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Conserved domains on  [gi|1622959823|ref|XP_028708352|]
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integrator complex subunit 9 isoform X4 [Macaca mulatta]

Protein Classification

integrator complex subunit 9( domain architecture ID 11039990)

integrator complex subunit 9 is a component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing

Gene Ontology:  GO:0032039|GO:0016180|GO:0005634
PubMed:  16239144

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-159 2.67e-62

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.


The actual alignment was detected with superfamily member cd16294:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 166  Bit Score: 201.96  E-value: 2.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   1 MMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrcytmqe 80
Cdd:cd16294    55 MLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ-------------------------------------------- 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622959823  81 vnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVLVLTG 159
Cdd:cd16294    91 ---ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 201-319 3.21e-24

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: 98.00  E-value: 3.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  201 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 280
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622959823  281 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 319
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
 
Name Accession Description Interval E-value
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 1-159 2.67e-62

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: 201.96  E-value: 2.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   1 MMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrcytmqe 80
Cdd:cd16294    55 MLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ-------------------------------------------- 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622959823  81 vnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVLVLTG 159
Cdd:cd16294    91 ---ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 201-319 3.21e-24

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: 98.00  E-value: 3.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  201 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 280
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622959823  281 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 319
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 3-317 4.91e-13

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 70.99  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllpsPLkdavevstwrrcYTMQEVN 82
Cdd:COG1236    66 ALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE----------------PL------------YTEEDAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  83 SALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SSLLTTHPQPMDQAslknsDVLVL 157
Cdd:COG1236   117 RALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDDPLLAPPEPVPPA-----DVLIT 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 158 --T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQYIDSAGLSSVPLYfISPVANss 230
Cdd:COG1236   190 esTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRELKKEGRLPDIPIY-VSGMAI-- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 231 lEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHypsihgdfSNDFRQPCVVFTGhPS-LRFGDVVHFMELW 306
Cdd:COG1236   261 -RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--------ALNRKGPAIIIAP-SGmLTGGRILHHLKRF 325

                         330
                  ....*....|.
gi 1622959823 307 GKSSLNTVIFT 317
Cdd:COG1236   326 LWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 10-156 1.50e-08

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 54.91  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  10 HTGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQ 89
Cdd:pfam16661  61 HLGSNIPVYATLPVANLGRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  90 LVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVL 155
Cdd:pfam16661 114 TLKYSQTVDLKGKfdgLTITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES--LVRPTAL 191


                  .
gi 1622959823 156 V 156
Cdd:pfam16661 192 I 192
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 201-318 7.94e-06

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: 44.81  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 201 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 278
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622959823 279 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 318
Cdd:pfam10996  60 iNEGKGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTG 100
 
Name Accession Description Interval E-value
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 1-159 2.67e-62

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: 201.96  E-value: 2.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   1 MMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrcytmqe 80
Cdd:cd16294    55 MLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ-------------------------------------------- 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622959823  81 vnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVLVLTG 159
Cdd:cd16294    91 ---ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVLILTG 166
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 3-159 1.12e-44

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: 156.34  E-value: 1.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQSaslwknkdiqrllpsplkdavevstwrrCYTMQEVN 82
Cdd:cd07734    65 ALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQS----------------------------LYTPEDIE 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622959823  83 SALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVLVLTG 159
Cdd:cd07734   117 EALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 201-319 3.21e-24

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: 98.00  E-value: 3.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  201 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 280
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622959823  281 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 319
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 3-317 4.91e-13

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 70.99  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllpsPLkdavevstwrrcYTMQEVN 82
Cdd:COG1236    66 ALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE----------------PL------------YTEEDAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  83 SALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SSLLTTHPQPMDQAslknsDVLVL 157
Cdd:COG1236   117 RALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDDPLLAPPEPVPPA-----DVLIT 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 158 --T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQYIDSAGLSSVPLYfISPVANss 230
Cdd:COG1236   190 esTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRELKKEGRLPDIPIY-VSGMAI-- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 231 lEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHypsihgdfSNDFRQPCVVFTGhPS-LRFGDVVHFMELW 306
Cdd:COG1236   261 -RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--------ALNRKGPAIIIAP-SGmLTGGRILHHLKRF 325

                         330
                  ....*....|.
gi 1622959823 307 GKSSLNTVIFT 317
Cdd:COG1236   326 LWDPRNTILFV 336
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 3-130 1.20e-12

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: 66.78  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdIQRLLPSPLKDavevstwrrcYTMQEVN 82
Cdd:cd16293    64 ALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLY-------------------QSRGLEEDFNL----------FTLDDVD 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622959823  83 SALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY 130
Cdd:cd16293   115 EAFDRITQLKYSQPVNLRGKgdgLTITAYNAGHTLGGTIWKITKDSEDIVY 165
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 3-122 1.08e-08

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: 55.28  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfieRVpkaqsaslwKNKDIQRLLpsplkdavevstwrrcYTMQEVN 82
Cdd:cd16292    68 ALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYV----RV---------SNISSDEML----------------YTETDLE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622959823  83 SALSKIQLVGYSQKIELFGaVQVTPLSSGYALGSSNWIIQ 122
Cdd:cd16292   119 ASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVE 157
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 10-156 1.50e-08

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 54.91  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  10 HTGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQ 89
Cdd:pfam16661  61 HLGSNIPVYATLPVANLGRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  90 LVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVL 155
Cdd:pfam16661 114 TLKYSQTVDLKGKfdgLTITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES--LVRPTAL 191


                  .
gi 1622959823 156 V 156
Cdd:pfam16661 192 I 192
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-157 7.47e-08

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: 52.85  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHtGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqSASLWKnKDIQRLLPSPLkdavevstwrrcYTMQEVN 82
Cdd:cd16295    67 RLPLLVKE-GFRGPIYATPATKDLAELLLLD------------SAKIQE-EEAEHPPAEPL------------YTEEDVE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823  83 SALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSG-----SSLLTTHPQPMDQAslknsDVLVL 157
Cdd:cd16295   121 KALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGKRILFSGdlgrkNTPLLRDPAPPPEA-----DYLIM 195
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 3-130 5.97e-07

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: 50.34  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823   3 ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdiqrllpsplKDAVEVSTWRRCYTMQEVN 82
Cdd:cd16291    71 ALPYFTEVVGYDGPIYMTHPTKAICPILLEDYR----------------------------KIAVERKGETNFFTSQMIK 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622959823  83 SALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSY 130
Cdd:cd16291   123 DCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVY 170
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 201-318 7.94e-06

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: 44.81  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622959823 201 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 278
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622959823 279 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 318
Cdd:pfam10996  60 iNEGKGPKVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTG 100
 
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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