYtetdleesmdkieTINFHEVKEVAGIKF-------WCYHAGHVLGAAMFMIEIaGVKLLYTGDfSRQEDRHLMA 153
Cdd:cd07717   103 ASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYRFEE-GRKIAYLGD-TRPCEGLVEL 167

                         170
                  ....*....|....*...
gi 1012443600 154 AEipniKPDILIIESTYG 171
Cdd:cd07717   168 AK----GADLLIHEATFL 181
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 1-142 9.90e-06

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: 46.28  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihPGlegmdALPYI-DLIDPAEIDLLLISHFHLDHCGALPWFLqktsfkgrtfmthatkaiYRWLLSDYVKVSNI 79
Cdd:cd07716    31 LLDCG--SG-----VLSRLqRYIDPEDLDAVVLSHLHPDHCADLGVLQ------------------YARRYHPRGARKPP 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  80 -------SADDMLYTETDLEESMDkIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGD 142
Cdd:cd07716    86 lplygpaGPAERLAALYGLEDVFD-FHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGD 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-170 1.75e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.81  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihPGL-EGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG-RTFMTHATKAiyrwllsdyvkvsn 78
Cdd:COG1235    48 LIDAG--PDLrEQLLRLG----LDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLE-------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  79 iSADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCY---H-AGHVLGaamFMIEIAGVKLLYTGDFSrqedrHLMAA 154
Cdd:COG1235   108 -ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFpvpHdAGDPVG---YRIEDGGKKLAYATDTG-----YIPEE 178

                         170
                  ....*....|....*..
gi 1012443600 155 EIPNIK-PDILIIESTY 170
Cdd:COG1235   179 VLELLRgADLLILDATY 195
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
22-108 2.98e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 46.03  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALPWFLQKTsfKGRTFMTHatKAIYRWLLSDYVKVSNISaddMLYTETDLEESMDkieti 101
Cdd:COG1237    53 IDLSDIDAVVLSHGHYDHTGGLPALLELN--PKAPVYAH--PDAFEKRYSKRPGGKYIG---IPFSREELEKLGA----- 120


                  ....*..
gi 1012443600 102 NFHEVKE 108
Cdd:COG1237   121 RLILVKE 127
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 22-51 5.10e-05

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: 45.31  E-value: 5.10e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALPWFLQKTS 51
Cdd:cd07713    51 IDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 22-50 1.23e-04

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 44.13  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGAL------PWFLQKT 50
Cdd:cd07729    84 LDPEDIDYVILSHLHFDHAGGLdlfpnaTIIVQRA 118
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-46 3.53e-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: 3.53e-04
                          10        20
                  ....*....|....*....|....*
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALPWF 46
Cdd:cd07730    79 IDPEDIDAVILSHLHWDHIGGLSDF 103
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-56 2.23e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 40.55  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600   1 MLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 56
Cdd:PRK00055   33 LFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-49 4.34e-03

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 40.05  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600   1 MLDCGI-HPGlegmDALPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK 49
Cdd:COG0595    32 IVDCGLkFPE----DEMPGVDLVIPdisyleenkDKIKGIVLTHGHEDHIGALPYLLKE 86
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-41 4.62e-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) 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: 39.10  E-value: 4.62e-03
                          10        20
                  ....*....|....*....|
gi 1012443600  22 IDPAEIDLLLISHFHLDHCG 41
Cdd:cd07741    49 LDPTKLDAIILSHRHLDHSN 68
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 27-170 4.81e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 38.83  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  27 IDLLLISHFHLDHCGALPwFLQktsfKGRTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESM---DKIETINF 103
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLL-DLR----EGRPRPLYAPLGVLAHLRRNFPYLFLLEHYGVRVHEIDWGESFtvgDGGLTVTA 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600 104 HEVKEVAGIKFWcYHAGHVLGaamFMIEIAGVKLLYTGD---FSRQEDRHLMAAeipnikpDILIIESTY 170
Cdd:pfam12706 104 TPARHGSPRGLD-PNPGDTLG---FRIEGPGKRVYYAGDtgyFPDEIGERLGGA-------DLLLLDGGA 162
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 22-56 4.90e-03

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: 39.51  E-value: 4.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1012443600  22 IDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 56
Cdd:TIGR02651  47 ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 21-46 5.15e-03

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 38.43  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 1012443600  21 LIDPAEIDLLLISHFHLDHCGALPWF 46
Cdd:cd07725    50 GLKPSDIDRVLLTHHHPDHIGLAGKL 75
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-142 6.57e-03

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: 38.63  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012443600  10 LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---------------ATKAIYRWLlsdyv 74
Cdd:cd07726    42 LAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEA--LPNAKVYVHprgarhlidpsklwaSARAVYGDE----- 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012443600  75 kvsnisADDMLYTETDLEEsmDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGD 142
Cdd:cd07726   111 ------ADRLGGEILPVPE--ERVIVLEDGETLDLGGRTLEVIDTpGHAPHHLSFLDEESDG--LFTGD 169
 
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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