NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1056669025|ref|WP_068096660|]
View 

MULTISPECIES: GAF and ANTAR domain-containing protein [unclassified Mycobacterium]

Protein Classification

GAF and ANTAR domain-containing protein( domain architecture ID 10588503)

GAF and ANTAR (AmiR and NasR transcription antitermination regulator) domain-containing protein may bind cyclic nucleotides and RNA

Gene Ontology:  GO:0003723|GO:0005515
PubMed:  11796212|9433123|11032796|10966457

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANTAR pfam03861
ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding ...
 176-221 4.42e-14

ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.


:

Pssm-ID: 427550 [Multi-domain]  Cd Length: 46  Bit Score: 64.28  E-value: 4.42e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1056669025 176 ALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQ 221
Cdd:pfam03861   1 ALESRKVIEQAKGILMERLGLSEDEAFRLLRKLSMDRNVKLREVAE 46
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 43-163 3.04e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 45.54  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056669025  43 GSQYAGITLAERSKSVtnVAATHRYPVLLDEIQNRYAEGPCVEAAWRHHVMHVEDLSEEQRWpryRRHALEQTPIRSILS 122
Cdd:pfam13185  20 ASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK---KGLPAGHAGLRSFLS 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1056669025 123 YELFVDRGSMAALNFYADAPHAFPDDSLELGAVYATHIALA 163
Cdd:pfam13185  95 VPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIA 135
 
Name Accession Description Interval E-value
ANTAR pfam03861
ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding ...
 176-221 4.42e-14

ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.


Pssm-ID: 427550 [Multi-domain]  Cd Length: 46  Bit Score: 64.28  E-value: 4.42e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1056669025 176 ALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQ 221
Cdd:pfam03861   1 ALESRKVIEQAKGILMERLGLSEDEAFRLLRKLSMDRNVKLREVAE 46
ANTAR smart01012
ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found ...
 171-224 4.56e-14

ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins; The majority of the domain consists of a coiled-coil.


Pssm-ID: 198080 [Multi-domain]  Cd Length: 55  Bit Score: 64.42  E-value: 4.56e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1056669025  171 DQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLV 224
Cdd:smart01012   2 EQLREALESRKVIEQAKGILMERRGLSEEEAFELLRKLAMDRNVKLRDVAEAIV 55
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 165-232 8.18e-12

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 61.90  E-value: 8.18e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056669025 165 SMLRRQDQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLVDSEHPLKR 232
Cdd:COG3707   127 ALRRELAKLREALEERKLIERAKGILMERRGLSEDEAYRLLRKQAMDRRVKLAEVAEAILAAAELLKG 194
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 43-163 3.04e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 45.54  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056669025  43 GSQYAGITLAERSKSVtnVAATHRYPVLLDEIQNRYAEGPCVEAAWRHHVMHVEDLSEEQRWpryRRHALEQTPIRSILS 122
Cdd:pfam13185  20 ASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK---KGLPAGHAGLRSFLS 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1056669025 123 YELFVDRGSMAALNFYADAPHAFPDDSLELGAVYATHIALA 163
Cdd:pfam13185  95 VPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIA 135
GAF COG2203
GAF domain [Signal transduction mechanisms];
80-225 1.44e-03

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 39.41  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056669025  80 EGPCVEAAWRHHVMHVEDLSEEQRWPRYRRHALEQTPIRSILSYELFVDRGSMAALNFYADAPHAFPDDSLELGAVYATH 159
Cdd:COG2203   260 EGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQ 339

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056669025 160 IALAWSMLRRQDQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLVD 225
Cdd:COG2203   340 AAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
 
Name Accession Description Interval E-value
ANTAR pfam03861
ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding ...
 176-221 4.42e-14

ANTAR domain; ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.


Pssm-ID: 427550 [Multi-domain]  Cd Length: 46  Bit Score: 64.28  E-value: 4.42e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1056669025 176 ALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQ 221
Cdd:pfam03861   1 ALESRKVIEQAKGILMERLGLSEDEAFRLLRKLSMDRNVKLREVAE 46
ANTAR smart01012
ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found ...
 171-224 4.56e-14

ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins; The majority of the domain consists of a coiled-coil.


Pssm-ID: 198080 [Multi-domain]  Cd Length: 55  Bit Score: 64.42  E-value: 4.56e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1056669025  171 DQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLV 224
Cdd:smart01012   2 EQLREALESRKVIEQAKGILMERRGLSEEEAFELLRKLAMDRNVKLRDVAEAIV 55
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 165-232 8.18e-12

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 61.90  E-value: 8.18e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056669025 165 SMLRRQDQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLVDSEHPLKR 232
Cdd:COG3707   127 ALRRELAKLREALEERKLIERAKGILMERRGLSEDEAYRLLRKQAMDRRVKLAEVAEAILAAAELLKG 194
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 43-163 3.04e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 45.54  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056669025  43 GSQYAGITLAERSKSVtnVAATHRYPVLLDEIQNRYAEGPCVEAAWRHHVMHVEDLSEEQRWpryRRHALEQTPIRSILS 122
Cdd:pfam13185  20 ASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK---KGLPAGHAGLRSFLS 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1056669025 123 YELFVDRGSMAALNFYADAPHAFPDDSLELGAVYATHIALA 163
Cdd:pfam13185  95 VPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIA 135
GAF COG2203
GAF domain [Signal transduction mechanisms];
80-225 1.44e-03

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 39.41  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056669025  80 EGPCVEAAWRHHVMHVEDLSEEQRWPRYRRHALEQTPIRSILSYELFVDRGSMAALNFYADAPHAFPDDSLELGAVYATH 159
Cdd:COG2203   260 EGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQ 339

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056669025 160 IALAWSMLRRQDQFRSALASRDMIGQAKGIIMERFNLDAIEAFELLTRLSQQSNTRLIDIAQGLVD 225
Cdd:COG2203   340 AAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH