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Conserved domains on  [gi|1016470356|ref|NP_001309199|]
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cleavage and polyadenylation specificity factor subunit 2 isoform 2 [Homo sapiens]

Protein Classification

CPSF2-like_MBL-fold and Beta-Casp domain-containing protein( domain architecture ID 10888779)

protein containing domains CPSF2-like_MBL-fold, Beta-Casp, RMMBL, and CPSF100_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 2.52e-128

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: 379.17  E-value: 2.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   7 LTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYA 86
Cdd:cd16293     1 FTPLSGAGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  87 TIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDG 166
Cdd:cd16293    81 TLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTITAYNAGHTLGGTIWKITKDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016470356 167 eEEIVYAVDFNHKREIHLNGCSLEMLS--RPSLLITDSFN 204
Cdd:cd16293   161 -EDIVYAVDWNHKKERHLNGAVLDSFGglRPSLLITDADN 199
CPSF100_C pfam13299
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 557-728 3.81e-65

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


:

Pssm-ID: 463836  Cd Length: 162  Bit Score: 212.89  E-value: 3.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 557 VRLKDSLVSSLQFCKAKDAELAWIDGVLDMRvskvdtgvILEEGELKDDGEDSEMQVEAPSDSsviaQQKAMKSLFGDDE 636
Cdd:pfam13299   1 VKLSDSLVSSLKWQKVRGLEVAWVTGRLDRA--------ALEEGAAEEEEEEEDEEEENANKK----QKLEQFSLKDDDE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 637 KETGEESEIIPTLEPLPPHEVP-GHQSVFMNEPRLSDFKQVLLREGIQAEFVG-GVLVCNNQVAVRRTETGRIGLEGCLC 714
Cdd:pfam13299  69 KESKESKDSIPTLDPLPSNLAPaVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGeGTLVCNGTVAVRKTETGRIEIEGVGG 148

                         170
                  ....*....|....
gi 1016470356 715 QDFYRIRDLLYEQY 728
Cdd:pfam13299 149 PTFYAVRRLIYEQL 162
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 243-368 2.20e-28

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: 110.32  E-value: 2.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  243 VLELAQLLDQIWRTKdaGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEdKRNNPFQFRHLSLCHGLSD---LAR 319
Cdd:smart01027   1 TQELLLILEELWREG--ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFE-QGRNPFDFKNLKFVKSLEEskrLND 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1016470356  320 VPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFL 368
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 480-540 2.85e-12

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: 62.25  E-value: 2.85e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016470356 480 IKARVTYID-YEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGkdIKVYMP 540
Cdd:pfam07521   4 VRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELG--IEVFVP 63
 
Name Accession Description Interval E-value
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 2.52e-128

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: 379.17  E-value: 2.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   7 LTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYA 86
Cdd:cd16293     1 FTPLSGAGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  87 TIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDG 166
Cdd:cd16293    81 TLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTITAYNAGHTLGGTIWKITKDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016470356 167 eEEIVYAVDFNHKREIHLNGCSLEMLS--RPSLLITDSFN 204
Cdd:cd16293   161 -EDIVYAVDWNHKKERHLNGAVLDSFGglRPSLLITDADN 199
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 22-199 1.06e-87

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 273.70  E-value: 1.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  22 LLQVDEFRFLLDCGWDEHFS-MDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGK----LGLNCAIYATIPVYKMGQM 96
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSyESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYKfgshLGSNIPVYATLPVANLGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  97 FMYDLYQSRHN--TEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKdGEEEIVYAV 174
Cdd:pfam16661  81 STYDLYASRGIlgPYDSSELDLDDIDAAFDKIKTLKYSQTVDLKGKFDGLTITPYNSGHTLGGTIWKISK-NSEKIVYAV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1016470356 175 DFNHKREIHLNGCS--------LEMLSRPSLLI 199
Cdd:pfam16661 160 DWNHTKDSHLNGASlldstgkpLESLVRPTALI 192
CPSF100_C pfam13299
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 557-728 3.81e-65

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


Pssm-ID: 463836  Cd Length: 162  Bit Score: 212.89  E-value: 3.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 557 VRLKDSLVSSLQFCKAKDAELAWIDGVLDMRvskvdtgvILEEGELKDDGEDSEMQVEAPSDSsviaQQKAMKSLFGDDE 636
Cdd:pfam13299   1 VKLSDSLVSSLKWQKVRGLEVAWVTGRLDRA--------ALEEGAAEEEEEEEDEEEENANKK----QKLEQFSLKDDDE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 637 KETGEESEIIPTLEPLPPHEVP-GHQSVFMNEPRLSDFKQVLLREGIQAEFVG-GVLVCNNQVAVRRTETGRIGLEGCLC 714
Cdd:pfam13299  69 KESKESKDSIPTLDPLPSNLAPaVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGeGTLVCNGTVAVRKTETGRIEIEGVGG 148

                         170
                  ....*....|....
gi 1016470356 715 QDFYRIRDLLYEQY 728
Cdd:pfam13299 149 PTFYAVRRLIYEQL 162
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 243-368 2.20e-28

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: 110.32  E-value: 2.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  243 VLELAQLLDQIWRTKdaGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEdKRNNPFQFRHLSLCHGLSD---LAR 319
Cdd:smart01027   1 TQELLLILEELWREG--ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFE-QGRNPFDFKNLKFVKSLEEskrLND 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1016470356  320 VPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFL 368
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 6-387 2.86e-27

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 114.90  E-value: 2.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   6 KLTTLSGVQEESALCYLLQVDEFRFLLDCGWD--------EHFSMDIIDslrkhvhqIDAVLLSHP--DplHLGALPYAV 75
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFqggkernwPPFPFRPSD--------VDAVVLTHAhlD--HSGALPLLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  76 gKLGLNCAIYATIPVYK-MGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLkgkgHGLSITPLPAGHM 154
Cdd:COG1236    72 -KEGFRGPIYATPATADlARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEI----GGVRVTFHPAGHI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 155 IGGTIWKIvKDGEEEIVYAVDFNHKREIHLNGcsLEMLSRPSLLITDSfnaTY---VQPRRKQRDEQLLTNVLETLRGDG 231
Cdd:COG1236   147 LGSAQVEL-EVGGKRIVFSGDYGREDDPLLAP--PEPVPPADVLITES---TYgdrLHPPREEVEAELAEWVRETLARGG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 232 NVLI---AVDTAGRVL-ELAQLLDQiWRTKDA-----GLGVYSLALLnnvsynvvefsksqvewmsDKLMRCFEDKRNNP 302
Cdd:COG1236   221 TVLIpafALGRAQELLyLLRELKKE-GRLPDIpiyvsGMAIRATEIY-------------------RRHGEYLRDEAQDP 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 303 FQFRHLSLCHGLSDLARV--PSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLID-NPSEKI--T 377
Cdd:COG1236   281 FALPNLRFVTSVEESKALnrKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRgAKEVKIfgE 360

                         410
                  ....*....|
gi 1016470356 378 EIELRKRVKL 387
Cdd:COG1236   361 EVPVRARVER 370
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 243-366 8.18e-20

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: 85.26  E-value: 8.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 243 VLELAQLLDQIWRTKDagLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNpfqfrhlslchglSDLARVPS 322
Cdd:pfam10996   1 AQELLYLLDELWREGR--LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKSES-------------KAINEGKG 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1016470356 323 PKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLAR 366
Cdd:pfam10996  66 PKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 480-540 2.85e-12

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: 62.25  E-value: 2.85e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016470356 480 IKARVTYID-YEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGkdIKVYMP 540
Cdd:pfam07521   4 VRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELG--IEVFVP 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-182 3.94e-09

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: 56.41  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   20 CYLLQVDEFRFLLDCGWDEhfSMDIIDSLRKH-VHQIDAVLLSHPDPLHLGALPYAVGKlgLNCAIYATipvyKMGQMFM 98
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGE--AEDLLAELKKLgPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAP----EGTAELL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   99 YDLYQSRHNTEDFtlftlddvDAAFDKIQQLKFSQIVNLkgKGHGLSITPLPaGHMIGGTiwkIVKDGEEEIVYAVDFNH 178
Cdd:smart00849  74 KDLLALLGELGAE--------AEPAPPDRTLKDGDELDL--GGGELEVIHTP-GHTPGSI---VLYLPEGKILFTGDLLF 139


                   ....
gi 1016470356  179 KREI 182
Cdd:smart00849 140 AGGD 143
 
Name Accession Description Interval E-value
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 2.52e-128

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: 379.17  E-value: 2.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   7 LTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYA 86
Cdd:cd16293     1 FTPLSGAGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  87 TIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDG 166
Cdd:cd16293    81 TLPVHKMGRMFMYDLYQSRGLEEDFNLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTITAYNAGHTLGGTIWKITKDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016470356 167 eEEIVYAVDFNHKREIHLNGCSLEMLS--RPSLLITDSFN 204
Cdd:cd16293   161 -EDIVYAVDWNHKKERHLNGAVLDSFGglRPSLLITDADN 199
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 22-199 1.06e-87

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 273.70  E-value: 1.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  22 LLQVDEFRFLLDCGWDEHFS-MDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGK----LGLNCAIYATIPVYKMGQM 96
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSFSyESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYKfgshLGSNIPVYATLPVANLGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  97 FMYDLYQSRHN--TEDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKdGEEEIVYAV 174
Cdd:pfam16661  81 STYDLYASRGIlgPYDSSELDLDDIDAAFDKIKTLKYSQTVDLKGKFDGLTITPYNSGHTLGGTIWKISK-NSEKIVYAV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1016470356 175 DFNHKREIHLNGCS--------LEMLSRPSLLI 199
Cdd:pfam16661 160 DWNHTKDSHLNGASlldstgkpLESLVRPTALI 192
CPSF100_C pfam13299
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 557-728 3.81e-65

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


Pssm-ID: 463836  Cd Length: 162  Bit Score: 212.89  E-value: 3.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 557 VRLKDSLVSSLQFCKAKDAELAWIDGVLDMRvskvdtgvILEEGELKDDGEDSEMQVEAPSDSsviaQQKAMKSLFGDDE 636
Cdd:pfam13299   1 VKLSDSLVSSLKWQKVRGLEVAWVTGRLDRA--------ALEEGAAEEEEEEEDEEEENANKK----QKLEQFSLKDDDE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 637 KETGEESEIIPTLEPLPPHEVP-GHQSVFMNEPRLSDFKQVLLREGIQAEFVG-GVLVCNNQVAVRRTETGRIGLEGCLC 714
Cdd:pfam13299  69 KESKESKDSIPTLDPLPSNLAPaVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGeGTLVCNGTVAVRKTETGRIEIEGVGG 148

                         170
                  ....*....|....
gi 1016470356 715 QDFYRIRDLLYEQY 728
Cdd:pfam13299 149 PTFYAVRRLIYEQL 162
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 8-202 1.16e-29

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: 116.28  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   8 TTLSGVQEESALCYLLQVDEFRFLLDCGWdeHFSMDIIDSL----RKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCA 83
Cdd:cd07734     1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGM--NPGKEDPEAClpqfELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  84 IYATIPVYKMGQMFMYDLYQSRHNT-EDFTLFTLDDVDAAFDKIQQLKFSQIVNLKGkghGLSITPLPAGHMIGGTIWKI 162
Cdd:cd07734    79 IYATHPTVALGRLLLEDYVKSAERIgQDQSLYTPEDIEEALKHIVPLGYGQSIDLFP---ALSLTAYNAGHVLGAAMWEI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016470356 163 VKDGeEEIVYAVDFNHKREIHLNGCSLeMLSRPSLLITDS 202
Cdd:cd07734   156 QIYG-EKLVYTGDFSNTEDRLLPAASI-LPPRPDLLITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 243-368 2.20e-28

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: 110.32  E-value: 2.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  243 VLELAQLLDQIWRTKdaGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEdKRNNPFQFRHLSLCHGLSD---LAR 319
Cdd:smart01027   1 TQELLLILEELWREG--ELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFE-QGRNPFDFKNLKFVKSLEEskrLND 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1016470356  320 VPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFL 368
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 6-387 2.86e-27

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 114.90  E-value: 2.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   6 KLTTLSGVQEESALCYLLQVDEFRFLLDCGWD--------EHFSMDIIDslrkhvhqIDAVLLSHP--DplHLGALPYAV 75
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFqggkernwPPFPFRPSD--------VDAVVLTHAhlD--HSGALPLLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  76 gKLGLNCAIYATIPVYK-MGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLKFSQIVNLkgkgHGLSITPLPAGHM 154
Cdd:COG1236    72 -KEGFRGPIYATPATADlARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEI----GGVRVTFHPAGHI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 155 IGGTIWKIvKDGEEEIVYAVDFNHKREIHLNGcsLEMLSRPSLLITDSfnaTY---VQPRRKQRDEQLLTNVLETLRGDG 231
Cdd:COG1236   147 LGSAQVEL-EVGGKRIVFSGDYGREDDPLLAP--PEPVPPADVLITES---TYgdrLHPPREEVEAELAEWVRETLARGG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 232 NVLI---AVDTAGRVL-ELAQLLDQiWRTKDA-----GLGVYSLALLnnvsynvvefsksqvewmsDKLMRCFEDKRNNP 302
Cdd:COG1236   221 TVLIpafALGRAQELLyLLRELKKE-GRLPDIpiyvsGMAIRATEIY-------------------RRHGEYLRDEAQDP 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 303 FQFRHLSLCHGLSDLARV--PSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLID-NPSEKI--T 377
Cdd:COG1236   281 FALPNLRFVTSVEESKALnrKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRgAKEVKIfgE 360

                         410
                  ....*....|
gi 1016470356 378 EIELRKRVKL 387
Cdd:COG1236   361 EVPVRARVER 370
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 243-366 8.18e-20

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: 85.26  E-value: 8.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356 243 VLELAQLLDQIWRTKDagLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNpfqfrhlslchglSDLARVPS 322
Cdd:pfam10996   1 AQELLYLLDELWREGR--LPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKSES-------------KAINEGKG 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1016470356 323 PKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLAR 366
Cdd:pfam10996  66 PKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 7-177 1.51e-16

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: 78.65  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   7 LTTLSGVQEESALCYLLQVDEFRFLLDCG------------WDEhFSMDIidslrkhvHQIDAVLLSHPDPLHLGALPYA 74
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGlfqggkeleelnNEP-FPFDP--------KEIDAVILTHAHLDHSGRLPLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  75 VgKLGLNCAIYATIPVYKMGQMFMYD-LYQSRHNTEDFT---LFTLDDVDAAFDKIQQLKFSQIVNLkgkGHGLSITPLP 150
Cdd:cd16295    72 V-KEGFRGPIYATPATKDLAELLLLDsAKIQEEEAEHPPaepLYTEEDVEKALKHFRPVEYGEPFEI---GPGVKVTFYD 147

                         170       180
                  ....*....|....*....|....*..
gi 1016470356 151 AGHMIGGTIWKIVKDGEEEIVYAVDFN 177
Cdd:cd16295   148 AGHILGSASVELEIGGGKRILFSGDLG 174
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 5-202 5.94e-16

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: 76.86  E-value: 5.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   5 IKLTTLSGVQEESALCYLLQVDEFRFLLDCG----WDEHFSMDIIDSLRkhVHQIDAVLLSHPDPLHLGALPYAVGKLGL 80
Cdd:cd16292     1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGihpgYSGLASLPFFDEID--LSEIDLLLITHFHLDHCGALPYFLQKTNF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  81 NCAIYATIPVYKMGQMFMYDLYQ-SRHNTEDFtLFTLDDVDAAFDKIQQLKFSQIVNLKgkghGLSITPLPAGHMIGGTI 159
Cdd:cd16292    79 KGRVFMTHPTKAIYKWLLSDYVRvSNISSDEM-LYTETDLEASMDKIETIDFHQEVEVN----GIKFTAYNAGHVLGAAM 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1016470356 160 WKIVKDGeEEIVYAVDFNHKREIHLNGCSLEMLsRPSLLITDS 202
Cdd:cd16292   154 FMVEIAG-VRVLYTGDYSREEDRHLPAAEIPPI-KPDVLIVES 194
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 20-202 3.41e-15

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: 74.60  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  20 CYLLQVDEFRFLLDCGW-----DEH----FSMdiIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYATIPV 90
Cdd:cd16291    14 CILVTIGGKNIMFDCGMhmgynDERrfpdFSY--ISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVGYDGPIYMTHPT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  91 YKMGQMFMYD---LYQSRHNTEDFtlFTLDDVDAAFDKIQQLKFSQIVNLKGkghGLSITPLPAGHMIGGTIWKiVKDGE 167
Cdd:cd16291    92 KAICPILLEDyrkIAVERKGETNF--FTSQMIKDCMKKVIAVNLHETVQVDD---ELEIKAYYAGHVLGAAMFY-VRVGD 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1016470356 168 EEIVYAVDFNHKREIHLNGCSLEMLsRPSLLITDS 202
Cdd:cd16291   166 ESVVYTGDYNMTPDRHLGAAWIDRL-RPDLLITES 199
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 5-172 3.32e-14

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: 70.99  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   5 IKLTTLSGvqEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDslrkhVHQIDAVLLShpDPLHLGALPYAVGKLGLNCAI 84
Cdd:cd16294     1 MKLYCLSG--HPTLPCNVLKFKSTTIMLDCGLDCPPETELID-----LSTVDVILIS--NYHCMLALPFITEYTGFTGVV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  85 YATIPVYKMGQMFMYDLYQsrhntedftlftlddvdaAFDKIQQLKFSQIVNLKGkghGLSITPLPAGHMIGGTIWkIVK 164
Cdd:cd16294    72 YATEPTVQIGRLLMEELVQ------------------ALSKIQLVGYSQKLDLFG---AVQVTALSSGYCLGSSNW-VIQ 129


                  ....*...
gi 1016470356 165 DGEEEIVY 172
Cdd:cd16294   130 SHYEKISY 137
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 480-540 2.85e-12

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: 62.25  E-value: 2.85e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016470356 480 IKARVTYID-YEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGkdIKVYMP 540
Cdd:pfam07521   4 VRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELG--IEVFVP 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-182 3.94e-09

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: 56.41  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   20 CYLLQVDEFRFLLDCGWDEhfSMDIIDSLRKH-VHQIDAVLLSHPDPLHLGALPYAVGKlgLNCAIYATipvyKMGQMFM 98
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGE--AEDLLAELKKLgPKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAP----EGTAELL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   99 YDLYQSRHNTEDFtlftlddvDAAFDKIQQLKFSQIVNLkgKGHGLSITPLPaGHMIGGTiwkIVKDGEEEIVYAVDFNH 178
Cdd:smart00849  74 KDLLALLGELGAE--------AEPAPPDRTLKDGDELDL--GGGELEVIHTP-GHTPGSI---VLYLPEGKILFTGDLLF 139


                   ....
gi 1016470356  179 KREI 182
Cdd:smart00849 140 AGGD 143
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 20-91 5.16e-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: 53.21  E-value: 5.16e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016470356  20 CYLLQVDEFRFLLDCGWdehfsmDIIDSLRKHV--HQIDAVLLS--HPDplH---LGALPYAVgKLGLNCAIYATIPVY 91
Cdd:cd07716    20 GYLLEADGFRILLDCGS------GVLSRLQRYIdpEDLDAVVLShlHPD--HcadLGVLQYAR-RYHPRGARKPPLPLY 89
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 20-207 3.28e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 49.12  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  20 CYLLQVDEFRFLLDCGwdehFSM-DIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNC-AIYATIPVYK-MGQM 96
Cdd:COG1235    37 SILVEADGTRLLIDAG----PDLrEQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATPGTLEaLERR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  97 F--MYDLYQSRHNTEDFTL---FTLDDvdaafdkiqqlkfsqivnlkgkghgLSITPLPAGHMIGGTI-WKIvKDGEEEI 170
Cdd:COG1235   113 FpyLFAPYPGKLEFHEIEPgepFEIGG-------------------------LTVTPFPVPHDAGDPVgYRI-EDGGKKL 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1016470356 171 VYAVDFNhkreiHLNGCSLEMLSRPSLLItdsFNATY 207
Cdd:COG1235   167 AYATDTG-----YIPEEVLELLRGADLLI---LDATY 195
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-210 3.84e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 48.13  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  20 CYLLQVDEFRFLLDCGWDEHFS-MDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKlgLNCAIYATIPVYKMGQMFM 98
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAAlLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEA--TDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  99 YDLYQSRHNTEDFTLFTLDDVDAAFDKiqqlkfsQIVNLKGKGHGLSITPLPAGHMIggtiwkIVKDGEEEIVYAVDFNH 178
Cdd:pfam00753  86 LGLAASRLGLPGPPVVPLPPDVVLEEG-------DGILGGGLGLLVTHGPGHGPGHV------VVYYGGGKVLFTGDLLF 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016470356 179 KREIHLNGC----------SLEMLSRPSLLITDSFNATYVQP 210
Cdd:pfam00753 153 AGEIGRLDLplggllvlhpSSAESSLESLLKLAKLKAAVIVP 194
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
20-87 5.94e-06

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 49.68  E-value: 5.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016470356  20 CYLLQVDEFRFLLDCGW----DEHFSMDII----DSLRKHVHQIDAVLLSHP--DplHLGALPYAVGKlgLNCAIYAT 87
Cdd:COG0595    21 MYVYEYDDDIIIVDCGLkfpeDEMPGVDLVipdiSYLEENKDKIKGIVLTHGheD--HIGALPYLLKE--LNVPVYGT 94
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 20-87 9.17e-06

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: 47.79  E-value: 9.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016470356  20 CYLLQVDEFRFLLDCGW----DEHFSMDII----DSLRKHVHQIDAVLLSHP--DplHLGALPYAVGKlgLNCAIYAT 87
Cdd:cd07714    13 MYVVEYDDDIIIIDCGLkfpdEDMPGVDYIipdfSYLEENKDKIKGIFITHGheD--HIGALPYLLPE--LNVPIYAT 86
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 20-86 1.15e-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: 46.99  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470356  20 CYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGlnCAIYA 86
Cdd:COG0491    17 SYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFG--APVYA 81
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 20-72 8.33e-04

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: 41.09  E-value: 8.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016470356  20 CYLLQVDEFRFLLDCGWDEHFSMDIIDslrKHVHQIDAVLLS--HPDplHLGALP 72
Cdd:cd16272    19 SYLLETGGTRILLDCGEGTVYRLLKAG---VDPDKLDAIFLShfHLD--HIGGLP 68
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 31-78 8.43e-04

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: 41.77  E-value: 8.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470356  31 LLDCGWDEHFSM---DIIDSLRKH-VHQIDAVLLSHPDPLHLGALP-----YAVGKL 78
Cdd:COG2333    25 LIDTGPRPSFDAgerVVLPYLRALgIRRLDLLVLTHPDADHIGGLAavleaFPVGRV 81
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
20-72 1.05e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 41.33  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016470356  20 CYLLQVDEFRFLLDCGwdEHfsmdIIDSLRKH---VHQIDAVLLSHPDPLHLGALP 72
Cdd:COG1234    21 SYLLEAGGERLLIDCG--EG----TQRQLLRAgldPRDIDAIFITHLHGDHIAGLP 70
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 20-173 1.17e-03

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: 40.73  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356  20 CYLLQVDEFR-FLLDCGWDEHfsMDIIDSLRKHVHQIDAVLLSH--PDplHLGALPYAVGKLGlncaiyatIPVYkMGQM 96
Cdd:cd06262    12 CYLVSDEEGEaILIDPGAGAL--EKILEAIEELGLKIKAILLTHghFD--HIGGLAELKEAPG--------APVY-IHEA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470356  97 FMYDLYQSRHNTEDFTLFTLDDVDAafdkIQQLKFSQIVNLkgKGHGLSITPLPaGHMIGGTIWKIvkdGEEEIVYA 173
Cdd:cd06262    79 DAELLEDPELNLAFFGGGPLPPPEP----DILLEDGDTIEL--GGLELEVIHTP-GHTPGSVCFYI---EEEGVLFT 145
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 6-91 3.60e-03

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: 39.91  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470356   6 KLTTL-------SGVQEESALCYLLQVDEFRFLLDCGWDEHF-----SMDIidSLRKhvhqIDAVLLSHP--DplHLGAL 71
Cdd:cd07713     1 KITVLvdntagdEGLLAEHGLSLLIETEGKKILFDTGQSGVLlhnakKLGI--DLSD----IDAVVLSHGhyD--HTGGL 72

                          90       100
                  ....*....|....*....|
gi 1016470356  72 PYAVgklglncAIYATIPVY 91
Cdd:cd07713    73 KALL-------ELNPKAPVY 85
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 18-78 5.19e-03

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: 38.65  E-value: 5.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016470356  18 ALCYLLQVDEFRFLLDCGWDEHF-SMDIIDSLR-KHVHQIDAVLLSHPDPLHLGALP-----YAVGKL 78
Cdd:cd07731    10 GDAILIQTPGKTILIDTGPRDSFgEDVVVPYLKaRGIKKLDYLILTHPDADHIGGLDavlknFPVKEV 77
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-73 7.17e-03

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 38.39  E-value: 7.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016470356  20 CYLLQVDEFRFLLDCGWDEHFSMdiidsLRKHVH--QIDAVLLSHPDPLHLGALPY 73
Cdd:cd07740    18 CFHVASEAGRFLIDCGASSLIAL-----KRAGIDpnAIDAIFITHLHGDHFGGLPF 68
 
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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