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Conserved domains on  [gi|359279877|ref|NP_001240660|]
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integrator complex subunit 9 isoform 2 [Mus musculus]

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; ...
 60-241 3.63e-79

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: 248.18  E-value: 3.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  60 CLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTMQIGRLLMEELVNfiervpkaqsaslwknkdiqr 139
Cdd:cd16294   32 CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 140 llpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLL 219
Cdd:cd16294   91 --------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVL 144

                        170       180
                 ....*....|....*....|..
gi 359279877 220 TTHPQPMDQASLKNSDVLILTG 241
Cdd:cd16294  145 TTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 283-401 6.01e-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: 97.23  E-value: 6.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877   283 DLLECLYQYIDSAGLSNIPFYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYRSIhgdfsND 362
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 359279877   363 FRQPCVLFTGHPSLRFGDVVHFMELWGKSSLNTIIFTEP 401
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 ...
 60-241 3.63e-79

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: 248.18  E-value: 3.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  60 CLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTMQIGRLLMEELVNfiervpkaqsaslwknkdiqr 139
Cdd:cd16294   32 CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 140 llpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLL 219
Cdd:cd16294   91 --------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVL 144

                        170       180
                 ....*....|....*....|..
gi 359279877 220 TTHPQPMDQASLKNSDVLILTG 241
Cdd:cd16294  145 TTHPQPMDQTSLKNSDVLILTG 166
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 283-401 6.01e-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: 97.23  E-value: 6.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877   283 DLLECLYQYIDSAGLSNIPFYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYRSIhgdfsND 362
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 359279877   363 FRQPCVLFTGHPSLRFGDVVHFMELWGKSSLNTIIFTEP 401
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 67-399 1.05e-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: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  67 IDLSTVDVILISnyHC----MMALPYITEHtGFTGTVYATEPTMQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllp 142
Cdd:COG1236   46 FRPSDVDAVVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE--------------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 143 sPLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SS 217
Cdd:COG1236  108 -PL------------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 218 LLTTHPQPMDQAslknsDVLIL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQ 290
Cdd:COG1236  173 PLLAPPEPVPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 291 YIDSAGLSNIPFYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKhyRSIhgdfsnDFRQPC 367
Cdd:COG1236  242 LKKEGRLPDIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEES--KAL------NRKGPA 304

                        330       340       350
                 ....*....|....*....|....*....|...
gi 359279877 368 VLFTGhPS-LRFGDVVHFMELWGKSSLNTIIFT 399
Cdd:COG1236  305 IIIAP-SGmLTGGRILHHLKRFLWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 29-238 5.61e-12

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 64.92  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877   29 PGWslkDGNAFLDKELKECSGHvfvdsvpefcLPETELIDLSTVDVILISNYhcMMALPYITEHTGFTGTVYATEPTMQI 108
Cdd:pfam16661  13 PGW---DGSFSYESDLKYLEKI----------LPEVDLILLSHPTLEHLGAY--PLLYYKFGSHLGSNIPVYATLPVANL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  109 GRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQLVGYSQKIELFGA---V 185
Cdd:pfam16661  78 GRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIKTLKYSQTVDLKGKfdgL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359279877  186 QVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVLI 238
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 ...
 283-400 2.88e-05

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: 43.66  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  283 DLLECLYQYIDSAGLSNIPFYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYRSIHGDFS-- 360
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 359279877  361 -NDFRQPCVLFTGHPSLRFGDVVHFMELWGKSSLNTIIFTE 400
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 ...
 60-241 3.63e-79

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: 248.18  E-value: 3.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  60 CLPETELIDLSTVDVILISNYHCMMALPYITEHTGFTGTVYATEPTMQIGRLLMEELVNfiervpkaqsaslwknkdiqr 139
Cdd:cd16294   32 CPPETELIDLSTVDVILISNYHCMLALPFITEYTGFTGVVYATEPTVQIGRLLMEELVQ--------------------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 140 llpsplkdavevstwrrcytmqevnsALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSGSSLL 219
Cdd:cd16294   91 --------------------------ALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYEKISYVSGSSVL 144

                        170       180
                 ....*....|....*....|..
gi 359279877 220 TTHPQPMDQASLKNSDVLILTG 241
Cdd:cd16294  145 TTHPQPMDQTSLKNSDVLILTG 166
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 57-241 3.12e-55

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: 186.00  E-value: 3.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  57 PEFCLPETELiDLSTVDVILISNYHCMM--ALPYITEHTGFTGTVYATEPTMQIGRLLMEELVNFIERVPKAQSaslwkn 134
Cdd:cd07734   36 PEACLPQFEL-LPPEIDAILISHFHLDHcgALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQS------ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 135 kdiqrllpsplkdavevstwrrCYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVS 214
Cdd:cd07734  109 ----------------------LYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTG 166

                        170       180
                 ....*....|....*....|....*..
gi 359279877 215 GSSLLTTHPQPMDQASLKNSDVLILTG 241
Cdd:cd07734  167 DFSNTEDRLLPAASILPPRPDLLITES 193
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 283-401 6.01e-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: 97.23  E-value: 6.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877   283 DLLECLYQYIDSAGLSNIPFYFISPVANSSLEFSQIFAEWLCHNKQSKVYLPEPPFPHAELIQTNKLKHYRSIhgdfsND 362
Cdd:smart01027   3 ELLLILEELWREGELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRNPFDFKNLKFVKSLEESKRL-----ND 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 359279877   363 FRQPCVLFTGHPSLRFGDVVHFMELWGKSSLNTIIFTEP 401
Cdd:smart01027  78 YKGPKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGY 116
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 60-204 9.29e-16

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: 76.08  E-value: 9.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  60 CLPETELIDLSTVDVILISNYH---CMmALPYITEHTGFTGTVYATEPTMQIGRLLMEELVnfieRVpkaqsaslwKNKD 136
Cdd:cd16292   41 SLPFFDEIDLSEIDLLLITHFHldhCG-ALPYFLQKTNFKGRVFMTHPTKAIYKWLLSDYV----RV---------SNIS 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359279877 137 IQRLLpsplkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGaVQVTPLSSGYALGSSNWIIQ 204
Cdd:cd16292  107 SDEML----------------YTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAMFMVE 157
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 70-212 9.82e-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: 76.02  E-value: 9.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  70 STVDVILIS--NYHCMMALPYITEHTGFTGTVYATEPTMQIGRLLMEELVnfiervpkaqsaslwknkdIQRLLPSPLKD 147
Cdd:cd16293   47 PTIDAVLLShpDLEHLGALPYLVGKLGLTCPVYATLPVHKMGRMFMYDLY-------------------QSRGLEEDFNL 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359279877 148 avevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGA---VQVTPLSSGYALGSSNWIIQSHYEKVSY 212
Cdd:cd16293  108 ----------FTLDDVDEAFDRITQLKYSQPVNLRGKgdgLTITAYNAGHTLGGTIWKITKDSEDIVY 165
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 67-399 1.05e-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: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  67 IDLSTVDVILISnyHC----MMALPYITEHtGFTGTVYATEPTMQIGRLLMEELVNFIERVPKAQsaslwknkdiqrllp 142
Cdd:COG1236   46 FRPSDVDAVVLT--HAhldhSGALPLLVKE-GFRGPIYATPATADLARILLGDSAKIQEEEAEAE--------------- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 143 sPLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELfGAVQVTPLSSGYALGSSNWIIQSHYEKVSYvSG-----SS 217
Cdd:COG1236  108 -PL------------YTEEDAERALELFQTVDYGEPFEI-GGVRVTFHPAGHILGSAQVELEVGGKRIVF-SGdygreDD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 218 LLTTHPQPMDQAslknsDVLIL--T-GLTQIPtaNPDGMVGEFCSNLALTVRNGGNVLVPCYPSG----VIYDllecLYQ 290
Cdd:COG1236  173 PLLAPPEPVPPA-----DVLITesTyGDRLHP--PREEVEAELAEWVRETLARGGTVLIPAFALGraqeLLYL----LRE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 291 YIDSAGLSNIPFYfISPVANsslEFSQIF---AEWLCHNKQSKVylpepPFPHAELIQTNKLKhyRSIhgdfsnDFRQPC 367
Cdd:COG1236  242 LKKEGRLPDIPIY-VSGMAI---RATEIYrrhGEYLRDEAQDPF-----ALPNLRFVTSVEES--KAL------NRKGPA 304

                        330       340       350
                 ....*....|....*....|....*....|...
gi 359279877 368 VLFTGhPS-LRFGDVVHFMELWGKSSLNTIIFT 399
Cdd:COG1236  305 IIIAP-SGmLTGGRILHHLKRFLWDPRNTILFV 336
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 29-238 5.61e-12

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 64.92  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877   29 PGWslkDGNAFLDKELKECSGHvfvdsvpefcLPETELIDLSTVDVILISNYhcMMALPYITEHTGFTGTVYATEPTMQI 108
Cdd:pfam16661  13 PGW---DGSFSYESDLKYLEKI----------LPEVDLILLSHPTLEHLGAY--PLLYYKFGSHLGSNIPVYATLPVANL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  109 GRLLMEElvnfiervpkaqsasLWKNKDIQRLLPSPLKDavevstwrrcytMQEVNSALSKIQLVGYSQKIELFGA---V 185
Cdd:pfam16661  78 GRVSTYD---------------LYASRGILGPYDSSELD------------LDDIDAAFDKIKTLKYSQTVDLKGKfdgL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359279877  186 QVTPLSSGYALGSSNWIIQSHYEKVSY-----------VSGSSLLTTHPQPMDQasLKNSDVLI 238
Cdd:pfam16661 131 TITPYNSGHTLGGTIWKISKNSEKIVYavdwnhtkdshLNGASLLDSTGKPLES--LVRPTALI 192
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 67-239 2.99e-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: 60.17  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  67 IDLSTVDVILISNYH---CMmALPYITEHtGFTGTVYATEPTMQIGRLLMEElvnfiervpkaqSASLWKnKDIQRLLPS 143
Cdd:cd16295   47 FDPKEIDAVILTHAHldhSG-RLPLLVKE-GFRGPIYATPATKDLAELLLLD------------SAKIQE-EEAEHPPAE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877 144 PLkdavevstwrrcYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSYVSG-----SSL 218
Cdd:cd16295  112 PL------------YTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSASVELEIGGGKRILFSGdlgrkNTP 179

                        170       180
                 ....*....|....*....|.
gi 359279877 219 LTTHPQPMDQAslknsDVLIL 239
Cdd:cd16295  180 LLRDPAPPPEA-----DYLIM 195
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 72-212 2.22e-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: 57.66  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  72 VDVILISNYH---CMmALPYITEHTGFTGTVYATEPTMQIGRLLMEELVnfiervpkaqsaslwknkdiqrllpsplKDA 148
Cdd:cd16291   56 IDCVIISHFHldhCG-ALPYFTEVVGYDGPIYMTHPTKAICPILLEDYR----------------------------KIA 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359279877 149 VEVSTWRRCYTMQEVNSALSKIQLVGYSQKIELFGAVQVTPLSSGYALGSSNWIIQSHYEKVSY 212
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 ...
 283-400 2.88e-05

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: 43.66  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279877  283 DLLECLYQYIDSAGLSNIPFYFISPVANSSLEFSQIFAEWLchnkqskvylpeppfphaeliqtNKLKHYRSIHGDFS-- 360
Cdd:pfam10996   3 ELLYLLDELWREGRLPKIPIYLDSPLAIKATEVYRRYPEYL-----------------------DDEARHFVISKSESka 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 359279877  361 -NDFRQPCVLFTGHPSLRFGDVVHFMELWGKSSLNTIIFTE 400
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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