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Conserved domains on  [gi|489625375|ref|WP_003529815|]
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MULTISPECIES: type II toxin-antitoxin system VapC family toxin [Sinorhizobium]

Protein Classification

type II toxin-antitoxin system VapC family toxin( domain architecture ID 10177355)

type II toxin-antitoxin (TA) system VapC family toxin functions as a ribonuclease that is neutralized by its cognate VapB family antitoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIN_MT3492-like cd09874
VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 ...
 2-137 3.39e-41

VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 and other uncharacterized, annotated PilT protein domain proteins; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis CDC1551, hypothetical protein MT3492, and similar bacterial and archaeal proteins are included in this subfamily. They are PIN domain homologs of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


:

Pssm-ID: 350222  Cd Length: 134  Bit Score: 133.78  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   2 LYLDTSMIVAALSNEAMTPRVQGWLAEQDpAELLISDWTVTEVSSAMAIKLRTGQIDLEQRAAALAIFNKLVAESLTVLS 81
Cdd:cd09874    1 LYLDTSALVKLYVREPGSDAVRALLDAAS-DVLAISDLTRVEFASALARKVREGELSEEQARAALAAFERDWASLLRVVP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489625375  82 VTGGQFRAAAKFADQHmlGLRAGDALHLAVASEHGA-TVHTLDRRLAEAGPALGVPT 137
Cdd:cd09874   80 VTDSLFRRAAELAERH--GLRALDALHLASALRLGAlTFVTADKRLAEAARAEGLKV 134
 
Name Accession Description Interval E-value
PIN_MT3492-like cd09874
VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 ...
 2-137 3.39e-41

VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 and other uncharacterized, annotated PilT protein domain proteins; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis CDC1551, hypothetical protein MT3492, and similar bacterial and archaeal proteins are included in this subfamily. They are PIN domain homologs of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350222  Cd Length: 134  Bit Score: 133.78  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   2 LYLDTSMIVAALSNEAMTPRVQGWLAEQDpAELLISDWTVTEVSSAMAIKLRTGQIDLEQRAAALAIFNKLVAESLTVLS 81
Cdd:cd09874    1 LYLDTSALVKLYVREPGSDAVRALLDAAS-DVLAISDLTRVEFASALARKVREGELSEEQARAALAAFERDWASLLRVVP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489625375  82 VTGGQFRAAAKFADQHmlGLRAGDALHLAVASEHGA-TVHTLDRRLAEAGPALGVPT 137
Cdd:cd09874   80 VTDSLFRRAAELAERH--GLRALDALHLASALRLGAlTFVTADKRLAEAARAEGLKV 134
VapC COG1848
VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN ...
 1-129 2.82e-19

VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN domain [Defense mechanisms];


Pssm-ID: 441453  Cd Length: 134  Bit Score: 77.71  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   1 MLYLDTSMIVAAL-SNEAMTPRVQGWL--AEQDPAELLISDWTVTEVSSAMAiklRTGQIDLEQRAAALAIFnklvAESL 77
Cdd:COG1848    1 MILLDTNVLIYALeGDSPFHERARELLerAEEGEEELYTSPLVLAEVLYVLT---RPGGLSLEEARELLEAL----LSNI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489625375  78 TVLSVTGGQFRAAAKFADQHmlGLRAGDALHLAVASEHGAT-VHTLDRRLAEA 129
Cdd:COG1848   74 EVVPVDEEILEEAAELLAKY--GLRLNDALHLATALEHGADaLVTFDRDFARV 124
PIN pfam01850
PIN domain;
2-130 2.17e-09

PIN domain;


Pssm-ID: 426475  Cd Length: 121  Bit Score: 52.03  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375    2 LYLDTSMIVAALSNEAMTPRVQGWLAEQDpaELLISDWTVTEVSSAmaIKLRTGQIDLEQRAAALaifnkLVAESLTVLS 81
Cdd:pfam01850   1 IVLDTSVLIALLRGEPLHEAARELLEAAG--ELVTSAIVLAELLYG--LNRRLGLGKAAELVELL-----LLLSALEVLP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489625375   82 VTGGQFRAAAKFADQHMlGLRAGDALHLAVASEHGATVHTLDRRLAEAG 130
Cdd:pfam01850  72 IDAELAEEAAELRLKYG-KLGPNDALIAATAKEHGAKLITFDEDFARVA 119
 
Name Accession Description Interval E-value
PIN_MT3492-like cd09874
VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 ...
 2-137 3.39e-41

VapC-like PIN domain of the hypothetical protein MT3492 of Mycobacterium tuberculosis CDC1551 and other uncharacterized, annotated PilT protein domain proteins; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis CDC1551, hypothetical protein MT3492, and similar bacterial and archaeal proteins are included in this subfamily. They are PIN domain homologs of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350222  Cd Length: 134  Bit Score: 133.78  E-value: 3.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   2 LYLDTSMIVAALSNEAMTPRVQGWLAEQDpAELLISDWTVTEVSSAMAIKLRTGQIDLEQRAAALAIFNKLVAESLTVLS 81
Cdd:cd09874    1 LYLDTSALVKLYVREPGSDAVRALLDAAS-DVLAISDLTRVEFASALARKVREGELSEEQARAALAAFERDWASLLRVVP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489625375  82 VTGGQFRAAAKFADQHmlGLRAGDALHLAVASEHGA-TVHTLDRRLAEAGPALGVPT 137
Cdd:cd09874   80 VTDSLFRRAAELAERH--GLRALDALHLASALRLGAlTFVTADKRLAEAARAEGLKV 134
VapC COG1848
VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN ...
 1-129 2.82e-19

VapC family ribonuclease, toxin component of the VapBC toxin-antitoxin module, contains PIN domain [Defense mechanisms];


Pssm-ID: 441453  Cd Length: 134  Bit Score: 77.71  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   1 MLYLDTSMIVAAL-SNEAMTPRVQGWL--AEQDPAELLISDWTVTEVSSAMAiklRTGQIDLEQRAAALAIFnklvAESL 77
Cdd:COG1848    1 MILLDTNVLIYALeGDSPFHERARELLerAEEGEEELYTSPLVLAEVLYVLT---RPGGLSLEEARELLEAL----LSNI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489625375  78 TVLSVTGGQFRAAAKFADQHmlGLRAGDALHLAVASEHGAT-VHTLDRRLAEA 129
Cdd:COG1848   74 EVVPVDEEILEEAAELLAKY--GLRLNDALHLATALEHGADaLVTFDRDFARV 124
VapC COG4113
RNA interferase (RNase) VapC, contains PIN domain [Defense mechanisms];
2-133 2.17e-17

RNA interferase (RNase) VapC, contains PIN domain [Defense mechanisms];


Pssm-ID: 443289  Cd Length: 125  Bit Score: 72.63  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   2 LYLDTSMIVAALSNEAMTPRVQGWLaEQDPAELLISDWTVTEVSSAMAIKLRTGQIDLEQRAAALAIFNKLVaesLTVLS 81
Cdd:COG4113    1 IVVDASALVKWLLPEEGSEEALRLL-ERAADELVAPDLALYEVANVLWKAVRRGRLTEEEAEEALELLLELP---IEVVP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489625375  82 VTGgQFRAAAKFADQHmlGLRAGDALHLAVASEHGATVHTLDRRLAEAGPAL 133
Cdd:COG4113   77 VTE-LLERALELARRH--GLTAYDAAYLALAERLGAPLVTADRRLARAARAL 125
PIN_Pae0151-like cd09873
VapC-like PIN domain of the Pyrobaculum aerophilum Pae0151 and Pae2754 proteins and homologs; ...
 4-136 1.73e-12

VapC-like PIN domain of the Pyrobaculum aerophilum Pae0151 and Pae2754 proteins and homologs; Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of the Pyrobaculum aerophilum proteins, Pae0151 and Pae2754, and homologs are included in this subfamily. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350221  Cd Length: 128  Bit Score: 60.24  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   4 LDTSMIVAALSNEAMTPRVQGWLaEQDPAELLISDWTVTEVSSAMAIKLRTGQIDLEQRAAALAIFNKLVAESLTVLSVt 83
Cdd:cd09873    2 VDASVAVKWLLPEEESEAADRLL-ERLEEELVAPDLWLYEVANVLRKAVRRGRLTEEEAEEALEDLLDLPIEIDPDPEL- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489625375  84 ggqFRAAAKFADQHmlGLRAGDALHLAVASEHGATVHTLDRRLAEAGPALGVP 136
Cdd:cd09873   80 ---LEEALELARRH--GLTAYDAAYLALAERLGAPLVTADRKLARAAKAAGVK 127
PIN pfam01850
PIN domain;
2-130 2.17e-09

PIN domain;


Pssm-ID: 426475  Cd Length: 121  Bit Score: 52.03  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375    2 LYLDTSMIVAALSNEAMTPRVQGWLAEQDpaELLISDWTVTEVSSAmaIKLRTGQIDLEQRAAALaifnkLVAESLTVLS 81
Cdd:pfam01850   1 IVLDTSVLIALLRGEPLHEAARELLEAAG--ELVTSAIVLAELLYG--LNRRLGLGKAAELVELL-----LLLSALEVLP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489625375   82 VTGGQFRAAAKFADQHMlGLRAGDALHLAVASEHGATVHTLDRRLAEAG 130
Cdd:pfam01850  72 IDAELAEEAAELRLKYG-KLGPNDALIAATAKEHGAKLITFDEDFARVA 119
VapC COG1487
Ribonuclease/mRNA interferase VapC, contains PIN domain [Defense mechanisms];
4-125 1.01e-07

Ribonuclease/mRNA interferase VapC, contains PIN domain [Defense mechanisms];


Pssm-ID: 441096  Cd Length: 128  Bit Score: 47.55  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   4 LDTSMIVAALSNEAmtPRVQGWLAEQDPAELLISDWTVTEVSSAMAIKLrtgqiDLEQRAAALAIFnklvaESLTVLSVT 83
Cdd:COG1487    3 LDTNVLIDLLRGRP--PAVLAWLAELEAGELAISAITLAELLYGARRSP-----DAKRRAALEAFL-----EAFPVLPFD 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489625375  84 GGQFRAAAKFADQHML---GLRAGDALHLAVASEHGATVHTLDRR 125
Cdd:COG1487   71 AEAARRAGELRAALRRagrPIGLADLLIAATALAHGLTLVTRNTK 115
PIN_VapC4-5_FitB-like cd18746
uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily; ...
 4-119 1.65e-03

uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily; The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350313 [Multi-domain]  Cd Length: 133  Bit Score: 36.26  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   4 LDTsMIVAALSNEAMTPRVQGWLAEQDPAELLISDWTVTEVSSAMAIKLRTgqiDLEQRAAALAIFNKLVAE-SLTVLSV 82
Cdd:cd18746    2 LDT-NVISELRKPRPDPGVVAWLAAVDEDDLFLSVITIGEIRKGIERLRRR---DPARAARLEAWLDGLLLRfAGRILPV 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489625375  83 TGGQFRAAAKFADQHMLGLRAGDALHLAVASEHGATV 119
Cdd:cd18746   78 DAEVARRWGRLHAPAPAPLPVADALIAATALVHGLTL 114
PIN_VapC-like cd09854
VapC-like PIN domains of VapC and Smg6 ribonucleases, ribosome assembly factor NOB1, ...
 3-131 1.92e-03

VapC-like PIN domains of VapC and Smg6 ribonucleases, ribosome assembly factor NOB1, rRNA-processing protein Fcf1, Archaeoglobus fulgidus AF0591 protein, and homologs; PIN (PilT N terminus) domains of such ribonucleases as the toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1, are included in VapC-like this family. Also included are the PIN domains of the Pyrobaculum aerophilum Pea0151 and Archaeoglobus fulgidus AF0591 proteins and other similar archaeal homologs. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350205  Cd Length: 129  Bit Score: 36.10  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   3 YLDTSMIVAALSNEAMTPRVQGWLAE-QDPAELLISDWTVTEVSSAMAiKLRTGQIDLEQRAAALAIfnKLVAESLTVLs 81
Cdd:cd09854    1 VLDTNVLIALLSSEPESEAAKELLALlLGDSELVIPPLVLAELLRLLA-RERGARRALEILELLRAL--EVVEEEPALA- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489625375  82 vtggqFRAAAKFADQHMLGLRAGDALHLAVASEHG-ATVHTLDRRLAEAGP 131
Cdd:cd09854   77 -----EIALEVLALGLERGLDFGDALILALAKELGgAVLVTNDRDFRRLAK 122
PIN_VapC4-5_FitB-like cd18741
uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily; ...
 4-125 2.74e-03

uncharacterized subgroup of the PIN_VapC4-5_FitB-like subfamily of the PIN domain superfamily; The PIN_VapC4-5_FitB-like subfamily includes the Virulence associated protein C (VapC)-like PIN (PilT N terminus) domain of Mycobacterium tuberculosis VapC4 and VapC5 ribonuclease toxins of the VapBC toxin/antitoxin (TA) system, and Neisseria gonorrhoeae FitB toxin of the FitAB TA system. This subfamily belongs to the VapC-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350308  Cd Length: 120  Bit Score: 35.55  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489625375   4 LDTSMIVAALSNEAMTPRvqgWLAEQDPAELLISDWTVTEVSSAMAIKlrtgqidleqraAALAIFNKLVaESLTVLSVT 83
Cdd:cd18741    2 LDTDILIDFLRGNPSAAE---KLLELLGGNLAISVITVAELYAGARNK------------KELEKLEKLL-SLFEVIPVD 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489625375  84 ------GGQFRAaaKFADQHmlGLRAGDALHLAVASEHGATVHTLDRR 125
Cdd:cd18741   66 eeiaelAGELRR--KYRKSH--GLGLPDALIAATALEHGLTLVTLNVK 109
 
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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