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Conserved domains on  [gi|374253826|ref|NP_001243391|]
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integrator complex subunit 11 isoform 4 [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
COG1782 super family cl34358
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 39-348 1.59e-71

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


The actual alignment was detected with superfamily member COG1782:

Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 234.64  E-value: 1.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  39 FHVLPHG----VNDELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTI 112
Cdd:COG1782  137 FITLDYGevtdIAPDIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 113 RDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQK 191
Cdd:COG1782  216 HPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 192 IRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 265
Cdd:COG1782  296 LRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRL 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 266 LSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPAN 342
Cdd:COG1782  376 LDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPEN 454


                 ....*.
gi 374253826 343 GETVTL 348
Cdd:COG1782  455 LETIRL 460
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 39-348 1.59e-71

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: 234.64  E-value: 1.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  39 FHVLPHG----VNDELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTI 112
Cdd:COG1782  137 FITLDYGevtdIAPDIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 113 RDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQK 191
Cdd:COG1782  216 HPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 192 IRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 265
Cdd:COG1782  296 LRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRL 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 266 LSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPAN 342
Cdd:COG1782  376 LDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPEN 454


                 ....*.
gi 374253826 343 GETVTL 348
Cdd:COG1782  455 LETIRL 460
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 147-265 8.45e-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: 150.77  E-value: 8.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826   147 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 219
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253826   220 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 265
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 46-106 8.96e-41

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: 145.10  E-value: 8.96e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253826  46 VNDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 106
Cdd:cd16291  139 VDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 147-263 2.84e-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: 2.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  147 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 225
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253826  226 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 263
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
 
Name Accession Description Interval E-value
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 39-348 1.59e-71

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: 234.64  E-value: 1.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  39 FHVLPHG----VNDELEIKAYYAGHVLGAAMFQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPNLLITESTYATTI 112
Cdd:COG1782  137 FITLDYGevtdIAPDIKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 113 RDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQK 191
Cdd:COG1782  216 HPSREEAEEELAKVINETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 192 IRKT-FVQRNMFEFKHIKAFD-----RAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 265
Cdd:COG1782  296 LRDLiFKGENPFLFENLHYVEsveesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRL 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 266 LSGQRKLEMEGRQVlEVKMQVEYM-SFSAHADAKGIMQLVGQAE--PESVLLVHGEAKKMEFLKQKIEQELRVNCYMPAN 342
Cdd:COG1782  376 LDGAKEVKIFGETI-PVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPEN 454


                 ....*.
gi 374253826 343 GETVTL 348
Cdd:COG1782  455 LETIRL 460
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 48-318 3.13e-71

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 232.00  E-value: 3.13e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  48 DELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpNLLITESTYATTIRDSKRCRERDFLKK 126
Cdd:COG1236  134 GGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEW 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 127 VHETVERGGKVLIPVFALGRAQE-LCILLETFWERMNLKVPIYFStGLTEKANHYYKLFIPWTNQKIrktfvqRNMFEFK 205
Cdd:COG1236  212 VRETLARGGTVLIPAFALGRAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALP 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826 206 HIK----AFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVlE 281
Cdd:COG1236  285 NLRfvtsVEESKALNRKGPAIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGEEV-P 363

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 374253826 282 VKMQVE-YMSFSAHADAKGIMQLVGQAE-PESVLLVHGE 318
Cdd:COG1236  364 VRARVErLFGLSAHADWDELLEWIKATGkPERVFLVHGE 402
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 147-265 8.45e-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: 150.77  E-value: 8.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826   147 AQELCILLETFWERMNL-KVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RAFADNPG 219
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 374253826   220 PMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKI 265
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 46-106 8.96e-41

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: 145.10  E-value: 8.96e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253826  46 VNDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 106
Cdd:cd16291  139 VDDELEIKAYYAGHVLGAAMFYVRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 147-263 2.84e-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: 2.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  147 AQELCILLETFWER-MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKtfvqrnmfeFKHIKAFDRAFADNPGPMVVFA 225
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARH---------FVISKSESKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 374253826  226 TPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGH 263
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 46-106 7.27e-25

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: 101.64  E-value: 7.27e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253826  46 VNDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 106
Cdd:cd07734  133 LFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 51-106 1.31e-17

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: 81.09  E-value: 1.31e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 374253826  51 EIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITES 106
Cdd:cd16292  139 KFTAYNAGHVLGAAMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 280-340 2.79e-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: 70.34  E-value: 2.79e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253826  280 LEVKMQVEYMS-FSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMP 340
Cdd:pfam07521   2 IPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 40-106 7.09e-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: 67.55  E-value: 7.09e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253826  40 HVLPHGVNDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--RPNLLITES 106
Cdd:cd16293  128 PVNLRGKGDGLTITAYNAGHTLGGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 39-106 6.65e-10

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: 58.62  E-value: 6.65e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253826  39 FHVLPHG----VNDELEIKAYYAGHVLGAAMFQIKVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpNLLITES 106
Cdd:cd16295  126 FRPVEYGepfeIGPGVKVTFYDAGHILGSASVELEIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIMES 197
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 44-103 3.16e-09

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 56.45  E-value: 3.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374253826   44 HGVNDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--------RPNLLI 103
Cdd:pfam16661 124 KGKFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-105 9.23e-03

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: 37.59  E-value: 9.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374253826  49 ELEIKAYYAGH-VLGAAMFQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PNLLITE 105
Cdd:cd07732  141 DFTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
 
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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