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Conserved domains on  [gi|1386876293|ref|NP_001349967|]
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integrator complex subunit 9 isoform 4 [Homo sapiens]

Protein Classification

integrator complex subunit 9( domain architecture ID 10888785)

integrator complex subunit 9 is part of the complex that is 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

Graphical summary

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List of domain hits

 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 ...
 1-265 3.97e-94

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: 287.85  E-value: 3.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnafldkelkecsghvfvdsv 80
Cdd:cd16294     1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  81 pefCLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkd 160
Cdd:cd16294    32 ---CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ------------------ 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 161 iqrllpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGS 240
Cdd:cd16294    91 -----------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGS 141

                         250       260
                  ....*....|....*....|....*
gi 1386876293 241 SLLTTHPQPMDQASLKNSDVLVLTG 265
Cdd:cd16294   142 SVLTTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 307-425 4.01e-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: 4.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  307 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 386
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1386876293  387 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 425
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 ...
 1-265 3.97e-94

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: 287.85  E-value: 3.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnafldkelkecsghvfvdsv 80
Cdd:cd16294     1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  81 pefCLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkd 160
Cdd:cd16294    32 ---CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ------------------ 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 161 iqrllpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGS 240
Cdd:cd16294    91 -----------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGS 141

                         250       260
                  ....*....|....*....|....*
gi 1386876293 241 SLLTTHPQPMDQASLKNSDVLVLTG 265
Cdd:cd16294   142 SVLTTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 307-425 4.01e-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: 4.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  307 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 386
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1386876293  387 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 425
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-423 1.37e-14

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 76.38  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   1 MKLYCL--SGHPTLPCNVLKFKSTTIMLDCGLDMTST-LNFLPLPlvqsprlsnlpgwslkdgnafldkelkecsghvfv 77
Cdd:COG1236     1 MKLTFLgaAGEVTGSCYLLETGGTRILIDCGLFQGGKeRNWPPFP----------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  78 dsvpefclpetelIDLSTVDVILISnyHC----MMALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsa 153
Cdd:COG1236    46 -------------FRPSDVDAVVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE-- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 154 slwknkdiqrllpsPLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEK 233
Cdd:COG1236   108 --------------PL------------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKR 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 234 VSYvSG-----SSLLTTHPQPMDQAslknsDVLVL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG-- 303
Cdd:COG1236   161 IVF-SGdygreDDPLLAPPEPVPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGra 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 304 --VIYDllecLYQYIDSAGLSSVPLYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHyps 378
Cdd:COG1236   233 qeLLYL----LRELKKEGRLPDIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--- 296

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1386876293 379 ihgdfSNDFRQPCVVFTGhPS-LRFGDVVHFMELWGKSSLNTVIFT 423
Cdd:COG1236   297 -----ALNRKGPAIIIAP-SGmLTGGRILHHLKRFLWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 53-262 3.03e-11

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 63.00  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  53 PGWslkDGNAFLDKELKECSGHvfvdsvpefcLPETELIDLSTVDVILISNYhcMMALPYITEHTGFTGTVYATEPTVQI 132
Cdd:pfam16661  13 PGW---DGSFSYESDLKYLEKI----------LPEVDLILLSHPTLEHLGAY--PLLYYKFGSHLGSNIPVYATLPVANL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 133 GRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQLVGYSQKIELFGA---V 209
Cdd:pfam16661  78 GRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIKTLKYSQTVDLKGKfdgL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876293 210 QVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVLV 262
Cdd:pfam16661 131 TITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES--LVRPTALI 192
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 307-424 9.26e-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: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 307 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 384
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1386876293 385 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 424
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 ...
 1-265 3.97e-94

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: 287.85  E-value: 3.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnafldkelkecsghvfvdsv 80
Cdd:cd16294     1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  81 pefCLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkd 160
Cdd:cd16294    32 ---CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ------------------ 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 161 iqrllpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGS 240
Cdd:cd16294    91 -----------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGS 141

                         250       260
                  ....*....|....*....|....*
gi 1386876293 241 SLLTTHPQPMDQASLKNSDVLVLTG 265
Cdd:cd16294   142 SVLTTHPQPMDQTSLKNSDVLILTG 166
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 2-265 4.47e-65

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: 212.96  E-value: 4.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   2 KLYCLSGHPTLPCNVLKFKSTTIMLDCGLDMTSTLnflplplvqsprlsnlpgwslkdgnafldkelkecsghvfvdsvP 81
Cdd:cd07734     1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKED--------------------------------------------P 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  82 EFCLPETELiDLSTVDVILISNYHCMM--ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQSaslwknk 159
Cdd:cd07734    37 EACLPQFEL-LPPEIDAILISHFHLDHcgALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQS------- 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 160 diqrllpsplkdavevstwrrCYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSG 239
Cdd:cd07734   109 ---------------------LYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGD 167

                         250       260
                  ....*....|....*....|....*.
gi 1386876293 240 SSLLTTHPQPMDQASLKNSDVLVLTG 265
Cdd:cd07734   168 FSNTEDRLLPAASILPPRPDLLITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 307-425 4.01e-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: 4.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  307 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 386
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1386876293  387 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 425
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 14-228 1.03e-18

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: 84.56  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  14 CNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlPGWSlkdgnafldkelkecsGHvfvDSVPEFclpetELIDL 93
Cdd:cd16292    16 CVILEFKGKTIMLDCGIH---------------------PGYS----------------GL---ASLPFF-----DEIDL 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  94 STVDVILISNYH---CMmALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfieRVpkaqsaslwKNKDIQRLLpsplk 170
Cdd:cd16292    51 SEIDLLLITHFHldhCG-ALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYV----RV---------SNISSDEML----- 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876293 171 davevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGaVQVTPLSSGYALGSSNWIIQ 228
Cdd:cd16292   112 -----------YTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVE 157
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-236 3.72e-16

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: 77.56  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   7 SGHPtlPCNVLKFKSTTIMLDCGldmtstlnflplplvqsprlsnlpgWSLKDGNAFLDkELKECsghvfvdsvpefclp 86
Cdd:cd16293     9 DESP--LCYLLEIDDVTILLDCG-------------------------WDESFDMEYLE-SLKRI--------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  87 etelidLSTVDVILIS--NYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdIQRL 164
Cdd:cd16293    46 ------APTIDAVLLShpDLEHLGALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLY-------------------QSRG 100

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876293 165 LPSPLKDavevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY 236
Cdd:cd16293   101 LEEDFNL----------FTLDDVDEAFDRITQLKYSQPVNLRGKgdgLTITAYNAGHTLGGTIWKITKDSEDIVY 165
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-423 1.37e-14

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 76.38  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293   1 MKLYCL--SGHPTLPCNVLKFKSTTIMLDCGLDMTST-LNFLPLPlvqsprlsnlpgwslkdgnafldkelkecsghvfv 77
Cdd:COG1236     1 MKLTFLgaAGEVTGSCYLLETGGTRILIDCGLFQGGKeRNWPPFP----------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  78 dsvpefclpetelIDLSTVDVILISnyHC----MMALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsa 153
Cdd:COG1236    46 -------------FRPSDVDAVVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE-- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 154 slwknkdiqrllpsPLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEK 233
Cdd:COG1236   108 --------------PL------------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKR 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 234 VSYvSG-----SSLLTTHPQPMDQAslknsDVLVL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG-- 303
Cdd:COG1236   161 IVF-SGdygreDDPLLAPPEPVPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGra 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 304 --VIYDllecLYQYIDSAGLSSVPLYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHyps 378
Cdd:COG1236   233 qeLLYL----LRELKKEGRLPDIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--- 296

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1386876293 379 ihgdfSNDFRQPCVVFTGhPS-LRFGDVVHFMELWGKSSLNTVIFT 423
Cdd:COG1236   297 -----ALNRKGPAIIIAP-SGmLTGGRILHHLKRFLWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 53-262 3.03e-11

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 63.00  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  53 PGWslkDGNAFLDKELKECSGHvfvdsvpefcLPETELIDLSTVDVILISNYhcMMALPYITEHTGFTGTVYATEPTVQI 132
Cdd:pfam16661  13 PGW---DGSFSYESDLKYLEKI----------LPEVDLILLSHPTLEHLGAY--PLLYYKFGSHLGSNIPVYATLPVANL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 133 GRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQLVGYSQKIELFGA---V 209
Cdd:pfam16661  78 GRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIKTLKYSQTVDLKGKfdgL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876293 210 QVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVLV 262
Cdd:pfam16661 131 TITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES--LVRPTALI 192
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 14-263 1.07e-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: 61.32  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  14 CNVLKFKSTTIMLDCGL----DMTSTLNFLPLPlvqsprlsnlpgwslkdgnafldkelkecsghvfvdsvpefclpete 89
Cdd:cd16295    14 CYLLETGGKRILLDCGLfqggKELEELNNEPFP----------------------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  90 lIDLSTVDVILISNYH---CMmALPYITEHtGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqSASLWKnKDIQRLLP 166
Cdd:cd16295    47 -FDPKEIDAVILTHAHldhSG-RLPLLVKE-GFRGPIYATPATKDLAELLLLD------------SAKIQE-EEAEHPPA 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 167 SPLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSG-----SS 241
Cdd:cd16295   111 EPL------------YTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGKRILFSGdlgrkNT 178

                         250       260
                  ....*....|....*....|..
gi 1386876293 242 LLTTHPQPMDQAslknsDVLVL 263
Cdd:cd16295   179 PLLRDPAPPPEA-----DYLIM 195
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 96-236 3.34e-09

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: 57.27  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293  96 VDVILISNYH---CMmALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdiqrllpsplKDA 172
Cdd:cd16291    56 IDCVIISHFHldhCG-ALPYFTEVVGYDGPIYMTHPTKAICPILLEDYR----------------------------KIA 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876293 173 VEVSTWRRCYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSY 236
Cdd:cd16291   107 VERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVY 170
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 307-424 9.26e-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: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876293 307 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 384
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1386876293 385 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 424
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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