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Conserved domains on  [gi|24648013|ref|NP_650738|]
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cleavage and polyadenylation specificity factor 73 [Drosophila melanogaster]

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; ...
 18-211 3.62e-144

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


:

Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.62e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  18 LQIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKG 97
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQMLYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIAG 177
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 24648013 178 IKILYTGDFSRQEDRHLMAAEVPPMKPDVLITES 211
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 19-427 7.85e-121

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.05  E-value: 7.85e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  19 QIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLsgmDALPYVDL-IEADEIDLLFISHFHLDHCGALPWfLMKTSFKG 97
Cdd:COG1236   2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG---KERNWPPFpFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQM-LYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIA 176
Cdd:COG1236  78 PIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 177 GIKILYTGDFSRQEDRhLMAAEVPPMKPDVLITESTYGTHIHEKREDRENRFTSLVQKIVQQGGRCLIPVFALGRAQELL 256
Cdd:COG1236 158 GKRIVFSGDYGREDDP-LLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 257 LILDEFWSQNpDLHEIPIyYASSLAKKCMAVYQTYINAMNDRIRrqiavnNPFVFRHISNLKGIDHFEDI---GPCVIMA 333
Cdd:COG1236 237 YLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEESKALnrkGPAIIIA 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 334 SPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAVLSEPEEItTLSGQKLPLNMSVD-YISFSAHTDYQQTSEFI 412
Cdd:COG1236 309 PSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWI 387

                       410
                ....*....|....*.
gi 24648013 413 R-LLKPTHVVLVHGEQ 427
Cdd:COG1236 388 KaTGKPERVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-680 5.06e-64

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: 210.82  E-value: 5.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   486 KLSGVLVKRDFKYHLLAPSDLGKYTDMSMSVVTQRQSIPWGSSLSTLELLLDRIgAGCVEVLEAERK---LRVFGCIELT 562
Cdd:pfam11718   2 LVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQM-FGDVEELEDKEGkptLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   563 VEQKIIVMEWQATHVNDVYADAVLACIMQSELGGTNLKGATKQ-----TKSEDSRFRECLIETLQDTFGDNCVPKMFEGD 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPASVKLSELPlrnphAESDPEERIERLIMLLEAQFGEDCVIELPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24648013   638 LLPVTVSGKRAEINLETLAISCaEDDVLRQMLNTTVQKLHQTL 680
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVEC-EDEVLKDRVETVVERAVEAV 202
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 18-211 3.62e-144

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


Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.62e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  18 LQIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKG 97
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQMLYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIAG 177
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 24648013 178 IKILYTGDFSRQEDRHLMAAEVPPMKPDVLITES 211
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 19-427 7.85e-121

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.05  E-value: 7.85e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  19 QIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLsgmDALPYVDL-IEADEIDLLFISHFHLDHCGALPWfLMKTSFKG 97
Cdd:COG1236   2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG---KERNWPPFpFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQM-LYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIA 176
Cdd:COG1236  78 PIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 177 GIKILYTGDFSRQEDRhLMAAEVPPMKPDVLITESTYGTHIHEKREDRENRFTSLVQKIVQQGGRCLIPVFALGRAQELL 256
Cdd:COG1236 158 GKRIVFSGDYGREDDP-LLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 257 LILDEFWSQNpDLHEIPIyYASSLAKKCMAVYQTYINAMNDRIRrqiavnNPFVFRHISNLKGIDHFEDI---GPCVIMA 333
Cdd:COG1236 237 YLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEESKALnrkGPAIIIA 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 334 SPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAVLSEPEEItTLSGQKLPLNMSVD-YISFSAHTDYQQTSEFI 412
Cdd:COG1236 309 PSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWI 387

                       410
                ....*....|....*.
gi 24648013 413 R-LLKPTHVVLVHGEQ 427
Cdd:COG1236 388 KaTGKPERVFLVHGEP 403
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-680 5.06e-64

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: 210.82  E-value: 5.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   486 KLSGVLVKRDFKYHLLAPSDLGKYTDMSMSVVTQRQSIPWGSSLSTLELLLDRIgAGCVEVLEAERK---LRVFGCIELT 562
Cdd:pfam11718   2 LVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQM-FGDVEELEDKEGkptLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   563 VEQKIIVMEWQATHVNDVYADAVLACIMQSELGGTNLKGATKQ-----TKSEDSRFRECLIETLQDTFGDNCVPKMFEGD 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPASVKLSELPlrnphAESDPEERIERLIMLLEAQFGEDCVIELPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24648013   638 LLPVTVSGKRAEINLETLAISCaEDDVLRQMLNTTVQKLHQTL 680
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVEC-EDEVLKDRVETVVERAVEAV 202
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 483-683 9.50e-55

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: 186.46  E-value: 9.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    483 VGSKLSGVLVKRDFKYHLLAPSDLGKYTDMSMSVVTQRQSIPWGSSLSTLE---LLLDRIGAGCVEVLEAERK----LRV 555
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPSSASLLLvllELMFEFGFVEEDVDEEEKKekaaLIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    556 FGCIELTVEQKIIVMEWQATHVNDVYADAVLACIMQSELGGTNLKG----ATKQTKSEDSRFRECLIE-TLQDTFGDNCV 630
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPSPAKVksssKSKHHHHNDEEFREKLIEiLLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24648013    631 pKMFEGDLLPVTVSGKRAEINLETLAISCAEDDVLRQMLNTTVQKLHQTLVSA 683
Cdd:smart01098 161 -NVEEGEDLKVTVDGKTANIDLETLKVVEEDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 252-373 3.64e-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: 154.23  E-value: 3.64e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    252 AQELLLILDEFWSQNpDLHEIPIYYASSLAKKCMAVYQTYINAMNDRIRRQIAV-NNPFVFRHISNLKGIDHFEDI---- 326
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 24648013    327 GPCVIMASPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAV 373
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 ...
 252-371 3.70e-37

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: 134.18  E-value: 3.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   252 AQELLLILDEFWSQNPdLHEIPIYYASSLAKKCMAVYQTYINAMNDRIRRQIavnnpfvfRHISNLKGIDhfEDIGPCVI 331
Cdd:pfam10996   1 AQELLYLLDELWREGR-LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV--------ISKSESKAIN--EGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 24648013   332 MASPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAK 371
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
32-224 9.32e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 74.46  E-value: 9.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  32 SCIMLEFKGKKIMLDCGihPG-LSGMDALPyvdlIEADEIDLLFISHFHLDHCGALPWFLMKTSFKGR-----CFMTHAT 105
Cdd:COG1234  20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGRekpltIYGPPGT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 106 KAIYRWMLSDYIKISNISTEqmlyteadleasmekIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIAGIKILYTGD 185
Cdd:COG1234  94 KEFLEALLKASGTDLDFPLE---------------FHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24648013 186 FSRQEDRHLMAAEVppmkpDVLITESTYGTHIHEKREDR 224
Cdd:COG1234 159 TRPCEALVELAKGA-----DLLIHEATFLDEEAELAKET 192
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
32-204 9.64e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.48  E-value: 9.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    32 SCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLiEADEIDLLFISHFHLDHCGALPWFLMKTSFKGRCFMTHATKAIYRW 111
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   112 MLSDYIKISNISTEqmlyteadlEASMEKIETINFHEERDVMGVRFcAYIAGHVLGAAMFMIEIAGIKILYTGDFSRQED 191
Cdd:pfam00753  86 LGLAASRLGLPGPP---------VVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|...
gi 24648013   192 RHLMAAEVPPMKP 204
Cdd:pfam00753 156 IGRLDLPLGGLLV 168
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-186 9.65e-14

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: 69.89  E-value: 9.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013     32 SCIMLEFKGKKIMLDCGIHPGlsgMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKgrcfmTHATKAIYRW 111
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA---EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAP-----VYAPEGTAEL 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648013    112 MLSDYIKISNisteqmlytEADLEASMEKIETINFHEERDVMGVRFCA-YIAGHVLGAAMFMIEIAgiKILYTGDF 186
Cdd:smart00849  73 LKDLLALLGE---------LGAEAEPAPPDRTLKDGDELDLGGGELEViHTPGHTPGSIVLYLPEG--KILFTGDL 137
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 32-98 1.55e-08

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: 56.46  E-value: 1.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648013    32 SCIMLEFKGKKIMLDCG-------IHPGLSGMDalpyvdlieadeIDLLFISHFHLDHCGALPWFLMKTSFKGR 98
Cdd:TIGR02651  19 PSIALKLNGELWLFDCGegtqrqmLRSGISPMK------------IDRIFITHLHGDHILGLPGLLSTMSFQGR 80
PRK00055 PRK00055
ribonuclease Z; Reviewed
 32-214 1.80e-08

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 55.96  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   32 SCIMLEFKGKKIMLDCG-------IHPGLSGMDalpyvdlieadeIDLLFISHFHLDHCGALPWFLMKTSFKGRcfmTHA 104
Cdd:PRK00055  21 SSILLRLGGELFLFDCGegtqrqlLKTGIKPRK------------IDKIFITHLHGDHIFGLPGLLSTRSLSGR---TEP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  105 TKAIYRWMLSDYIKISNISTEQMLY--TEADleasmeKIETINfHEERDVMGVRFCAYIA------------GHVLGAAM 170
Cdd:PRK00055  86 LTIYGPKGIKEFVETLLRASGSLGYriAEKD------KPGKLD-AEKLKALGVPPGPLFGklkrgedvtledGRIINPAD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24648013  171 FM-IEIAGIKILYTGDFSRQEDRHLMAAEVppmkpDVLITESTYG 214
Cdd:PRK00055 159 VLgPPRKGRKVAYCGDTRPCEALVELAKGA-----DLLVHEATFG 198
 
Name Accession Description Interval E-value
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 18-211 3.62e-144

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


Pssm-ID: 293850  Cd Length: 194  Bit Score: 417.76  E-value: 3.62e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  18 LQIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKG 97
Cdd:cd16292   1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLSEIDLLLITHFHLDHCGALPYFLQKTNFKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQMLYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIAG 177
Cdd:cd16292  81 RVFMTHPTKAIYKWLLSDYVRVSNISSDEMLYTETDLEASMDKIETIDFHQEVEVNGIKFTAYNAGHVLGAAMFMVEIAG 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 24648013 178 IKILYTGDFSRQEDRHLMAAEVPPMKPDVLITES 211
Cdd:cd16292 161 VRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 19-427 7.85e-121

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 366.05  E-value: 7.85e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  19 QIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLsgmDALPYVDL-IEADEIDLLFISHFHLDHCGALPWfLMKTSFKG 97
Cdd:COG1236   2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG---KERNWPPFpFRPSDVDAVVLTHAHLDHSGALPL-LVKEGFRG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  98 RCFMTHATKAIYRWMLSDYIKISNISTEQM-LYTEADLEASMEKIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIA 176
Cdd:COG1236  78 PIYATPATADLARILLGDSAKIQEEEAEAEpLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEVG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 177 GIKILYTGDFSRQEDRhLMAAEVPPMKPDVLITESTYGTHIHEKREDRENRFTSLVQKIVQQGGRCLIPVFALGRAQELL 256
Cdd:COG1236 158 GKRIVFSGDYGREDDP-LLAPPEPVPPADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQELL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 257 LILDEFWSQNpDLHEIPIyYASSLAKKCMAVYQTYINAMNDRIRrqiavnNPFVFRHISNLKGIDHFEDI---GPCVIMA 333
Cdd:COG1236 237 YLLRELKKEG-RLPDIPI-YVSGMAIRATEIYRRHGEYLRDEAQ------DPFALPNLRFVTSVEESKALnrkGPAIIIA 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 334 SPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAVLSEPEEItTLSGQKLPLNMSVD-YISFSAHTDYQQTSEFI 412
Cdd:COG1236 309 PSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEV-KIFGEEVPVRARVErLFGLSAHADWDELLEWI 387

                       410
                ....*....|....*.
gi 24648013 413 R-LLKPTHVVLVHGEQ 427
Cdd:COG1236 388 KaTGKPERVFLVHGEP 403
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 19-441 4.40e-118

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: 360.98  E-value: 4.40e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  19 QIKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPG-----LSGMDALPyvdlIEADEIDLLFISHFHLDHCGALPwFLMKT 93
Cdd:COG1782   2 RITFLGAAREVTGSCHLLETGESRILLDCGLFQGgreerERNNDAFP----FDPEELDAVVLTHAHLDHSGLLP-LLVKY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  94 SFKGRCFMTHATKAIYRWMLSDYIKI-------------SNISTEQMLYTEADLEASMEKIETINFHEERDVM-GVRFCA 159
Cdd:COG1782  77 GYRGPIYCTPPTRDLMALLLLDSAKIqeeeaeyankkrySGHPPVEPLYTEKDVEKALKHFITLDYGEVTDIApDIKLTF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 160 YIAGHVLGAAMFMIEIAG--IKILYTGDFSRQEDRhLMAAEVPPMKPDVLITESTYGTHIHEKREDRENRFTSLVQKIVQ 237
Cdd:COG1782 157 YNAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTP-LLRPPTPFPRADTLIMESTYGGRLHPSREEAEEELAKVINETIE 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 238 QGGRCLIPVFALGRAQELLLILDEFWSQNpDLHEIPIYYASSLAKKCMAVYQTYINAMNDRIRRQIAVN-NPFVFRHISN 316
Cdd:COG1782 236 RGGKVLIPAFAVGRTQEILYVLNELMREG-KIPEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLIFKGeNPFLFENLHY 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 317 LKGIDHFEDI----GPCVIMASPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAVLSEPEEItTLSGQKLPLNM 392
Cdd:COG1782 315 VESVEESKEIndsdEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEV-KIFGETIPVRA 393

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 24648013 393 SVDYI-SFSAHTDYQQTSEFIRLL--KPTHVVLVHGEQNEMSRLKLALQREY 441
Cdd:COG1782 394 EVETIdGFSGHADRNELLNWLRRLkpKPKKVFLVHGEPEAAEALASSIRKKL 445
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 21-211 9.42e-81

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: 254.56  E-value: 9.42e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  21 KPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKGRCF 100
Cdd:cd07734   1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 101 MTHATKAIYRWMLSDYIKISNIS-TEQMLYTEADLEASMEKIETINFHEERDV-MGVRFCAYIAGHVLGAAMFMIEIAGI 178
Cdd:cd07734  81 ATHPTVALGRLLLEDYVKSAERIgQDQSLYTPEDIEEALKHIVPLGYGQSIDLfPALSLTAYNAGHVLGAAMWEIQIYGE 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 24648013 179 KILYTGDFSRQEDRHLMAAEVPPMKPDVLITES 211
Cdd:cd07734 161 KLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 20-211 4.96e-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: 226.37  E-value: 4.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  20 IKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIE-----ADEIDLLFISHFHLDHCGALPWFLMKTS 94
Cdd:cd16291   1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISqngpfTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  95 FKGRCFMTHATKAIYRWMLSDYIKIS-NISTEQMLYTEADLEASMEKIETINFHEERDV-MGVRFCAYIAGHVLGAAMFM 172
Cdd:cd16291  81 YDGPIYMTHPTKAICPILLEDYRKIAvERKGETNFFTSQMIKDCMKKVIAVNLHETVQVdDELEIKAYYAGHVLGAAMFY 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24648013 173 IEIAGIKILYTGDFSRQEDRHLMAAEVPPMKPDVLITES 211
Cdd:cd16291 161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 20-211 5.01e-66

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: 215.79  E-value: 5.01e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  20 IKPLGAGQEVGRSCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDL-IEADEIDLLFISHFHLDHCGALPwFLMKTSFKGR 98
Cdd:cd16295   1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFpFDPKEIDAVILTHAHLDHSGRLP-LLVKEGFRGP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  99 CFMTHATKAIYRWMLSDYIKISNISTEQM----LYTEADLEASMEKIETINFHEERDV-MGVRFCAYIAGHVLGAAMFMI 173
Cdd:cd16295  80 IYATPATKDLAELLLLDSAKIQEEEAEHPpaepLYTEEDVEKALKHFRPVEYGEPFEIgPGVKVTFYDAGHILGSASVEL 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24648013 174 EI-AGIKILYTGDFSRQEDRhLMAAEVPPMKPDVLITES 211
Cdd:cd16295 160 EIgGGKRILFSGDLGRKNTP-LLRDPAPPPEADYLIMES 197
CPSF73-100_C pfam11718
Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term; This is the C-terminal ...
 486-680 5.06e-64

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: 210.82  E-value: 5.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   486 KLSGVLVKRDFKYHLLAPSDLGKYTDMSMSVVTQRQSIPWGSSLSTLELLLDRIgAGCVEVLEAERK---LRVFGCIELT 562
Cdd:pfam11718   2 LVSGVLVKKDFNYHLMAPEDLREYTGLSTTTVTQRQSIPLSASFSLLRWHLEQM-FGDVEELEDKEGkptLRVMGCVTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   563 VEQKIIVMEWQATHVNDVYADAVLACIMQSELGGTNLKGATKQ-----TKSEDSRFRECLIETLQDTFGDNCVPKMFEGD 637
Cdd:pfam11718  81 VEKGEVTLEWEGNPVNDMIADSVLAVLLSVESSPASVKLSELPlrnphAESDPEERIERLIMLLEAQFGEDCVIELPKVP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24648013   638 LLPVTVSGKRAEINLETLAISCaEDDVLRQMLNTTVQKLHQTL 680
Cdd:pfam11718 161 GLEVTVDGKVANIDLETLEVEC-EDEVLKDRVETVVERAVEAV 202
CPSF73-100_C smart01098
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the ...
 483-683 9.50e-55

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: 186.46  E-value: 9.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    483 VGSKLSGVLVKRDFKYHLLAPSDLGKYTDMSMSVVTQRQSIPWGSSLSTLE---LLLDRIGAGCVEVLEAERK----LRV 555
Cdd:smart01098   1 EGQIISGILVKKDFNYDLLLPSDLDLRTDLSTSTIIQRQTIPLPSSASLLLvllELMFEFGFVEEDVDEEEKKekaaLIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    556 FGCIELTVEQKIIVMEWQATHVNDVYADAVLACIMQSELGGTNLKG----ATKQTKSEDSRFRECLIE-TLQDTFGDNCV 630
Cdd:smart01098  81 MGDVTVTYSGHMLVLEWESSPVNDMDADSDSAIILLISSEPSPAKVksssKSKHHHHNDEEFREKLIEiLLKEQFGDGVV 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24648013    631 pKMFEGDLLPVTVSGKRAEINLETLAISCAEDDVLRQMLNTTVQKLHQTLVSA 683
Cdd:smart01098 161 -NVEEGEDLKVTVDGKTANIDLETLKVVEEDDESLVERLEELLERIRLTLLPI 212
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 252-373 3.64e-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: 154.23  E-value: 3.64e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    252 AQELLLILDEFWSQNpDLHEIPIYYASSLAKKCMAVYQTYINAMNDRIRRQIAV-NNPFVFRHISNLKGIDHFEDI---- 326
Cdd:smart01027   1 TQELLLILEELWREG-ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKSLEESKRLndyk 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 24648013    327 GPCVIMASPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAKAV 373
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 ...
 252-371 3.70e-37

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: 134.18  E-value: 3.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   252 AQELLLILDEFWSQNPdLHEIPIYYASSLAKKCMAVYQTYINAMNDRIRRQIavnnpfvfRHISNLKGIDhfEDIGPCVI 331
Cdd:pfam10996   1 AQELLYLLDELWREGR-LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFV--------ISKSESKAIN--EGKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 24648013   332 MASPGMMQSGLSRELFESWCTDPKNGVIIAGYCVEGTLAK 371
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 22-211 1.20e-20

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


Pssm-ID: 293851  Cd Length: 199  Bit Score: 90.27  E-value: 1.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  22 PLGAGQEVGRSCIMLEFKGKKIMLDCGihpgLSGMDALPYVDLIE--ADEIDLLFISHFHLDHCGALPWFLMKTSFKGRC 99
Cdd:cd16293   3 PLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLKriAPTIDAVLLSHPDLEHLGALPYLVGKLGLTCPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 100 FMTHATKAIYR-WMLSDYIKISNISTEQmLYTEADLEASMEKIETINFHEERDVM----GVRFCAYIAGHVLGAAMFMIE 174
Cdd:cd16293  79 YATLPVHKMGRmFMYDLYQSRGLEEDFN-LFTLDDVDEAFDRITQLKYSQPVNLRgkgdGLTITAYNAGHTLGGTIWKIT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24648013 175 IAGIKILYTGDFSRQEDRHLMAAEVP---PMKPDVLITES 211
Cdd:cd16293 158 KDSEDIVYAVDWNHKKERHLNGAVLDsfgGLRPSLLITDA 197
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
32-224 9.32e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 74.46  E-value: 9.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  32 SCIMLEFKGKKIMLDCGihPG-LSGMDALPyvdlIEADEIDLLFISHFHLDHCGALPWFLMKTSFKGR-----CFMTHAT 105
Cdd:COG1234  20 SSYLLEAGGERLLIDCG--EGtQRQLLRAG----LDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGRekpltIYGPPGT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 106 KAIYRWMLSDYIKISNISTEqmlyteadleasmekIETINFHEERDVMGVRFCAYIAGHVLGAAMFMIEIAGIKILYTGD 185
Cdd:COG1234  94 KEFLEALLKASGTDLDFPLE---------------FHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24648013 186 FSRQEDRHLMAAEVppmkpDVLITESTYGTHIHEKREDR 224
Cdd:COG1234 159 TRPCEALVELAKGA-----DLLIHEATFLDEEAELAKET 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-210 1.83e-14

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: 72.64  E-value: 1.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  19 QIKPLGAGQEVGRSCIMLEFKGKKIMLDCGI-----------------------HPGLSGMDALPYVDLIEAD-EIDLLF 74
Cdd:cd07732   1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLpldpeskyfdevldflelgllpdIVGLYRDPLLLGGLRSEEDpSVDAVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  75 ISHFHLDHCGALPwfLMKTSFKgrCFMTHATKAIYRWMLSDYIKISNISteqmlyteadleasmEKIETINFHEERDVMG 154
Cdd:cd07732  81 LSHAHLDHYGLLN--YLRPDIP--VYMGEATKRILKALLPFFGEGDPVP---------------RNIRVFESGKSFTIGD 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648013 155 VRFCAYIAGH-VLGAAMFMIEIAGIKILYTGDF----SRQED-RHLMAAevPPMKPDVLITE 210
Cdd:cd07732 142 FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFrfhgRKPELtEAFVEK--APKNIDVLLME 201
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 20-185 2.54e-14

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: 71.53  E-value: 2.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  20 IKPLGAGQEV-----GRSCIMLEFKGKKIMLDCG--IHPGLSGMDALPyvdlieaDEIDLLFISHFHLDHCGALPWFLMK 92
Cdd:cd16272   1 LTFLGTGGAVpsltrNTSSYLLETGGTRILLDCGegTVYRLLKAGVDP-------DKLDAIFLSHFHLDHIGGLPTLLFA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  93 TSFKGRC-----FMTHATKAIYRWMLSDYIKISNISTEqmlyteadleasMEKIETINFHEERDVMGVRFCAYIAGHVLG 167
Cdd:cd16272  74 RRYGGRKkpltiYGPKGIKEFLEKLLNFPVEILPLGFP------------LEIEELEEGGEVLELGDLKVEAFPVKHSVE 141

                       170
                ....*....|....*...
gi 24648013 168 AAMFMIEIAGIKILYTGD 185
Cdd:cd16272 142 SLGYRIEAEGKSIVYSGD 159
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
32-204 9.64e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.48  E-value: 9.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    32 SCIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLiEADEIDLLFISHFHLDHCGALPWFLMKTSFKGRCFMTHATKAIYRW 111
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL-GPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   112 MLSDYIKISNISTEqmlyteadlEASMEKIETINFHEERDVMGVRFcAYIAGHVLGAAMFMIEIAGIKILYTGDFSRQED 191
Cdd:pfam00753  86 LGLAASRLGLPGPP---------VVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGE 155

                         170
                  ....*....|...
gi 24648013   192 RHLMAAEVPPMKP 204
Cdd:pfam00753 156 IGRLDLPLGGLLV 168
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-186 9.65e-14

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: 69.89  E-value: 9.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013     32 SCIMLEFKGKKIMLDCGIHPGlsgMDALPYVDLIEADEIDLLFISHFHLDHCGALPWFLMKTSFKgrcfmTHATKAIYRW 111
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEA---EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAP-----VYAPEGTAEL 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648013    112 MLSDYIKISNisteqmlytEADLEASMEKIETINFHEERDVMGVRFCA-YIAGHVLGAAMFMIEIAgiKILYTGDF 186
Cdd:smart00849  73 LKDLLALLGE---------LGAEAEPAPPDRTLKDGDELDLGGGELEViHTPGHTPGSIVLYLPEG--KILFTGDL 137
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 22-223 2.02e-13

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


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 70.51  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  22 PLGAGQEVGRSCIMLEFKGKKIMLDCGIH-PGlsgmDALPYVDLI---------EADEIDLLFISHFHLDHCGALPWFLM 91
Cdd:cd07714   2 PLGGLGEIGKNMYVVEYDDDIIIIDCGLKfPD----EDMPGVDYIipdfsyleeNKDKIKGIFITHGHEDHIGALPYLLP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  92 KTSFKgrCFMTHATKAIYRWMLSDYIKISNIsteqmlyteadleasmeKIETINFHEERDVMGVRFCAYIAGH-VLGAAM 170
Cdd:cd07714  78 ELNVP--IYATPLTLALIKKKLEEFKLIKKV-----------------KLNEIKPGERIKLGDFEVEFFRVTHsIPDSVG 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648013 171 FMIEIAGIKILYTGDF--------SRQEDRHLMaAEVPPMKPDVLITESTYGTHiHEKRED 223
Cdd:cd07714 139 LAIKTPEGTIVHTGDFkfdqtpvdGKPTDLEKL-AELGKEGVLLLLSDSVHVSG-HASQED 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 36-208 9.70e-13

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 67.24  E-value: 9.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013    36 LEFKGKKIMLDCGIHPGLSGMDALPYVDLIeADEIDLLFISHFHLDHCGALPWFLMKtsFKGRCFMT---HATKAIYRW- 111
Cdd:pfam16661   2 LEFDNVRILLDPGWDGSFSYESDLKYLEKI-LPEVDLILLSHPTLEHLGAYPLLYYK--FGSHLGSNipvYATLPVANLg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   112 ---MLSDYIKISNISTEQM-LYTEADLEASMEKIETINFHEERDVM----GVRFCAYIAGHVLGAAMFMIEIAGIKILYT 183
Cdd:pfam16661  79 rvsTYDLYASRGILGPYDSsELDLDDIDAAFDKIKTLKYSQTVDLKgkfdGLTITPYNSGHTLGGTIWKISKNSEKIVYA 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 24648013   184 GDFSRQEDRHLMAAEVPP---------MKPDVLI 208
Cdd:pfam16661 159 VDWNHTKDSHLNGASLLDstgkpleslVRPTALI 192
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 31-182 2.14e-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: 2.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  31 RSCIMLEFKGKKIMLDCGIhpglsgmDALPYVDLIEADEIDLLFISHFHldHCGALPWFLMKTSFKGRCFMTHATKAIYR 110
Cdd:cd16294  12 LPCNVLKFKSTTIMLDCGL-------DCPPETELIDLSTVDVILISNYH--CMLALPFITEYTGFTGVVYATEPTVQIGR 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648013 111 WMLSDYIkisnisteqmlyteadleASMEKIETINFHEERDVMG-VRFCAYIAGHVLGAAMFMIEIAGIKILY 182
Cdd:cd16294  83 LLMEELV------------------QALSKIQLVGYSQKLDLFGaVQVTALSSGYCLGSSNWVIQSHYEKISY 137
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 387-441 1.12e-10

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: 57.63  E-value: 1.12e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24648013   387 KLPLNMSVDYIS-FSAHTDYQQTSEFIRLLKPTHVVLVHGEQNEMSRLKLALQREY 441
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEEL 56
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
18-90 4.76e-10

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 62.39  E-value: 4.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  18 LQIKPLGAGQEVGRSCIMLEFKGKKIMLDCGI-HPGlsgmDALPYVDLI---------EADEIDLLFISHFHLDHCGALP 87
Cdd:COG0595   6 LRIIPLGGLGEIGKNMYVYEYDDDIIIVDCGLkFPE----DEMPGVDLVipdisyleeNKDKIKGIVLTHGHEDHIGALP 81


                ...
gi 24648013  88 WFL 90
Cdd:COG0595  82 YLL 84
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 32-214 5.74e-09

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: 57.46  E-value: 5.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  32 SCIMLEFKGKKIMLDCG-------IHPGLSGMDalpyvdlieadeIDLLFISHFHLDHCGALPWFLMKTSFKGRcfmtha 104
Cdd:cd07717  18 SSIALRLEGELWLFDCGegtqrqlLRAGLSPSK------------IDRIFITHLHGDHILGLPGLLSTMSLLGR------ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 105 TKAIY----RWmLSDYIKIS-NISTEQMLYteadleasmekieTINFHEERDVMGVRF-------CAYIAGHVLGAAMFM 172
Cdd:cd07717  80 TEPLTiygpKG-LKEFLETLlRLSASRLPY-------------PIEVHELEPDPGLVFeddgftvTAFPLDHRVPCFGYR 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24648013 173 IEIaGIKILYTGDfSRQEDRHLMAAEvppmKPDVLITESTYG 214
Cdd:cd07717 146 FEE-GRKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 32-98 1.55e-08

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: 56.46  E-value: 1.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648013    32 SCIMLEFKGKKIMLDCG-------IHPGLSGMDalpyvdlieadeIDLLFISHFHLDHCGALPWFLMKTSFKGR 98
Cdd:TIGR02651  19 PSIALKLNGELWLFDCGegtqrqmLRSGISPMK------------IDRIFITHLHGDHILGLPGLLSTMSFQGR 80
PRK00055 PRK00055
ribonuclease Z; Reviewed
 32-214 1.80e-08

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 55.96  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013   32 SCIMLEFKGKKIMLDCG-------IHPGLSGMDalpyvdlieadeIDLLFISHFHLDHCGALPWFLMKTSFKGRcfmTHA 104
Cdd:PRK00055  21 SSILLRLGGELFLFDCGegtqrqlLKTGIKPRK------------IDKIFITHLHGDHIFGLPGLLSTRSLSGR---TEP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  105 TKAIYRWMLSDYIKISNISTEQMLY--TEADleasmeKIETINfHEERDVMGVRFCAYIA------------GHVLGAAM 170
Cdd:PRK00055  86 LTIYGPKGIKEFVETLLRASGSLGYriAEKD------KPGKLD-AEKLKALGVPPGPLFGklkrgedvtledGRIINPAD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24648013  171 FM-IEIAGIKILYTGDFSRQEDRHLMAAEVppmkpDVLITESTYG 214
Cdd:PRK00055 159 VLgPPRKGRKVAYCGDTRPCEALVELAKGA-----DLLVHEATFG 198
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 31-213 1.25e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 53.36  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  31 RSCIMLEFKGKKIMLDCGihPGLSG-MDALPyvdlIEADEIDLLFISHFHLDHCGALPWFLMKTSFKG-RCFMTHATKAI 108
Cdd:COG1235  35 RSSILVEADGTRLLIDAG--PDLREqLLRLG----LDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLEA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 109 YRWMLSdyikisnisteqmlYTEADLEASMEkIETINFHEERDVMGVRFCAY----IAGHVLGaamFMIEIAGIKILYTG 184
Cdd:COG1235 109 LERRFP--------------YLFAPYPGKLE-FHEIEPGEPFEIGGLTVTPFpvphDAGDPVG---YRIEDGGKKLAYAT 170

                       170       180
                ....*....|....*....|....*....
gi 24648013 185 DFSRQEDRHLMAAEvppmKPDVLITESTY 213
Cdd:COG1235 171 DTGYIPEEVLELLR----GADLLILDATY 195
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-90 2.37e-07

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 51.49  E-value: 2.37e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648013  23 LGAGQEVG-----RSCIMLEFKGKKIMLDCG--IHPGLSGMDalpyvdlIEADEIDLLFISHFHLDHCGALPWFL 90
Cdd:cd07740   3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGasSLIALKRAG-------IDPNAIDAIFITHLHGDHFGGLPFFL 70
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 29-208 4.46e-07

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: 51.78  E-value: 4.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  29 VGR-SCIMLEFKGKKIML-DCGIHPGLSGMDA--LPYVDLIEADEIDLLFISHFHLDHCGALPWFLmktsfkgrcfmtha 104
Cdd:COG2333   8 VGQgDAILIRTPDGKTILiDTGPRPSFDAGERvvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVL-------------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 105 tkaiyrwmlsDYIKISNI-------STEQMLYTEADLEASMEKIETINFHEERDVMGVRFcayiagHVLGAAM------- 170
Cdd:COG2333  74 ----------EAFPVGRVlvsgppdTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRF------EVLWPPEdllegsd 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24648013 171 -------FMIEIAGIKILYTGDFSRQEDRHLMAAEvPPMKPDVLI 208
Cdd:COG2333 138 ennnslvLRLTYGGFSFLLTGDAEAEAEAALLARG-PDLKADVLK 181
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 32-83 7.92e-07

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: 49.75  E-value: 7.92e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24648013  32 SCIMLEFKGKKIMLDCGihPG-LSGMdaLPYVDLieaDEIDLLFISHFHLDHC 83
Cdd:cd07716  19 SGYLLEADGFRILLDCG--SGvLSRL--QRYIDP---EDLDAVVLSHLHPDHC 64
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 33-90 1.09e-06

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: 50.70  E-value: 1.09e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24648013  33 CIMLEFKGKKIMLDCGIHPGL-SGMDALPyVDLieaDEIDLLFISHFHLDHCGALPWFL 90
Cdd:cd07713  22 SLLIETEGKKILFDTGQSGVLlHNAKKLG-IDL---SDIDAVVLSHGHYDHTGGLKALL 76
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 29-223 1.22e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 49.92  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  29 VGRSCIMLEFKGKKIMLDcgihPGLSGMDALPYVDLIEADE---IDLLFISHFHLDHCGalpwflmktsfkgrcfmthat 105
Cdd:COG2220   9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLDPEDlpkIDAVLVTHDHYDHLD--------------------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013 106 KAIYRWMLSDYIKIsnISTEQMlytEADLEAS-MEKIETINFHEERDVMGVRFCAYIAGH--------VLGAAMFMIEIA 176
Cdd:COG2220  64 DATLRALKRTGATV--VAPLGV---AAWLRAWgFPRVTELDWGESVELGGLTVTAVPARHssgrpdrnGGLWVGFVIETD 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24648013 177 GIKILYTGD------FSRQEDRHlmaaevppmKPDVLITEsTYGTHIHEKRED 223
Cdd:COG2220 139 GKTIYHAGDtgyfpeMKEIGERF---------PIDVALLP-IGAYPFTMGPEE 181
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
33-90 6.87e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 48.34  E-value: 6.87e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  33 CIMLEFKGKKIMLDCGiHPG--LSGMDALPyVDLieaDEIDLLFISHFHLDHCGALPWFL 90
Cdd:COG1237  24 SALIETEGKRILFDTG-QSDvlLKNAEKLG-IDL---SDIDAVVLSHGHYDHTGGLPALL 78
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 33-185 3.24e-05

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: 45.45  E-value: 3.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  33 CIMLEFKGKKIMLDcgihPGLSGMDALPYVDLIEA--DEIDLLFISHFHLDHCGALPWFlmKTSFKGRcfmTHATKAIYR 110
Cdd:COG0491  17 SYLIVGGDGAVLID----TGLGPADAEALLAALAAlgLDIKAVLLTHLHPDHVGGLAAL--AEAFGAP---VYAHAAEAE 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648013 111 WMLSDyikisnisTEQMLYTEADLEASmekiETINFHEERDVMGVRFCAYIA-GHVLGAAMFMIEiaGIKILYTGD 185
Cdd:COG0491  88 ALEAP--------AAGALFGREPVPPD----RTLEDGDTLELGGPGLEVIHTpGHTPGHVSFYVP--DEKVLFTGD 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 33-87 1.94e-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: 1.94e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24648013  33 CIMLEFKGKKIMLDCGIHPGLSGMDALPYVDLIEADEIDLLFISHFHLDHCGALP 87
Cdd:cd07731  12 AILIQTPGKTILIDTGPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLD 66
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 32-91 2.26e-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: 42.89  E-value: 2.26e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648013  32 SCIMLEFKGKKIMLDCGihPG------LSGMDAlpyvdlieaDEIDLLFISHFHLDHCGALPWFLM 91
Cdd:cd07719  19 PSTLVVVGGRVYLVDAG--SGvvrrlaQAGLPL---------GDLDAVFLTHLHSDHVADLPALLL 73
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 40-86 3.17e-04

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 42.97  E-value: 3.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648013  40 GKKIMLDCGIHPGLSGMDALPYVDL------------------IEADEIDLLFISHFHLDHCGAL 86
Cdd:cd07729  41 EGTILVDTGFHPDAADDPGGLELAFppgvteeqtleeqlarlgLDPEDIDYVILSHLHFDHAGGL 105
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 39-186 3.85e-04

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: 41.89  E-value: 3.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648013  39 KGKKIMLDcgihPGLSGMDALpyVDLIEAD--EIDLLFISHFHLDHCGALPWFlmKTSFKGRCFMTHATKAiyrwMLSDy 116
Cdd:cd06262  19 EGEAILID----PGAGALEKI--LEAIEELglKIKAILLTHGHFDHIGGLAEL--KEAPGAPVYIHEADAE----LLED- 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648013 117 ikisniSTEQMLYTEADLEASMEKIETINFHEERDVMGVRF-CAYIAGHVLGAAMFMIEIAgiKILYTGDF 186
Cdd:cd06262  86 ------PELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELeVIHTPGHTPGSVCFYIEEE--GVLFTGDT 148
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 65-110 8.00e-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: 41.87  E-value: 8.00e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24648013  65 IEADEIDLLFISHFHLDHCGALPWFlmktsFKGRCFMTHATKAIYR 110
Cdd:cd07730  79 IDPEDIDAVILSHLHWDHIGGLSDF-----PNARLIVGPGAKEALR 119
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 32-89 8.44e-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: 41.33  E-value: 8.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648013  32 SCIMLEFKGKKIMLDCG--IHP-GLSGMDALPYVdlieadEIDLLFiSHFHLDH-CGaLPWF 89
Cdd:cd07715  24 SCVEVRAGGELLILDAGtgIRElGNELMKEGPPG------EAHLLL-SHTHWDHiQG-FPFF 77
 
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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