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Conserved domains on  [gi|15599247|ref|NP_252741|]
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transcription antitermination protein NusB [Pseudomonas aeruginosa PAO1]

Protein Classification

transcription antitermination protein NusB( domain architecture ID 10011308)

transcription antitermination protein NusB (N utilization substance protein B) is a lambda and rRNA transcription antitermination protein which also plays a role in ribosomal RNA biogenesis

CATH:  1.10.940.10
Gene Symbol:  nusB
Gene Ontology:  GO:0031564|GO:0003723|GO:0006353
SCOP:  4001076

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nusB PRK00202
transcription antitermination factor NusB;
19-153 1.25e-67

transcription antitermination factor NusB;


:

Pssm-ID: 234686 [Multi-domain]  Cd Length: 137  Bit Score: 201.56  E-value: 1.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   19 AARRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVEL 97
Cdd:PRK00202   1 AARRKAREAAVQALYQWELSGNDIAEIIEAQLLEEQYDKADPAYFRSLVRGVVENQAELDELISPYLkDWTLERLDPVER 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599247   98 AILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPRLRAAE 153
Cdd:PRK00202  81 AILRLALYELLFRDDVPYKVVINEAIELAKKFGDEDSHKFVNGVLDKIAKELRPAE 136
 
Name Accession Description Interval E-value
nusB PRK00202
transcription antitermination factor NusB;
19-153 1.25e-67

transcription antitermination factor NusB;


Pssm-ID: 234686 [Multi-domain]  Cd Length: 137  Bit Score: 201.56  E-value: 1.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   19 AARRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVEL 97
Cdd:PRK00202   1 AARRKAREAAVQALYQWELSGNDIAEIIEAQLLEEQYDKADPAYFRSLVRGVVENQAELDELISPYLkDWTLERLDPVER 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599247   98 AILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPRLRAAE 153
Cdd:PRK00202  81 AILRLALYELLFRDDVPYKVVINEAIELAKKFGDEDSHKFVNGVLDKIAKELRPAE 136
nusB TIGR01951
transcription antitermination factor NusB; A transcription antitermination complex active in ...
 21-148 2.53e-61

transcription antitermination factor NusB; A transcription antitermination complex active in many bacteria was designated N-utilization substance (Nus) in E. coli because of its interaction with phage lambda protein N. This model represents NusB. Other components are NusA and NusG. NusE is, in fact, ribosomal protein S10. [Transcription, Transcription factors]


Pssm-ID: 273891 [Multi-domain]  Cd Length: 129  Bit Score: 185.39  E-value: 2.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247    21 RRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVELAI 99
Cdd:TIGR01951   1 RRKARELALQALYQWELSGEDVDEIIEEFLEERELDEEDREYFRELVRGVLENQEEIDELISPHLeDWTLERLDPVDRAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15599247   100 LRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPR 148
Cdd:TIGR01951  81 LRLAIYELLYRPDVPYKVVINEAVELAKKFGDEDSHKFVNGVLDKIAKE 129
NusB COG0781
Transcription antitermination protein NusB [Transcription];
27-152 9.87e-60

Transcription antitermination protein NusB [Transcription];


Pssm-ID: 440544 [Multi-domain]  Cd Length: 128  Bit Score: 181.11  E-value: 9.87e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  27 LAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVELAILRLSTY 105
Cdd:COG0781   2 LALQALYQVELSGAYANEILEEFLEDEELSEADRAFATELVYGVLRNQEELDALIAPYLkDWPLERLDPVDRAILRLAAY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599247 106 ELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPRLRAA 152
Cdd:COG0781  82 ELLYLDDVPYKVAINEAVELAKKFGTEDSPKFVNGVLDKIAKELRAE 128
NusB pfam01029
NusB family; The NusB protein is involved in the regulation of rRNA biosynthesis by ...
 22-146 1.58e-40

NusB family; The NusB protein is involved in the regulation of rRNA biosynthesis by transcriptional antitermination.


Pssm-ID: 460031 [Multi-domain]  Cd Length: 133  Bit Score: 132.78  E-value: 1.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247    22 RKARSLAVQALYSWQIAGQPLHEIEAQFR------TDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDP 94
Cdd:pfam01029   1 RNARELALQALYQVEINGSDEEEKGAYLNealdkaLEGDLSEEDRAFATELVYGVLRNLEELDALIEKLLeNWPLERLSP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15599247    95 VELAILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLA 146
Cdd:pfam01029  81 VDRAILRLGLYELLFLDDVPPHVAINEAVELAKKFGGEKSAKFVNGVLRNVA 132
Terminator_NusB cd00619
Transcription termination factor NusB (N protein-Utilization Substance B). NusB plays a key ...
 21-147 1.17e-39

Transcription termination factor NusB (N protein-Utilization Substance B). NusB plays a key role in the regulation of ribosomal RNA biosynthesis in eubacteria by modulating the efficiency of transcriptional antitermination. NusB along with other Nus factors (NusA, NusE/S10 and NusG) forms the core complex with the boxA element of the nut site of the rRNA operons. These interactions help RNA polymerase to counteract polarity during transcription of rRNA operons and allow stable antitermination. The transcription antitermination system can be appropriated by some bacteriophages such as lambda, which use the system to switch between the lysogenic and lytic modes of phage propagation.


Pssm-ID: 238342 [Multi-domain]  Cd Length: 130  Bit Score: 130.48  E-value: 1.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  21 RRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCLDR-PLAEIDPVELAI 99
Cdd:cd00619   1 RRRARELAVQALYAWELAPEILAEVVSLLELLQYKSKKVLPFALKLVRGVLENIEEIDELIEKHLRNwSLDRLAIVERAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15599247 100 LRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAP 147
Cdd:cd00619  81 LRLAVYELLFLPDVPHPVVINEAIELAKRFGGDDSHKFVNGVLDKIAK 128
 
Name Accession Description Interval E-value
nusB PRK00202
transcription antitermination factor NusB;
19-153 1.25e-67

transcription antitermination factor NusB;


Pssm-ID: 234686 [Multi-domain]  Cd Length: 137  Bit Score: 201.56  E-value: 1.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   19 AARRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVEL 97
Cdd:PRK00202   1 AARRKAREAAVQALYQWELSGNDIAEIIEAQLLEEQYDKADPAYFRSLVRGVVENQAELDELISPYLkDWTLERLDPVER 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599247   98 AILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPRLRAAE 153
Cdd:PRK00202  81 AILRLALYELLFRDDVPYKVVINEAIELAKKFGDEDSHKFVNGVLDKIAKELRPAE 136
nusB TIGR01951
transcription antitermination factor NusB; A transcription antitermination complex active in ...
 21-148 2.53e-61

transcription antitermination factor NusB; A transcription antitermination complex active in many bacteria was designated N-utilization substance (Nus) in E. coli because of its interaction with phage lambda protein N. This model represents NusB. Other components are NusA and NusG. NusE is, in fact, ribosomal protein S10. [Transcription, Transcription factors]


Pssm-ID: 273891 [Multi-domain]  Cd Length: 129  Bit Score: 185.39  E-value: 2.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247    21 RRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVELAI 99
Cdd:TIGR01951   1 RRKARELALQALYQWELSGEDVDEIIEEFLEERELDEEDREYFRELVRGVLENQEEIDELISPHLeDWTLERLDPVDRAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15599247   100 LRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPR 148
Cdd:TIGR01951  81 LRLAIYELLYRPDVPYKVVINEAVELAKKFGDEDSHKFVNGVLDKIAKE 129
NusB COG0781
Transcription antitermination protein NusB [Transcription];
27-152 9.87e-60

Transcription antitermination protein NusB [Transcription];


Pssm-ID: 440544 [Multi-domain]  Cd Length: 128  Bit Score: 181.11  E-value: 9.87e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  27 LAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDPVELAILRLSTY 105
Cdd:COG0781   2 LALQALYQVELSGAYANEILEEFLEDEELSEADRAFATELVYGVLRNQEELDALIAPYLkDWPLERLDPVDRAILRLAAY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599247 106 ELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAPRLRAA 152
Cdd:COG0781  82 ELLYLDDVPYKVAINEAVELAKKFGTEDSPKFVNGVLDKIAKELRAE 128
NusB pfam01029
NusB family; The NusB protein is involved in the regulation of rRNA biosynthesis by ...
 22-146 1.58e-40

NusB family; The NusB protein is involved in the regulation of rRNA biosynthesis by transcriptional antitermination.


Pssm-ID: 460031 [Multi-domain]  Cd Length: 133  Bit Score: 132.78  E-value: 1.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247    22 RKARSLAVQALYSWQIAGQPLHEIEAQFR------TDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCL-DRPLAEIDP 94
Cdd:pfam01029   1 RNARELALQALYQVEINGSDEEEKGAYLNealdkaLEGDLSEEDRAFATELVYGVLRNLEELDALIEKLLeNWPLERLSP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15599247    95 VELAILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLA 146
Cdd:pfam01029  81 VDRAILRLGLYELLFLDDVPPHVAINEAVELAKKFGGEKSAKFVNGVLRNVA 132
Terminator_NusB cd00619
Transcription termination factor NusB (N protein-Utilization Substance B). NusB plays a key ...
 21-147 1.17e-39

Transcription termination factor NusB (N protein-Utilization Substance B). NusB plays a key role in the regulation of ribosomal RNA biosynthesis in eubacteria by modulating the efficiency of transcriptional antitermination. NusB along with other Nus factors (NusA, NusE/S10 and NusG) forms the core complex with the boxA element of the nut site of the rRNA operons. These interactions help RNA polymerase to counteract polarity during transcription of rRNA operons and allow stable antitermination. The transcription antitermination system can be appropriated by some bacteriophages such as lambda, which use the system to switch between the lysogenic and lytic modes of phage propagation.


Pssm-ID: 238342 [Multi-domain]  Cd Length: 130  Bit Score: 130.48  E-value: 1.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  21 RRKARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCLDR-PLAEIDPVELAI 99
Cdd:cd00619   1 RRRARELAVQALYAWELAPEILAEVVSLLELLQYKSKKVLPFALKLVRGVLENIEEIDELIEKHLRNwSLDRLAIVERAI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15599247 100 LRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAP 147
Cdd:cd00619  81 LRLAVYELLFLPDVPHPVVINEAIELAKRFGGDDSHKFVNGVLDKIAK 128
NusB_Sun cd00447
RNA binding domain of NusB (N protein-Utilization Substance B) and Sun (also known as RrmB or ...
 23-147 2.22e-27

RNA binding domain of NusB (N protein-Utilization Substance B) and Sun (also known as RrmB or Fmu) proteins. This family includes two orthologous groups exemplified by the transcription termination factor NusB and the N-terminal domain of the rRNA-specific 5-methylcytidine transferase (m5C-methyltransferase) Sun. The NusB protein plays a key role in the regulation of ribosomal RNA biosynthesis in eubacteria by modulating the efficiency of transcriptional antitermination. NusB along with other Nus factors (NusA, NusE/S10 and NusG) forms the core complex with the boxA element of the nut site of the rRNA operons. These interactions help RNA polymerase to counteract polarity during transcription of rRNA operons and allow stable antitermination. The transcription antitermination system can be appropriated by some bacteriophages such as lambda, which use the system to switch between the lysogenic and lytic modes of phage propagation. The m5C-methyltransferase Sun shares the N-terminal non-catalytic RNA-binding domain with NusB.


Pssm-ID: 238253 [Multi-domain]  Cd Length: 129  Bit Score: 98.96  E-value: 2.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  23 KARSLAVQALYSWQIAGQPLHEIEAQFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCLDRP-LAEIDPVELAILR 101
Cdd:cd00447   1 SAREIAFQALYQVEIRNGISLEAVLSALEKLQLAKKDRPFALELVYGVLRNLPELDDIISPLLKKWlLDRLDKVDRAILR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599247 102 LSTYELR-NRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAP 147
Cdd:cd00447  81 LLLYELYqLLYDVPPPVAINEAVELAKRFGDDDSAKFVNGVLRRIAK 127
Methyltransferase_Sun cd00620
N-terminal RNA binding domain of the methyltransferase Sun. The rRNA-specific 5-methylcytidine ...
 36-142 1.31e-14

N-terminal RNA binding domain of the methyltransferase Sun. The rRNA-specific 5-methylcytidine transferase Sun, also known as RrmB or Fmu shares the RNA-binding non-catalytic domain with the transcription termination factor NusB. The precise biological role of this domain in Sun is unknown, although it is likely to be involved in sequence-specific RNA binding. The C-terminal methyltransferase domain of Sun has been shown to catalyze formation of m5C at position 967 of 16S rRNA in Escherichia coli.


Pssm-ID: 238343 [Multi-domain]  Cd Length: 126  Bit Score: 66.21  E-value: 1.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247  36 QIAGQPLHEIEAQFRTDN---------DFSEVDGAYFHEILHGVPRQKSELDSTFEPCLDRPLAEIDPVELAILRLSTYE 106
Cdd:cd00620   5 STAAEVLRDVLQRGASLNavlsalqkkDKSDRDRGLATELVYGTLRWLALLDWIINPLLKKPDVGKDPDVRNLLRLGLYQ 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599247 107 LrNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVL 142
Cdd:cd00620  85 L-LYLDVPPHAAVDETVEIAKIRKDLGRAGLVNAVL 119
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
23-142 7.77e-12

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 61.73  E-value: 7.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   23 KARSLAVQALYswqiagqplhEIEA----------QFRTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCLdRPLAEI 92
Cdd:PRK14902   4 NARELALEVLI----------KVENngaysnialnKVLKKSELSDKDKALLTELVYGTIQRKLTLDYYLAPFI-KKRKKL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15599247   93 DPVELAILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVL 142
Cdd:PRK14902  73 DPWVRNLLRMSLYQLLYLDKVPDHAAVNEAVEIAKKRGHKGIAKFVNGVL 122
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 23-147 1.38e-09

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 55.45  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   23 KARSLAVQALYSWQI----AGQPLHEIEAQFRTDndfsEVDGAYFHEILHGVPRQKSELDSTFEPCLDRPLAEIDPVELA 98
Cdd:PRK14904   3 TARELALQVLQELETgerkSDTLLHRMLERSSLE----RNDRALATELVNGVLRYRLQLDFIISRFYHHDLEKAAPVLKN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15599247   99 ILRLSTYELRNRIDVPYKVVINEGIELAKTFGATDGHKFVNGVLDKLAP 147
Cdd:PRK14904  79 ILRLGVYQLLFLDRVPRWAAVNECVKLARKYKGEHMAKLVNGVLRNISP 127
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
25-142 8.93e-05

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 41.33  E-value: 8.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   25 RSLAVQALYSWQIAGQPLHEIEAQfrTDNDFSEVDGAYFHEILHGVPRQKSELDSTFEPCLDRPLAEIDPVELAILRLST 104
Cdd:PRK10901   5 RALAAAAILQVVDQGQSLSAALPA--LQQKVSDKDRALLQELCYGVLRRLPRLEWLIAQLLAKPLKGKQRIVHALLLVGL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15599247  105 YELRN-RIdvPYKVVINEGIELAKTFGATDGHKFVNGVL 142
Cdd:PRK10901  83 YQLLYtRI--PAHAAVDETVEAAKALKRPWAKGLVNAVL 119
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 49-154 2.78e-04

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 39.86  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   49 FRTDND--FS---EVDGAYFHEILHGVPRQKSELDSTFEPCLDRPlaEIDPVELAILRLSTYELRNRIDVPYKVVINEGI 123
Cdd:PRK14903  23 FREDVDsvLSfldDKDRRFFKELVWGVVRKEELLDWYINQLLKKK--DIPPAVRVALRMGAYQLLFMNSVPDYAAVSETV 100

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15599247  124 ELAKTfgaTDGHKFVNGVLDKLAPRLRAAEL 154
Cdd:PRK14903 101 KLVKN---ENFKKLVNAVLRRLRTVPEPKEL 128
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 53-153 1.63e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 37.60  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599247   53 NDFSEVDGAYFHEILHGVPRQKSELDSTFEpCLDRPLAEIDPVELA-ILRLSTYELR--NRIdvPYKVVINEGIELAKTF 129
Cdd:PRK14901  31 YPLSGADRALVTELVYGCIRRRRTLDAWID-QLGKKPAHKQPPDLRwLLHLGLYQLRymDRI--PASAAVNTTVELAKQN 107

                         90       100
                 ....*....|....*....|....*.
gi 15599247  130 GATDGHKFVNGVLdklapR--LRAAE 153
Cdd:PRK14901 108 GLGGLAGVVNGIL-----RqyLRARE 128
 
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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