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Conserved domains on  [gi|223555970|ref|NP_001138631|]
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integrator complex subunit 9 isoform 2 [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 ...
1-244 2.74e-95

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: 289.78  E-value: 2.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnaFLDKTELIDLSTVDVILI 80
Cdd:cd16294    1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD-------------------------------CPPETELIDLSTVDVILI 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  81 SNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrc 160
Cdd:cd16294   50 SNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 161 ytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVL 240
Cdd:cd16294   91 --------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVL 162

                 ....
gi 223555970 241 VLTG 244
Cdd:cd16294  163 ILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
286-404 4.18e-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: 97.61  E-value: 4.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   286 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 365
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 223555970   366 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 404
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 ...
1-244 2.74e-95

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: 289.78  E-value: 2.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnaFLDKTELIDLSTVDVILI 80
Cdd:cd16294    1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD-------------------------------CPPETELIDLSTVDVILI 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  81 SNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrc 160
Cdd:cd16294   50 SNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 161 ytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVL 240
Cdd:cd16294   91 --------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVL 162

                 ....
gi 223555970 241 VLTG 244
Cdd:cd16294  163 ILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
286-404 4.18e-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: 97.61  E-value: 4.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   286 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 365
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 223555970   366 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 404
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
1-402 2.91e-17

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 84.47  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   1 MKLYCL--SGHPTLPCNVLKFKSTTIMLDCGLDMTST-LNFLPLPlvqsprlsnlpgwslkdgnafldktelIDLSTVDV 77
Cdd:COG1236    1 MKLTFLgaAGEVTGSCYLLETGGTRILIDCGLFQGGKeRNWPPFP---------------------------FRPSDVDA 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  78 ILISnyHC----MMALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllpsPLkdave 153
Cdd:COG1236   54 VVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE----------------PL----- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 154 vstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SSLLTTHPQP 228
Cdd:COG1236  110 -------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDDPLLAPPEP 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 229 MDQAslknsDVLVL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQYIDSAGLS 301
Cdd:COG1236  181 VPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRELKKEGRLP 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 302 SVPLYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHypsihgdfSNDFRQPCVVFTGhPS 378
Cdd:COG1236  250 DIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--------ALNRKGPAIIIAP-SG 311
                        410       420
                 ....*....|....*....|....*
gi 223555970 379 -LRFGDVVHFMELWGKSSLNTVIFT 402
Cdd:COG1236  312 mLTGGRILHHLKRFLWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
16-241 2.93e-12

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 65.69  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   16 VLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkDGNAFLDKTELID--LSTVDVILISnyH----CMMAL 89
Cdd:pfam16661   1 LLEFDNVRILLDPGWD---------------------------GSFSYESDLKYLEkiLPEVDLILLS--HptleHLGAY 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   90 PYI----TEHTGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQE 165
Cdd:pfam16661  52 PLLyykfGSHLGSNIPVYATLPVANLGRVSTYD---------------LYASRGILGPYDSSELD------------LDD 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  166 VNSALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQ 231
Cdd:pfam16661 105 IDAAFDKIKTLKYSQTVDLKGKfdgLTITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES 184
                         250
                  ....*....|
gi 223555970  232 asLKNSDVLV 241
Cdd:pfam16661 185 --LVRPTALI 192
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
286-403 9.29e-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: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  286 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 363
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 223555970  364 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 403
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 ...
1-244 2.74e-95

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: 289.78  E-value: 2.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkdgnaFLDKTELIDLSTVDVILI 80
Cdd:cd16294    1 MKLYCLSGHPTLPCNVLKFKSTTIMLDCGLD-------------------------------CPPETELIDLSTVDVILI 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  81 SNYHCMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNfiervpkaqsaslwknkdiqrllpsplkdavevstwrrc 160
Cdd:cd16294   50 SNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 161 ytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDVL 240
Cdd:cd16294   91 --------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVLTTHPQPMDQTSLKNSDVL 162

                 ....
gi 223555970 241 VLTG 244
Cdd:cd16294  163 ILTG 166
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
2-244 4.71e-66

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: 214.89  E-value: 4.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   2 KLYCLSGHPTLPCNVLKFKSTTIMLDCGLDMTSTLNFLPLPlvqsprlsnlpgwslkdgnafldKTELiDLSTVDVILIS 81
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDPEACLP-----------------------QFEL-LPPEIDAILIS 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  82 NYHCMM--ALPYITEHTGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQSaslwknkdiqrllpsplkdavevstwrr 159
Cdd:cd07734   57 HFHLDHcgALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQS---------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 160 CYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLLTTHPQPMDQASLKNSDV 239
Cdd:cd07734  109 LYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDL 188

                 ....*
gi 223555970 240 LVLTG 244
Cdd:cd07734  189 LITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
286-404 4.18e-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: 97.61  E-value: 4.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   286 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYPSIhgdfsND 365
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 223555970   366 FRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTEP 404
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
14-207 5.03e-21

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: 91.11  E-value: 5.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  14 CNVLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlPGWSLKDGNAFLDkteLIDLSTVDVILISNYH---CMmALP 90
Cdd:cd16292   16 CVILEFKGKTIMLDCGIH---------------------PGYSGLASLPFFD---EIDLSEIDLLLITHFHldhCG-ALP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  91 YITEHTGFTGTVYATEPTVQIGRLLMEELVnfieRVpkaqsaslwKNKDIQRLLpsplkdavevstwrrcYTMQEVNSAL 170
Cdd:cd16292   71 YFLQKTNFKGRVFMTHPTKAIYKWLLSDYV----RV---------SNISSDEML----------------YTETDLEASM 121
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 223555970 171 SKIQLVGYSQKIELFGaVQVTPLSSGYALGSSNWIIQ 207
Cdd:cd16292  122 DKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVE 157
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
7-215 4.98e-18

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: 82.57  E-value: 4.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   7 SGHPtlPCNVLKFKSTTIMLDCGldmtstlnflplplvqsprlsnlpgWSLKDGNAFLDKTELIdLSTVDVILIS--NYH 84
Cdd:cd16293    9 DESP--LCYLLEIDDVTILLDCG-------------------------WDESFDMEYLESLKRI-APTIDAVLLShpDLE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  85 CMMALPYITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdIQRLLPSPLKDavevstwrrcYTMQ 164
Cdd:cd16293   61 HLGALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLY-------------------QSRGLEEDFNL----------FTLD 111
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223555970 165 EVNSALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY 215
Cdd:cd16293  112 DVDEAFDRITQLKYSQPVNLRGKgdgLTITAYNAGHTLGGTIWKITKDSEDIVY 165
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
1-402 2.91e-17

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 84.47  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   1 MKLYCL--SGHPTLPCNVLKFKSTTIMLDCGLDMTST-LNFLPLPlvqsprlsnlpgwslkdgnafldktelIDLSTVDV 77
Cdd:COG1236    1 MKLTFLgaAGEVTGSCYLLETGGTRILIDCGLFQGGKeRNWPPFP---------------------------FRPSDVDA 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  78 ILISnyHC----MMALPYITEHtGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllpsPLkdave 153
Cdd:COG1236   54 VVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE----------------PL----- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 154 vstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SSLLTTHPQP 228
Cdd:COG1236  110 -------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDDPLLAPPEP 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 229 MDQAslknsDVLVL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQYIDSAGLS 301
Cdd:COG1236  181 VPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRELKKEGRLP 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 302 SVPLYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKHypsihgdfSNDFRQPCVVFTGhPS 378
Cdd:COG1236  250 DIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEESK--------ALNRKGPAIIIAP-SG 311
                        410       420
                 ....*....|....*....|....*
gi 223555970 379 -LRFGDVVHFMELWGKSSLNTVIFT 402
Cdd:COG1236  312 mLTGGRILHHLKRFLWDPRNTILFV 336
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
14-242 1.76e-13

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: 69.41  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  14 CNVLKFKSTTIMLDCGL----DMTSTLNFLPLPlvqsprlsnlpgwslkdgnafldktelIDLSTVDVILISNYH---CM 86
Cdd:cd16295   14 CYLLETGGKRILLDCGLfqggKELEELNNEPFP---------------------------FDPKEIDAVILTHAHldhSG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  87 mALPYITEHtGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqSASLWKnKDIQRLLPSPLkdavevstwrrcYTMQEV 166
Cdd:cd16295   67 -RLPLLVKE-GFRGPIYATPATKDLAELLLLD------------SAKIQE-EEAEHPPAEPL------------YTEEDV 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970 167 NSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSG-----SSLLTTHPQPMDQAslknsDVLV 241
Cdd:cd16295  120 EKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGKRILFSGdlgrkNTPLLRDPAPPPEA-----DYLI 194

                 .
gi 223555970 242 L 242
Cdd:cd16295  195 M 195
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
16-241 2.93e-12

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 65.69  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   16 VLKFKSTTIMLDCGLDmtstlnflplplvqsprlsnlpgwslkDGNAFLDKTELID--LSTVDVILISnyH----CMMAL 89
Cdd:pfam16661   1 LLEFDNVRILLDPGWD---------------------------GSFSYESDLKYLEkiLPEVDLILLS--HptleHLGAY 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970   90 PYI----TEHTGFTGTVYATEPTVQIGRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQE 165
Cdd:pfam16661  52 PLLyykfGSHLGSNIPVYATLPVANLGRVSTYD---------------LYASRGILGPYDSSELD------------LDD 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  166 VNSALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQ 231
Cdd:pfam16661 105 IDAAFDKIKTLKYSQTVDLKGKfdgLTITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES 184
                         250
                  ....*....|
gi 223555970  232 asLKNSDVLV 241
Cdd:pfam16661 185 --LVRPTALI 192
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
14-215 6.48e-11

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: 61.89  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  14 CNVLKFKSTTIMLDCGLDMTSTlnflplplvQSPRLsnlPGWSLKDGNAflDKTELIDlstvdVILISNYH---CMmALP 90
Cdd:cd16291   14 CILVTIGGKNIMFDCGMHMGYN---------DERRF---PDFSYISQNG--PFTEHID-----CVIISHFHldhCG-ALP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  91 YITEHTGFTGTVYATEPTVQIGRLLMEELVnfiervpkaqsaslwknkdiqrllpsplKDAVEVSTWRRCYTMQEVNSAL 170
Cdd:cd16291   74 YFTEVVGYDGPIYMTHPTKAICPILLEDYR----------------------------KIAVERKGETNFFTSQMIKDCM 125
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 223555970 171 SKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSY 215
Cdd:cd16291  126 KKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFYVRVGDESVVY 170
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
286-403 9.29e-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: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223555970  286 DLLECLYQYIDSAGLSSVPLYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYPSIHGDFS-- 363
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 223555970  364 -NDFRQPCVVFTGHPSLRFGDVVHFMELWGKSSLNTVIFTE 403
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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