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Conserved domains on  [gi|1835468989|ref|XP_033767887|]
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Cft2 [Saccharomyces paradoxus]

Protein Classification

integrator complex subunit 9( domain architecture ID 11244932)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 19-211 2.55e-104

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


:

Pssm-ID: 406948  Cd Length: 192  Bit Score: 320.31  E-value: 2.55e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  19 VVRFDNVTLLIDPGWNPSKvSYEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYNFTSHFISRIQVYATLPVINLGR 98
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSF-SYESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYKFGSHLGSNIPVYATLPVANLGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  99 VSTIDSYASSGVIGPYDTNELDLEDIEKSFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWCISTYSEKLVYAK 178
Cdd:pfam16661  80 VSTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLKGKFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835468989 179 RWNHTRDNILNAASILDATGKPLSTLMRPSAII 211
Cdd:pfam16661 160 DWNHTKDSHLNGASLLDSTGKPLESLVRPTALI 192
CPSF100_C super family cl16218
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 736-860 1.84e-21

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


The actual alignment was detected with superfamily member pfam13299:

Pssm-ID: 463836  Cd Length: 162  Bit Score: 91.94  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989 736 DNL---LKWQRISDsYTVATVVGRLV-------------------------------KESLPQVNNHQKTASRSKLVLKP 781
Cdd:pfam13299   5 DSLvssLKWQKVRG-LEVAWVTGRLDraaleegaaeeeeeeedeeeenankkqkleqFSLKDDDEKESKESKDSIPTLDP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835468989 782 LGGSSRSHKTGALSIGDVRLVQLKKQLMEKNYIAEFKGEGTLVINEKVAVRKINDAETIIDGTPSELFDTVKKLVTDML 860
Cdd:pfam13299  84 LPSNLAPAVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGEGTLVCNGTVAVRKTETGRIEIEGVGGPTFYAVRRLIYEQL 162
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 254-372 1.09e-11

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: 62.56  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  254 FLDLFTQVHELLFEstkiNAHTQVPVLILSYARGRTLTYAKSMLEWLSPSLLKTWENRNNtsPFEIGSRIKIIAPNE--- 330
Cdd:smart01027   1 TQELLLILEELWRE----GELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRN--PFDFKNLKFVKSLEEskr 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835468989  331 LSKYPGSKICFVSEVEA---LINEVITKVGNSEKTTLIFTKPSFE 372
Cdd:smart01027  75 LNDYKGPKVIIASSGMLtggRSRHYLKRLAPDPRNTVILTGYQAE 119
 
Name Accession Description Interval E-value
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 19-211 2.55e-104

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 320.31  E-value: 2.55e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  19 VVRFDNVTLLIDPGWNPSKvSYEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYNFTSHFISRIQVYATLPVINLGR 98
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSF-SYESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYKFGSHLGSNIPVYATLPVANLGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  99 VSTIDSYASSGVIGPYDTNELDLEDIEKSFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWCISTYSEKLVYAK 178
Cdd:pfam16661  80 VSTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLKGKFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835468989 179 RWNHTRDNILNAASILDATGKPLSTLMRPSAII 211
Cdd:pfam16661 160 DWNHTKDSHLNGASLLDSTGKPLESLVRPTALI 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-216 9.61e-88

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: 277.09  E-value: 9.61e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989   7 CCDDGSGTTVGSVVRFDNVTLLIDPGWNPSKVsyEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYnftsHFISRIQ 86
Cdd:cd16293     4 LSGAGDESPLCYLLEIDDVTILLDCGWDESFD--MEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVG----KLGLTCP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  87 VYATLPVINLGRVSTIDSYASSGVIGPYdtNELDLEDIEKSFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWC 166
Cdd:cd16293    78 VYATLPVHKMGRMFMYDLYQSRGLEEDF--NLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTITAYNAGHTLGGTIWK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835468989 167 ISTYSEKLVYAKRWNHTRDNILNAASILDATGkplstlMRPSAIITTLDK 216
Cdd:cd16293   156 ITKDSEDIVYAVDWNHKKERHLNGAVLDSFGG------LRPSLLITDADN 199
CPSF100_C pfam13299
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 736-860 1.84e-21

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


Pssm-ID: 463836  Cd Length: 162  Bit Score: 91.94  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989 736 DNL---LKWQRISDsYTVATVVGRLV-------------------------------KESLPQVNNHQKTASRSKLVLKP 781
Cdd:pfam13299   5 DSLvssLKWQKVRG-LEVAWVTGRLDraaleegaaeeeeeeedeeeenankkqkleqFSLKDDDEKESKESKDSIPTLDP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835468989 782 LGGSSRSHKTGALSIGDVRLVQLKKQLMEKNYIAEFKGEGTLVINEKVAVRKINDAETIIDGTPSELFDTVKKLVTDML 860
Cdd:pfam13299  84 LPSNLAPAVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGEGTLVCNGTVAVRKTETGRIEIEGVGGPTFYAVRRLIYEQL 162
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 254-372 1.09e-11

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: 62.56  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  254 FLDLFTQVHELLFEstkiNAHTQVPVLILSYARGRTLTYAKSMLEWLSPSLLKTWENRNNtsPFEIGSRIKIIAPNE--- 330
Cdd:smart01027   1 TQELLLILEELWRE----GELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRN--PFDFKNLKFVKSLEEskr 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835468989  331 LSKYPGSKICFVSEVEA---LINEVITKVGNSEKTTLIFTKPSFE 372
Cdd:smart01027  75 LNDYKGPKVIIASSGMLtggRSRHYLKRLAPDPRNTVILTGYQAE 119
 
Name Accession Description Interval E-value
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 19-211 2.55e-104

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 320.31  E-value: 2.55e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  19 VVRFDNVTLLIDPGWNPSKvSYEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYNFTSHFISRIQVYATLPVINLGR 98
Cdd:pfam16661   1 LLEFDNVRILLDPGWDGSF-SYESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYKFGSHLGSNIPVYATLPVANLGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  99 VSTIDSYASSGVIGPYDTNELDLEDIEKSFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWCISTYSEKLVYAK 178
Cdd:pfam16661  80 VSTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLKGKFDGLTITPYNSGHTLGGTIWKISKNSEKIVYAV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835468989 179 RWNHTRDNILNAASILDATGKPLSTLMRPSAII 211
Cdd:pfam16661 160 DWNHTKDSHLNGASLLDSTGKPLESLVRPTALI 192
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-216 9.61e-88

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: 277.09  E-value: 9.61e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989   7 CCDDGSGTTVGSVVRFDNVTLLIDPGWNPSKVsyEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYnftsHFISRIQ 86
Cdd:cd16293     4 LSGAGDESPLCYLLEIDDVTILLDCGWDESFD--MEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVG----KLGLTCP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  87 VYATLPVINLGRVSTIDSYASSGVIGPYdtNELDLEDIEKSFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWC 166
Cdd:cd16293    78 VYATLPVHKMGRMFMYDLYQSRGLEEDF--NLFTLDDVDEAFDRITQLKYSQPVNLRGKGDGLTITAYNAGHTLGGTIWK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835468989 167 ISTYSEKLVYAKRWNHTRDNILNAASILDATGkplstlMRPSAIITTLDK 216
Cdd:cd16293   156 ITKDSEDIVYAVDWNHKKERHLNGAVLDSFGG------LRPSLLITDADN 199
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 4-214 6.25e-74

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: 239.93  E-value: 6.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989   4 KYNCCDDGSGTTVGSVVrFDNVTLLIDPGWNPSKVSYEQCIKYWEKVIPEIDVVILSQPTTECLGAHSLLYYNftshFIS 83
Cdd:cd07734     1 TPLGGGQEVGRSCFLVE-FKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRG----FIF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  84 RIQVYATLPVINLGRVSTIDSYASSGVIGPYDTnELDLEDIEKSFDHIVPLKYSQLVDLRsryDGLTLLAYNAGVCPGGS 163
Cdd:cd07734    76 RGPIYATHPTVALGRLLLEDYVKSAERIGQDQS-LYTPEDIEEALKHIVPLGYGQSIDLF---PALSLTAYNAGHVLGAA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835468989 164 IWCISTYSEKLVYAKRWNHTRDNILNAASILDAtgkplstlmRPSAIITTL 214
Cdd:cd07734   152 MWEIQIYGEKLVYTGDFSNTEDRLLPAASILPP---------RPDLLITES 193
CPSF100_C pfam13299
Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many ...
 736-860 1.84e-21

Cleavage and polyadenylation factor 2 C-terminal; This family lies at the C-terminus of many fungal and plant cleavage and polyadenylation specificity factor subunit 2 proteins. The exact function of the domain is not known, but is likely to function as a binding domain for the protein within the overall CPSF complex.


Pssm-ID: 463836  Cd Length: 162  Bit Score: 91.94  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989 736 DNL---LKWQRISDsYTVATVVGRLV-------------------------------KESLPQVNNHQKTASRSKLVLKP 781
Cdd:pfam13299   5 DSLvssLKWQKVRG-LEVAWVTGRLDraaleegaaeeeeeeedeeeenankkqkleqFSLKDDDEKESKESKDSIPTLDP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835468989 782 LGGSSRSHKTGALSIGDVRLVQLKKQLMEKNYIAEFKGEGTLVINEKVAVRKINDAETIIDGTPSELFDTVKKLVTDML 860
Cdd:pfam13299  84 LPSNLAPAVHQPLFVGDLRLSDLKKLLQSAGHTAEFRGEGTLVCNGTVAVRKTETGRIEIEGVGGPTFYAVRRLIYEQL 162
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 254-372 1.09e-11

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: 62.56  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  254 FLDLFTQVHELLFEstkiNAHTQVPVLILSYARGRTLTYAKSMLEWLSPSLLKTWENRNNtsPFEIGSRIKIIAPNE--- 330
Cdd:smart01027   1 TQELLLILEELWRE----GELPNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQGRN--PFDFKNLKFVKSLEEskr 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835468989  331 LSKYPGSKICFVSEVEA---LINEVITKVGNSEKTTLIFTKPSFE 372
Cdd:smart01027  75 LNDYKGPKVIIASSGMLtggRSRHYLKRLAPDPRNTVILTGYQAE 119
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 19-176 2.74e-04

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: 42.48  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835468989  19 VVRFDNVTLLIDPGWNpskvsyeqCIKYWEKV-IPEIDVVILSqpTTECLGAhsLLYYNFTSHFISRiqVYATLPVINLG 97
Cdd:cd16294    16 VLKFKSTTIMLDCGLD--------CPPETELIdLSTVDVILIS--NYHCMLA--LPFITEYTGFTGV--VYATEPTVQIG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835468989  98 RvstidsyassgvigpydtneLDLEDIEKSFDHIVPLKYSQLVDLrsrYDGLTLLAYNAGVCPGGSIWCISTYSEKLVY 176
Cdd:cd16294    82 R--------------------LLMEELVQALSKIQLVGYSQKLDL---FGAVQVTALSSGYCLGSSNWVIQSHYEKISY 137
 
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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