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Conserved domains on  [gi|767904818|ref|XP_011539952|]
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integrator complex subunit 11 isoform X3 [Homo sapiens]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440939)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme; similar to Thermus thermophilus ribonuclease TTHA0252, which exhibits endoribonuclease activity towards 23S and 16S rRNA in vitro and may function in RNA degradation

CATH:  3.60.15.30
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|11471246
SCOP:  3001057

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 2-292 3.19e-76

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 244.33  E-value: 3.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITES 80
Cdd:COG1236  115 AERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITES 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  81 TYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE-LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFI 159
Cdd:COG1236  192 TYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818 160 PWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTV 235
Cdd:COG1236  271 EYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTL 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818 236 GHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLVGQAE-PESVLLVHGE 292
Cdd:COG1236  345 GRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
 
Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 2-292 3.19e-76

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 244.33  E-value: 3.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITES 80
Cdd:COG1236  115 AERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITES 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  81 TYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE-LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFI 159
Cdd:COG1236  192 TYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818 160 PWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTV 235
Cdd:COG1236  271 EYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTL 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818 236 GHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLVGQAE-PESVLLVHGE 292
Cdd:COG1236  345 GRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 1-80 7.42e-57

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: 187.08  E-value: 7.42e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   1 MIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 80
Cdd:cd16291  120 MIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 121-239 9.14e-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: 150.00  E-value: 9.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   121 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 193
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767904818   194 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 239
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 121-237 2.36e-31

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: 116.46  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  121 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 199
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767904818  200 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 237
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
 
Name Accession Description Interval E-value
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 2-292 3.19e-76

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 244.33  E-value: 3.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITES 80
Cdd:COG1236  115 AERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITES 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  81 TYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQE-LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFI 159
Cdd:COG1236  192 TYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALGRAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818 160 PWTNQKIrktfvqRNMFEFKHIK----AFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTV 235
Cdd:COG1236  271 EYLRDEA------QDPFALPNLRfvtsVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTL 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818 236 GHKILSGQRKLEMEGRQVlEVKMQVE-YMSFSAHADAKGIMQLVGQAE-PESVLLVHGE 292
Cdd:COG1236  345 GRRLLRGAKEVKIFGEEV-PVRARVErLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 2-322 4.12e-75

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: 243.11  E-value: 4.12e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITE 79
Cdd:COG1782  130 VEKALKHFITLDYGEVTDIAPDIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIME 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  80 STYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLF 158
Cdd:COG1782  209 STYGGRLHPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAY 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818 159 IPWTNQKIRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQ 232
Cdd:COG1782  289 PEYLDEELRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAE 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818 233 GTVGHKILSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRV 309
Cdd:COG1782  369 GTLGRRLLDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGI 447

                        330
                 ....*....|...
gi 767904818 310 NCYMPANGETVTL 322
Cdd:COG1782  448 EVVIPENLETIRL 460
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 1-80 7.42e-57

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: 187.08  E-value: 7.42e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   1 MIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 80
Cdd:cd16291  120 MIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 121-239 9.14e-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: 150.00  E-value: 9.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   121 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 193
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767904818   194 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 239
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 1-80 2.71e-34

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: 127.06  E-value: 2.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   1 MIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 80
Cdd:cd07734  114 DIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 121-237 2.36e-31

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: 116.46  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818  121 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 199
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767904818  200 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 237
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 2-80 4.99e-23

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: 96.12  E-value: 4.99e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDeLEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 80
Cdd:cd16292  117 LEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 254-314 4.55e-15

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: 69.57  E-value: 4.55e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767904818  254 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 314
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 2-80 1.18e-14

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: 72.49  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818   2 IKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpNLLITE 79
Cdd:cd16295  119 VEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIME 196


                 .
gi 767904818  80 S 80
Cdd:cd16295  197 S 197
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 8-80 1.21e-13

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: 69.47  E-value: 1.21e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818   8 KVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--RPNLLITES 80
Cdd:cd16293  119 RITQLKYSQPVNLrgkGDGLTITAYNAGHTLGGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 8-77 1.21e-09

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 57.61  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904818    8 KVVAVHLHQTVQV---DDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--------RPNL 75
Cdd:pfam16661 111 KIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTA 190


                  ..
gi 767904818   76 LI 77
Cdd:pfam16661 191 LI 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-79 9.50e-04

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: 40.29  E-value: 9.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904818  15 HQTVQVDDeLEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 79
Cdd:cd07732  134 GKSFTIGD-FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-54 2.53e-03

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. 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: 293831  Cd Length: 160  Bit Score: 38.68  E-value: 2.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767904818   7 KKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKV-GSESVVYTGD 54
Cdd:cd16273   81 EYIVVLPMNTPVEIDGDVSVTLLDANHCPGAVMFLFELpDGRRILHTGD 129
 
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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