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Conserved domains on  [gi|341940395|sp|Q9QXK7|]
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RecName: Full=Cleavage and polyadenylation specificity factor subunit 3; AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit; Short=CPSF 73 kDa subunit; Short=mRNA 3'-end-processing endonuclease CPSF-73

Protein Classification

CPSF3/YSH1 family MBL fold metallo-hydrolase( domain architecture ID 11611285)

CPSF3/YSH1 family MBL fold metallo-hydrolase 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

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0031124|GO:0046872|GO:0004534|GO:0003723|GO:0004521
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 12-205 8.05e-148

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


:

Pssm-ID: 293850  Cd Length: 194  Bit Score: 427.00  E-value: 8.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292   81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 341940395 172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292  161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 2.54e-120

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 364.89  E-value: 2.54e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236    3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236   80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236  160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236  239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 330 GMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236  311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                        410
                 ....*....|....
gi 341940395 409 LKPP-HVILVHGEQ 421
Cdd:COG1236  390 TGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 2.45e-89

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


:

Pssm-ID: 463330  Cd Length: 204  Bit Score: 277.08  E-value: 2.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFYLLYYQLQKLTGDVEELEIQEK-PALKVFKSITVV 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940395  634 VLSVTVDGKTANINLETRAVECEegsedDESLREMVELAAQRLYEALTP 682
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 12-205 8.05e-148

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


Pssm-ID: 293850  Cd Length: 194  Bit Score: 427.00  E-value: 8.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292   81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 341940395 172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292  161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 2.54e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 364.89  E-value: 2.54e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236    3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236   80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236  160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236  239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 330 GMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236  311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                        410
                 ....*....|....
gi 341940395 409 LKPP-HVILVHGEQ 421
Cdd:COG1236  390 TGKPeRVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 2.45e-89

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


Pssm-ID: 463330  Cd Length: 204  Bit Score: 277.08  E-value: 2.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFYLLYYQLQKLTGDVEELEIQEK-PALKVFKSITVV 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940395  634 VLSVTVDGKTANINLETRAVECEegsedDESLREMVELAAQRLYEALTP 682
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 477-683 2.42e-63

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


Pssm-ID: 215023  Cd Length: 212  Bit Score: 209.19  E-value: 2.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   477 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFYLLYYQLQKLT---GDVEELEIQEKPALKV 550
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   551 FKSITVVQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCV 627
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940395   628 SVKDDSVLSVTVDGKTANINLETRAVECeegsEDDESLREMVELAAQRLYEALTPV 683
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 246-367 1.51e-44

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: 155.39  E-value: 1.51e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 320
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 341940395   321 GPSVVMASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 367
Cdd:smart01027  80 GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 246-365 2.58e-34

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: 126.09  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 325
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 341940395  326 MASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 365
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
26-218 3.37e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.56  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 99
Cdd:COG1234   20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 100 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 174
Cdd:COG1234   94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 341940395 175 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 218
Cdd:COG1234  154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-195 5.12e-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: 76.44  E-value: 5.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395    26 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   106 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 184
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 341940395   185 DRHLMAAEIPN 195
Cdd:smart00849 142 GDGRTLVDGGD 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-195 6.47e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 6.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 105
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  106 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 341940395  186 RHLMAAEIPN 195
Cdd:pfam00753 156 IGRLDLPLGG 165
PRK00055 PRK00055
ribonuclease Z; Reviewed
 26-93 1.22e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940395  26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:PRK00055  21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 26-93 6.04e-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: 6.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940395   26 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:TIGR02651  19 PSIALKLNGELWLFDCG-----EGtqrqmLRSG-----ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 12-205 8.05e-148

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


Pssm-ID: 293850  Cd Length: 194  Bit Score: 427.00  E-value: 8.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  12 LLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKG 91
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  92 RTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAG 171
Cdd:cd16292   81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 341940395 172 VKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16292  161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-421 2.54e-120

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 364.89  E-value: 2.54e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYidLIDPAEIDLLLISHFHLDHCGALPWfLQKTSFKGRT 93
Cdd:COG1236    3 LTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPF--PFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  94 FMTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:COG1236   80 YATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVGGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 173 KLLYTGDFSRQEDRHLMAAEIPNiKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLI 252
Cdd:COG1236  160 RIVFSGDYGREDDPLLAPPEPVP-PADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELLYL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 253 LDEYWQNHpELHDIPIyYASSLAKKCMAVYQTYVNAMNDKIRkqininNPFVFKHISNLKSMDH---FDDIGPSVVMASP 329
Cdd:COG1236  239 LRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEEskaLNRKGPAIIIAPS 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 330 GMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSVD-YISFSAHTDYQQTSEFIRA 408
Cdd:COG1236  311 GMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWIKA 389

                        410
                 ....*....|....
gi 341940395 409 LKPP-HVILVHGEQ 421
Cdd:COG1236  390 TGKPeRVFLVHGEP 403
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 17-456 8.61e-119

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: 362.91  E-value: 8.61e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  17 LGAGQEVGRSCIILEFKGRKIMLDCGIHPG-----LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPwFLQKTSFKG 91
Cdd:COG1782    6 LGAAREVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKYGYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  92 RTFMTHATKAIYRWLLSDYVKV-------------SNISADDMLYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAG 157
Cdd:COG1782   81 PIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTFYNAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 158 HVLGAAMFMIEIAG--VKLLYTGDFSRQEDRhLM--AAEIPNIkpDILIIESTYGTHIHEKREEREARFCNTVHDIVNRG 233
Cdd:COG1782  161 HILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLrpPTPFPRA--DTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 234 GRGLIPVFALGRAQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININ-NPFVFKHISNLK 312
Cdd:COG1782  238 GKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHYVE 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 313 SMDHFDDI----GPSVVMASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEItTMSGQKLPLKMSV 388
Cdd:COG1782  317 SVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRAEV 395

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940395 389 DYI-SFSAHTDYQQTSEFIRAL--KPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNPRNTEAVTL 456
Cdd:COG1782  396 ETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL------GIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 15-205 1.06e-92

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 285.38  E-value: 1.06e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  15 RPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTF 94
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  95 MTHATKAIYRWLLSDYVKVSNISADDM-LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:cd07734   81 ATHPTVALGRLLLEDYVKSAERIGQDQsLYTPEDIEEALKHIVPLGYGQSIDLFpALSLTAYNAGHVLGAAMWEIQIYGE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 341940395 173 KLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd07734  161 KLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 479-682 2.45e-89

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


Pssm-ID: 463330  Cd Length: 204  Bit Score: 277.08  E-value: 2.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  479 QRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFYLLYYQLQKLTGDVEELEIQEK-PALKVFKSITVV 557
Cdd:pfam11718   1 QLVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQMFGDVEELEDKEGkPTLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  558 QEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCVS-VKDDS 633
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPasvKLSELPLRNPHAESDPEERIERLIMLLEAQFGEDCVIeLPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940395  634 VLSVTVDGKTANINLETRAVECEegsedDESLREMVELAAQRLYEALTP 682
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVECE-----DEVLKDRVETVVERAVEAVAP 204
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 14-205 1.54e-70

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


Pssm-ID: 293849  Cd Length: 199  Bit Score: 227.91  E-value: 1.54e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAE-----IDLLLISHFHLDHCGALPWFLQKTS 88
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGpftehIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  89 FKGRTFMTHATKAIYRWLLSDYVKVS-NISADDMLYTETDLEESMDKIETINFHEVKEV-AGIKFWCYHAGHVLGAAMFM 166
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341940395 167 IEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIES 205
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 477-683 2.42e-63

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


Pssm-ID: 215023  Cd Length: 212  Bit Score: 209.19  E-value: 2.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   477 QGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYT---GPFYLLYYQLQKLT---GDVEELEIQEKPALKV 550
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPssaSLLLVLLELMFEFGfveEDVDEEEKKEKAALIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   551 FKSITVVQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNP---KIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCV 627
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPspaKVKSSSKSKHHHHNDEEFREKLIEILLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940395   628 SVKDDSVLSVTVDGKTANINLETRAVECeegsEDDESLREMVELAAQRLYEALTPV 683
Cdd:smart01098 161 NVEEGEDLKVTVDGKTANIDLETLKVVE----EDDESLVERLEELLERIRLTLLPI 212
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 14-205 1.33e-62

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 206.93  E-value: 1.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL-IDPAEIDLLLISHFHLDHCGALPwFLQKTSFKGR 92
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  93 TFMTHATKAIYRWLLSDYVKVSNISADDM----LYTETDLEESMDKIETINFHEVKEVA-GIKFWCYHAGHVLGAAMFMI 167
Cdd:cd16295   80 IYATPATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIGpGVKVTFYDAGHILGSASVEL 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341940395 168 EI-AGVKLLYTGDFSRQEDRhLMAAEIPNIKPDILIIES 205
Cdd:cd16295  160 EIgGGKRILFSGDLGRKNTP-LLRDPAPPPEADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 246-367 1.51e-44

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: 155.39  E-value: 1.51e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQINI-NNPFVFKHISNLKSMDHFDDI---- 320
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 341940395   321 GPSVVMASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHI 367
Cdd:smart01027  80 GPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 246-365 2.58e-34

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: 126.09  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  246 AQELLLILDEYWQNHpELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQIninnpfvfkhISNLKSMDHFDDIGPSVV 325
Cdd:pfam10996   1 AQELLYLLDELWREG-RLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV----------ISKSESKAINEGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 341940395  326 MASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAK 365
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
26-218 3.37e-19

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 87.56  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMTHAT 99
Cdd:COG1234   20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREkpltiYGPPGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 100 KAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVK-----EVAGIKFWCYHAGHVLGAAMFMIEIAGVKL 174
Cdd:COG1234   94 KEFLEALL-------KASGTDLDF-------------PLEFHEIEpgevfEIGGFTVTAFPLDHPVPAYGYRFEEPGRSL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 341940395 175 LYTGDfSRqedrhLMAAEIPNIK-PDILIIESTYGTHIHEKREER 218
Cdd:COG1234  154 VYSGD-TR-----PCEALVELAKgADLLIHEATFLDEEAELAKET 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 16-205 9.34e-19

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293851  Cd Length: 199  Bit Score: 84.88  E-value: 9.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  16 PLGAGQEVGRSCIILEFKGRKIMLDCG--IHPGLEGMDALPYIdlidPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:cd16293    3 PLSGAGDESPLCYLLEIDDVTILLDCGwdESFDMEYLESLKRI----APTIDAVLLSHPDLEHLGALPYLVGKLGLTCPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  94 FMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVA----GIKFWCYHAGHVLGAAMFMIEI 169
Cdd:cd16293   79 YATLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWKITK 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341940395 170 AGVKLLYTGDFSRQEDRHLMAAEIPNI---KPDILIIES 205
Cdd:cd16293  159 DSEDIVYAVDWNHKKERHLNGAVLDSFgglRPSLLITDA 197
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-195 5.12e-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: 76.44  E-value: 5.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395    26 SCIILEFKGRKIMLDCGIHpglEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHATKaiyrw 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   106 llsDYVKVSNISADDMLYtetdLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGDFSRQE 184
Cdd:smart00849  71 ---ELLKDLLALLGELGA----EAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLP--EGKILFTGDLLFAG 141

                          170
                   ....*....|.
gi 341940395   185 DRHLMAAEIPN 195
Cdd:smart00849 142 GDGRTLVDGGD 152
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-204 1.02e-15

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 76.11  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEVGRSCIILEFKGRKIMLDCG-----------------IHPGLEGMDALPYIDLI-------DPAEIDLLLI 69
Cdd:cd07732    2 ITIHRGTNEIGGNCIEVETGGTRILLDFGlpldpeskyfdevldflELGLLPDIVGLYRDPLLlgglrseEDPSVDAVLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  70 SHFHLDHCGALPWFLQKTSFkgrtFMTHATKAIYRWLLSDYVKVSNISADdmlytetdleesmdkIETINFHEVKEVAGI 149
Cdd:cd07732   82 SHAHLDHYGLLNYLRPDIPV----YMGEATKRILKALLPFFGEGDPVPRN---------------IRVFESGKSFTIGDF 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 150 KFWCYHAGH-VLGAAMFMIEIAGVKLLYTGDF----SRQEDRHLMAAEIPNiKPDILIIE 204
Cdd:cd07732  143 TVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELTEAFVEKAPK-NIDVLLME 201
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-205 2.18e-15

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 74.61  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  14 IRPLGAGQEV-----GRSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFLQK 86
Cdd:cd16272    1 LTFLGTGGAVpsltrNTSSYLLETGGTRILLDCGegTVYRLLKAG-------VDPDKLDAIFLSHFHLDHIGGLPTLLFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  87 TSFKGRT-----FMTHATKAIYRWLLSDYVKVSnisaddmlytetDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLG 161
Cdd:cd16272   74 RRYGGRKkpltiYGPKGIKEFLEKLLNFPVEIL------------PLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVE 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 341940395 162 AAMFMIEIAGVKLLYTGDfsrqedrhlmAAEIPNIKP-----DILIIES 205
Cdd:cd16272  142 SLGYRIEAEGKSIVYSGD----------TGPCENLVElakgaDLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-195 6.47e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 6.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLiDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRW 105
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  106 LLSDYVKVSNISAddmlytetdLEESMDKIETINFHEVkEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:pfam00753  86 LGLAASRLGLPGP---------PVVPLPPDVVLEEGDG-ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|
gi 341940395  186 RHLMAAEIPN 195
Cdd:pfam00753 156 IGRLDLPLGG 165
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 29-202 1.99e-13

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 69.16  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   29 ILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPaEIDLLLISHFHLDHCGALPWFLQKtsfKGRTFMTH----ATKAIY- 103
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSYESDLKYLEKILP-EVDLILLSHPTLEHLGAYPLLYYK---FGSHLGSNipvyATLPVAn 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  104 --RWLLSDYVKVSNISA--DDMLYTETDLEESMDKIETINFHEVKEV----AGIKFWCYHAGHVLGAAMFMIEIAGVKLL 175
Cdd:pfam16661  77 lgRVSTYDLYASRGILGpyDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkfDGLTITPYNSGHTLGGTIWKISKNSEKIV 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 341940395  176 YTGDFSRQEDRHLMAAEIPN---------IKPDILI 202
Cdd:pfam16661 157 YAVDWNHTKDSHLNGASLLDstgkpleslVRPTALI 192
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 16-217 1.43e-12

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 68.20  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  16 PLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMdalPYIDLIDP---------AEIDLLLISHFHLDHCGALPWFLQK 86
Cdd:cd07714    2 PLGGLGEIGKNMYVVEYDDDIIIIDCGLKFPDEDM---PGVDYIIPdfsyleenkDKIKGIFITHGHEDHIGALPYLLPE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  87 -------TSFkgrtfmthaTKAIYRWLLSDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGH- 158
Cdd:cd07714   79 lnvpiyaTPL---------TLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHs 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940395 159 VLGAAMFMIEIAGVKLLYTGDF--------SRQEDRHLMaAEIPNIKPDILIIESTYGTHiHEKREE 217
Cdd:cd07714  133 IPDSVGLAIKTPEGTIVHTGDFkfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 25-168 2.16e-12

integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293852 [Multi-domain]  Cd Length: 166  Bit Score: 65.59  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  25 RSCIILEFKGRKIMLDCGIhpglegmDALPYIDLIDPAEIDLLLISHFHldHCGALPWFLQKTSFKGRTFMTHATKAIYR 104
Cdd:cd16294   12 LPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGR 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940395 105 WLLSDYVkvsnisaddmlytetdleESMDKIETINFHEVKEVAG-IKFWCYHAGHVLGAAMFMIE 168
Cdd:cd16294   83 LLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQ 129
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 381-448 2.31e-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: 2.31e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940395  381 KLPLKMSVDYIS-FSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYedndevHIEVHNP 448
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL------GIEVFVP 63
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 27-180 4.19e-10

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 59.61  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  27 CIILEFKGRK-IMLDcgihPGLEGMDALpyIDLID--PAEIDLLLISHFHLDHCGALPWFLQKTSFKgrtfmTHATKAIY 103
Cdd:cd06262   12 CYLVSDEEGEaILID----PGAGALEKI--LEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAP-----VYIHEADA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940395 104 RWLLSDyvkvsnisADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEIAGVklLYTGDF 180
Cdd:cd06262   81 ELLEDP--------ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEGV--LFTGDT 148
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 4-207 4.34e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 60.68  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   4 IPAEESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGihPGL-EGMDALPyidlIDPAEIDLLLISHFHLDHCGALPW 82
Cdd:COG1235   14 VPQIGCDCPVCASTDPRYGRTRSSILVEADGTRLLIDAG--PDLrEQLLRLG----LDPSKIDAILLTHEHADHIAGLDD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  83 FLQKTSFKG-RTFMTHATKAiyrwllsdyvkvsniSADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCY---H-AG 157
Cdd:COG1235   88 LRPRYGPNPiPVYATPGTLE---------------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFpvpHdAG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 341940395 158 HVLGaamFMIEIAGVKLLYTGDFSrqedrHLMAAEIPNIK-PDILIIESTY 207
Cdd:COG1235  153 DPVG---YRIEDGGKKLAYATDTG-----YIPEEVLELLRgADLLILDATY 195
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 26-208 8.52e-10

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 59.77  E-value: 8.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT-----FMT 96
Cdd:cd07717   18 SSIALRLEGELWLFDCG-----EGtqrqLLRAG----LSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTepltiYGP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  97 HATKAIYRWLLsdyvkvsNISADDMLYtetdleesmdkieTINFHEVKEVAGIKF-------WCYHAGHVLGAAMFMIEI 169
Cdd:cd07717   89 KGLKEFLETLL-------RLSASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYRFEE 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341940395 170 aGVKLLYTGDfSRQEDRHLMAAEipniKPDILIIESTYG 208
Cdd:cd07717  149 -GRKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
10-86 7.28e-09

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 58.92  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  10 DQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGI-HPGlegmDALPYIDLIDP---------AEIDLLLISHFHLDHCGA 79
Cdd:COG0595    4 DKLRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLkFPE----DEMPGVDLVIPdisyleenkDKIKGIVLTHGHEDHIGA 79


                 ....*..
gi 341940395  80 LPWFLQK 86
Cdd:COG0595   80 LPYLLKE 86
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-84 1.06e-08

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 55.73  E-value: 1.06e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940395  17 LGAGQEVG-----RSCIILEFKGRKIMLDCG--IHPGLEGMDalpyidlIDPAEIDLLLISHFHLDHCGALPWFL 84
Cdd:cd07740    3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 23-203 1.11e-08

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 56.40  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  23 VGR-SCIILEFKGRKIML-DCGIHPGLEGMDA--LPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH- 97
Cdd:COG2333    8 VGQgDAILIRTPDGKTILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEA--FPVGRVLVSg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  98 --ATKAIYRWLLsDYVKVSNIsaddmlytetdleesmdKIETINFHEVKEVAGIKFWCYHAGHVLGAAM--------FMI 167
Cdd:COG2333   86 ppDTSETYERLL-EALKEKGI-----------------PVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSdennnslvLRL 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 341940395 168 EIAGVKLLYTGDFSRQEDRHLMAAEiPNIKPDILII 203
Cdd:COG2333  148 TYGGFSFLLTGDAEAEAEAALLARG-PDLKADVLKV 182
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 23-217 1.98e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 55.31  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  23 VGRSCIILEFKGRKIMLDcgihPGLEGMDALPYIDLIDPAE---IDLLLISHFHLDHCGalpwflqktsfkgrtfmthat 99
Cdd:COG2220    9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLDPEDlpkIDAVLVTHDHYDHLD--------------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 100 KAIYRWLLSDYVKV-SNISADDMLytetdLEESMDKIETINFHEVKEVAGIKFWCYHAGH--------VLGAAMFMIEIA 170
Cdd:COG2220   64 DATLRALKRTGATVvAPLGVAAWL-----RAWGFPRVTELDWGESVELGGLTVTAVPARHssgrpdrnGGLWVGFVIETD 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 341940395 171 GVKLLYTGD------FSRQEDRHlmaaeipniKPDILIIEsTYGTHIHEKREE 217
Cdd:COG2220  139 GKTIYHAGDtgyfpeMKEIGERF---------PIDVALLP-IGAYPFTMGPEE 181
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 26-179 2.80e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 53.99  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGihPGlegmdALPYI-DLIDPAEIDLLLISHFHLDHCGALPWFLqktsfkgrtfmthatkaiYR 104
Cdd:cd07716   19 SGYLLEADGFRILLDCG--SG-----VLSRLqRYIDPEDLDAVVLSHLHPDHCADLGVLQ------------------YA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 105 WLLSDYVKVSNI-------SADDMLYTETDLEESMDkIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYT 177
Cdd:cd07716   74 RRYHPRGARKPPlplygpaGPAERLAALYGLEDVFD-FHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYT 152


                 ..
gi 341940395 178 GD 179
Cdd:cd07716  153 GD 154
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-179 1.06e-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: 53.16  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  27 CIILEFKGRKIMLDcgihPGLEGMDALPYIDLID--PAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTHAT-KAIY 103
Cdd:COG0491   17 SYLIVGGDGAVLID----TGLGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEA--FGAPVYAHAAEaEALE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940395 104 RWLLSDYVKVSNISADdmlytetdleesmdkiETINFHEVKEVAGIKFWCYHA-GHVLGAAMFMIEiaGVKLLYTGD 179
Cdd:COG0491   91 APAAGALFGREPVPPD----------------RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD 149
PRK00055 PRK00055
ribonuclease Z; Reviewed
 26-93 1.22e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 53.65  E-value: 1.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940395  26 SCIILEFKGRKIMLDCGihpglEG----MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:PRK00055  21 SSILLRLGGELFLFDCG-----EGtqrqLLKTG----IKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRT 83
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 27-88 2.07e-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: 2.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940395  27 CIILEFKGRKIMLDCGIHPGLEG-MDALPyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTS 88
Cdd:cd07713   22 SLLIETEGKKILFDTGQSGVLLHnAKKLG----IDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
27-145 5.09e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 5.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  27 CIILEFKGRKIMLDCGiHPG--LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKTsfKGRTFMTHatKAIYR 104
Cdd:COG1237   24 SALIETEGKRILFDTG-QSDvlLKNAEKL----GIDLSDIDAVVLSHGHYDHTGGLPALLELN--PKAPVYAH--PDAFE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 341940395 105 WLLSDYVKVSNISaddMLYTETDLEESMDkietiNFHEVKE 145
Cdd:COG1237   95 KRYSKRPGGKYIG---IPFSREELEKLGA-----RLILVKE 127
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 26-87 2.52e-06

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 49.14  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGIHPGLEGMDALPYIDL------------------IDPAEIDLLLISHFHLDHCGAL------P 81
Cdd:cd07729   33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGLdlfpnaT 112


                 ....*.
gi 341940395  82 WFLQKT 87
Cdd:cd07729  113 IIVQRA 118
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 3-179 4.54e-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: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   3 AIPAEESDQLLIRPLGAGQ-EVGRSCIILEFKGRKIMLD--CGIHPG------LEGMDALPYidliDPAEIDLLLISHFH 73
Cdd:cd07720   26 GAAPEAEAALLAAFLPPDPvETSVNAFLVRTGGRLILVDtgAGGLFGptagklLANLAAAGI----DPEDIDDVLLTHLH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  74 LDHCGALpwflqKTSFKGRTF---MTHATKAIYRWLLSDyvkvsNISADDMLYTETDLEESMDKIET----INFHEVKEV 146
Cdd:cd07720  102 PDHIGGL-----VDAGGKPVFpnaEVHVSEAEWDFWLDD-----ANAAKAPEGAKRFFDAARDRLRPyaaaGRFEDGDEV 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 341940395 147 A-GIKFWcYHAGHVLGAAMFMIEIAGVKLLYTGD 179
Cdd:cd07720  172 LpGITAV-PAPGHTPGHTGYRIESGGERLLIWGD 204
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 26-93 6.04e-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: 6.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940395   26 SCIILEFKGRKIMLDCGihpglEG-----MDALpyidlIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRT 93
Cdd:TIGR02651  19 PSIALKLNGELWLFDCG-----EGtqrqmLRSG-----ISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 26-207 1.05e-04

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


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 44.02  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCG--IHP-GLEGMDALPyidlidPAEIDLLLiSHFHLDH-CGaLPWF--LQKTSFKGRTFMTHAT 99
Cdd:cd07715   24 SCVEVRAGGELLILDAGtgIRElGNELMKEGP------PGEAHLLL-SHTHWDHiQG-FPFFapAYDPGNRIHIYGPHKD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 100 KAIYRWLLSDYVKVSN--ISADDMLytetdleesmdkiETINFHEVKE-----VAGIKFWCYHAGHVLGAAMFMIEIAGV 172
Cdd:cd07715   96 GGSLEEVLRRQMSPPYfpVPLEELL-------------AAIEFHDLEPgepfsIGGVTVTTIPLNHPGGALGYRIEEDGK 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 341940395 173 KLLYTGDFsrqEDRHLMAAEIPNIKP-----DILIIESTY 207
Cdd:cd07715  163 SVVYATDT---EHYPDDGESDEALLEfargaDLLIHDAQY 199
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 26-81 1.29e-04

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 43.27  E-value: 1.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940395  26 SCIILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCGALP 81
Cdd:cd07719   19 PSTLVVVGGRVYLVDAG--SGvVRRLAQAG----LPLGDLDAVFLTHLHSDHVADLP 69
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-179 1.32e-04

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 43.64  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDCGIHPG----LEGMDALpyidLIDPAEIDLLLISHFHLDHCGALPWFLQKtsFKGRTFMTH---- 97
Cdd:cd07726   17 ASYLLDGEGRPALIDTGPSSSvprlLAALEAL----GIAPEDVDYIILTHIHLDHAGGAGLLAEA--LPNAKVYVHprga 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  98 -----------ATKAIYRWLlsdyvkvsnisADDMLYTETDLEEsmDKIETINFHEVKEVAGIKFWCYHA-GHVLGAAMF 165
Cdd:cd07726   91 rhlidpsklwaSARAVYGDE-----------ADRLGGEILPVPE--ERVIVLEDGETLDLGGRTLEVIDTpGHAPHHLSF 157

                        170
                 ....*....|....
gi 341940395 166 MIEIAGVklLYTGD 179
Cdd:cd07726  158 LDEESDG--LFTGD 169
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 27-203 1.49e-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: 42.89  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  27 CIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKtsfkgrtfmthatkaiyrwl 106
Cdd:cd07731   12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKN-------------------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 107 lsdyVKVSNISADDMLYTETDLEESMDKIET--INFHEVK-----EVAGIKFWCYHAGHVLGAAM------FMIEIAGVK 173
Cdd:cd07731   72 ----FPVKEVYMPGVTHTTKTYEDLLDAIKEkgIPVTPCKagdrwQLGGVSFEVLSPPKDDYDDLnnnscvLRLTYGGTS 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 341940395 174 LLYTGDFSRQEDRHLMAAEiPNIKPDILII 203
Cdd:cd07731  148 FLLTGDAEKEAEEELLASG-PDLLADVLKV 176
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-78 1.69e-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: 1.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 341940395  28 IILEFKGRKIMLDCGihPG-LEGMDALPyidlIDPAEIDLLLISHFHLDHCG 78
Cdd:cd07741   23 IWIELNGKNIHIDPG--PGaLVRMCRPK----LDPTKLDAIILSHRHLDHSN 68
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-83 3.79e-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: 3.79e-04
                         10        20
                 ....*....|....*....|....*
gi 341940395  59 IDPAEIDLLLISHFHLDHCGALPWF 83
Cdd:cd07730   79 IDPEDIDAVILSHLHWDHIGGLSDF 103
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-78 6.97e-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: 6.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940395  29 ILEFKGRKIMLDCGI-----HPGLEGMDAL--PYID-L----IDPAEIDLLLISHFHLDHCG 78
Cdd:cd16277   17 LVRTPGRTILVDTGIgndkpRPGPPAFHNLntPYLErLaaagVRPEDVDYVLCTHLHVDHVG 78
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 35-81 8.58e-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: 8.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 341940395  35 RKIMLDCGihpglEGMDalPYIDLI-------DPAEIDLLLISHFHLDHCGALP 81
Cdd:cd07722   28 RRILIDTG-----EGRP--SYIPLLksvldseGNATISDILLTHWHHDHVGGLP 74
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 35-207 1.24e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 40.76  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395   35 RKIMLDCGihPGLEGMDAL---PYIDLIDPaeIDLLLISHFHLDHCGALPwFLQktsfKGRTFMTHATKAIYRWLLSDYV 111
Cdd:pfam12706   1 RRILIDPG--PDLRQQALPalqPGRLRDDP--IDAVLLTHDHYDHLAGLL-DLR----EGRPRPLYAPLGVLAHLRRNFP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  112 KVSNISADDMLYTETDLEESM---DKIETINFHEVKEVAGIKFWcYHAGHVLGaamFMIEIAGVKLLYTGD---FSRQED 185
Cdd:pfam12706  72 YLFLLEHYGVRVHEIDWGESFtvgDGGLTVTATPARHGSPRGLD-PNPGDTLG---FRIEGPGKRVYYAGDtgyFPDEIG 147

                         170       180
                  ....*....|....*....|..
gi 341940395  186 RHLMAAeipnikpDILIIESTY 207
Cdd:pfam12706 148 ERLGGA-------DLLLLDGGA 162
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 26-187 1.29e-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: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  26 SCIILEFKGRKIMLDcgihPGLEGMDALPYIDlIDPAEIDLLLISHFHLDHCGAlpwFLQKTSFKGRTFMtHATKAIYRW 105
Cdd:cd07738   16 SGFIIWINGRGIMVD----PPVNSTSYLRQNG-ISPRLVDHVILTHCHADHDAG---TFQKILEEEKITL-YTTRTINES 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395 106 LLSDYVKVSNISADdmlytetDLEESMDKIETINFHEVKeVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQED 185
Cdd:cd07738   87 FLRKYAALTGLPPD-------FLEELFDFRPVIIGEKTK-INGAEFEFDYSFHSIPTIRFKVSYGGKSIAYSGDTRYDPD 158


                 ..
gi 341940395 186 RH 187
Cdd:cd07738  159 GL 160
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-179 4.22e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 39.40  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  27 CIILEFKGRKIMLDCGI----------HPGLEG----MDALPYIDLiDPAEIDLLLISHFHLDHC-GALPWF---LQKTS 88
Cdd:cd16281   45 CLLIETGGRNILIDTGIgdkqdpkfrsIYVQHSehslLKSLARLGL-SPEDITDVILTHLHFDHCgGATRADddgLVELL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  89 FKGRTFMTHatKAIYRWLLSDYV--KVSNISADDMLytetdLEESmDKIETINFHEVKEVAGIKFWCYHaGHVLGAAMFM 166
Cdd:cd16281  124 FPNATYWVQ--KRHWEWALNPNPreRASFLPENIEP-----LEES-GRLKLIDGSDAELGPGIRFHLSD-GHTPGQMLPE 194

                        170
                 ....*....|...
gi 341940395 167 IEIAGVKLLYTGD 179
Cdd:cd16281  195 ISTPGGTVVFAAD 207
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 58-83 5.70e-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: 5.70e-03
                         10        20
                 ....*....|....*....|....*.
gi 341940395  58 LIDPAEIDLLLISHFHLDHCGALPWF 83
Cdd:cd07725   50 GLKPSDIDRVLLTHHHPDHIGLAGKL 75
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 28-179 6.42e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 38.78  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  28 IILEFKGRKIMLDCGIHPGL--------EGMDALPYI--DL----IDPAEIDLLLISHFHLDHCGALpwflqkTSFKGRT 93
Cdd:cd07728   46 ILIQYQGKNYLIDAGIGNGKltekqkrnFGVTEESSIeeSLaelgLTPEDIDYVLMTHLHFDHASGL------TKVKGEQ 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940395  94 FM------THATKAIyRWllsDYVKVSNISAddmlyTETDLEESMDKIE--TINF-HEVKEVAGIKFWcyH-AGHVLGAA 163
Cdd:cd07728  120 LVsvfpnaTIYVSEI-EW---EEMRNPNIRS-----KNTYWKENWEPIEdqVKTFsDEIEIVPGITMI--HtGGHSDGHS 188

                        170
                 ....*....|....*.
gi 341940395 164 MFMIEIAGVKLLYTGD 179
Cdd:cd07728  189 IIEIEQGGETAIHMAD 204
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 27-87 7.23e-03

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 38.36  E-value: 7.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940395  27 CIILEFKGRKIMLDCGIhPG-----LEGMDALPYidliDPAEIDLLLISHFHLDHCGALPWFLQKT 87
Cdd:cd07721   13 AYLIEDDDGLTLIDTGL-PGsakriLKALRELGL----SPKDIRRILLTHGHIDHIGSLAALKEAP 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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