NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|381384199|dbj|BAM01016|]
View 

hypothetical protein CLDAP_29760 [Caldilinea aerophila DSM 14535 = NBRC 104270]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YhfZ_C pfam14503
YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix ...
70-303 1.04e-105

YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix domain HTH_41 (pfam14502). It includes YhfZ proteins from Escherichia coli and Shigella flexneri.


:

Pssm-ID: 433998  Cd Length: 236  Bit Score: 307.67  E-value: 1.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199   70 DYVRLWQLGYQRPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAH 149
Cdd:pfam14503   1 DYKKLWELAGLGNLVGAMPLPYSRRYEGLATGLKAQFEDLGIPFNFAYMRGADVRLEALKEGRYDFAVVSRLAAERYLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  150 GFTATMVLALGAYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDA 229
Cdd:pfam14503  81 GPGLEIALELGPGTYVSAHVLLLRDGEKTEIKDGMRVGIDSNSADQRILTEAEFEGKDVEFVEIPYMQLLELLLAGDIDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199  230 VVW--TDLNTPALPDNITITPLTTDDDPMLSALSEAVLVVDPARPASAHLLQALLDVPALLEIQNEVIHRTRIPSY 303
Cdd:pfam14503 161 VVWnlDEVQDPLELGLRALPLTSLDARPIVEQASEAVLVIRKDNPGLKALLRNLIDVEAVLEIQKKVLEGERIPSY 236
HTH_ARSR super family cl46857
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
19-66 1.80e-11

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


The actual alignment was detected with superfamily member pfam14502:

Pssm-ID: 481197 [Multi-domain]  Cd Length: 48  Bit Score: 58.27  E-value: 1.80e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 381384199   19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAAQLEARGRLGTFV 66
Cdd:pfam14502   1 KAGERLPTISEYSHKFELSVGTVQKALKKLEDMKAIQLERRGHNGTYL 48
 
Name Accession Description Interval E-value
YhfZ_C pfam14503
YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix ...
70-303 1.04e-105

YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix domain HTH_41 (pfam14502). It includes YhfZ proteins from Escherichia coli and Shigella flexneri.


Pssm-ID: 433998  Cd Length: 236  Bit Score: 307.67  E-value: 1.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199   70 DYVRLWQLGYQRPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAH 149
Cdd:pfam14503   1 DYKKLWELAGLGNLVGAMPLPYSRRYEGLATGLKAQFEDLGIPFNFAYMRGADVRLEALKEGRYDFAVVSRLAAERYLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  150 GFTATMVLALGAYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDA 229
Cdd:pfam14503  81 GPGLEIALELGPGTYVSAHVLLLRDGEKTEIKDGMRVGIDSNSADQRILTEAEFEGKDVEFVEIPYMQLLELLLAGDIDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199  230 VVW--TDLNTPALPDNITITPLTTDDDPMLSALSEAVLVVDPARPASAHLLQALLDVPALLEIQNEVIHRTRIPSY 303
Cdd:pfam14503 161 VVWnlDEVQDPLELGLRALPLTSLDARPIVEQASEAVLVIRKDNPGLKALLRNLIDVEAVLEIQKKVLEGERIPSY 236
YhfZ_full NF041241
GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional ...
1-303 2.23e-105

GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional regulator YhfZ from Escherichia coli, with an N-terminal GntR-like domain, are quite divergent. See PF14503 (YhfZ_C) for the broader family. This HMM identifies a subset in which the motif MPLPYxxxYEGLA and the C-terminal PxY motifs are both well conserved, suggesting orthology with conserved function.


Pssm-ID: 469143 [Multi-domain]  Cd Length: 304  Bit Score: 309.47  E-value: 2.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199   1 MTRQGQAILALARVLADAKPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAAQLEARGRLGTFVAALDYVRLWQLGYQ 80
Cdd:NF041241   4 LKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLVKIDYKKLLELAGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  81 RPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAHGFTATMVLALG 160
Cdd:NF041241  84 GTIVGAMPLPYSRLYEGLATGLYAAFEKAGIPLNLAYMRGAKVRIEALLNGRYDFAVVSKLAAEQYIEEGEDLEIALDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 161 AYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDAVVWtdlNTPAL 240
Cdd:NF041241 164 PGSYVSEHVLLFRDGEKKEIRDGMRVGIDSSSLDQKILTEAEFEGKDVELVELSYNQLLDALAKGEIDAAVW---NLDEI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199 241 PDN---ITITPLTtdDDPMLSALSEAVLVVDPARPASAHLLQALLDVPALLEIQNEVIHRTRIPSY 303
Cdd:NF041241 241 KDKklgLNYQPLK--SEKANKDASEAVIVVRKDNEEIKALLRKLIDVEKVLAIQKKVLEGEIIPSY 304
PBP2_Yhfz cd13533
Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 ...
70-292 2.01e-70

Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 periplasmic-binding protein fold; This subfamily contains periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270251  Cd Length: 222  Bit Score: 217.53  E-value: 2.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  70 DYVRLWQLGYQRPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAH 149
Cdd:cd13533    1 DYKKLLEIAGIGSLVGAMPLPYSRRYEGLATGLYAQFEELKIPFNLAYMRGADNRIEALLEGRYDFAVVSRLAAEQAVDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 150 GFTATMVLALGAYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDA 229
Cdd:cd13533   81 GKDIEIVLELGPGTYVSQHVLLFRDPEDKEIQDGMRVGIDPSSADQRILTHRECEGKKVELVEINYNQLLQLLKSGEIDA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381384199 230 VVWTDLNTPALPDNITITPLTTDDDPMLSAlSEAVLVVDPARPASAHLLQALLDVPALLEIQN 292
Cdd:cd13533  161 AIWNLDEIQSKNLGLNYVPLKDEDARALRA-TEAVIVIRKGNPFLKRLLRALIDFPEVLEIQK 222
HTH_41 pfam14502
Helix-turn-helix domain;
19-66 1.80e-11

Helix-turn-helix domain;


Pssm-ID: 433997 [Multi-domain]  Cd Length: 48  Bit Score: 58.27  E-value: 1.80e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 381384199   19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAAQLEARGRLGTFV 66
Cdd:pfam14502   1 KAGERLPTISEYSHKFELSVGTVQKALKKLEDMKAIQLERRGHNGTYL 48
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
67-270 2.00e-08

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 54.63  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  67 AALDYVRLwQLGYQrPVVGALPLPYSRHvEGLatalhaqFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETA 146
Cdd:COG0715   17 AAAEKVTL-RLGWL-PNTDHAPLYVAKE-KGY-------FKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 147 HAHGFTATMVLALGAYTYLAghVLLLRDPMTHTLRD--GHRLGVDFLSADHTYISRAVSRG----KHVELVSIQYDQALE 220
Cdd:COG0715   87 RAKGAPVKAVAALSQSGGNA--LVVRKDSGIKSLADlkGKKVAVPGGSTSHYLLRALLAKAgldpKDVEIVNLPPPDAVA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 381384199 221 LLAAGAIDAVVWTDLNTPALPDNITITPLTTDDDpMLSALSEAVLVVDPA 270
Cdd:COG0715  165 ALLAGQVDAAVVWEPFESQAEKKGGGRVLADSAD-LVPGYPGDVLVASED 213
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
19-68 6.02e-06

DNA-binding transcriptional regulator YhcF, GntR family [Transcription];


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 44.40  E-value: 6.02e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 381384199  19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFVAA 68
Cdd:COG1725   29 KPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGL--IETRRGKGTFVAE 76
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
19-67 2.98e-05

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 41.28  E-value: 2.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 381384199  19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFVA 67
Cdd:cd07377   20 KPGDRLPSERELAEELGVSRTTVREALRELEAEGL--VERRPGRGTFVA 66
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-66 2.42e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 35.63  E-value: 2.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 381384199    19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFV 66
Cdd:smart00345  15 RPGDKLPSERELAAQLGVSRTTVREALSRLEAEGL--VQRRPGSGTFV 60
 
Name Accession Description Interval E-value
YhfZ_C pfam14503
YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix ...
70-303 1.04e-105

YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix domain HTH_41 (pfam14502). It includes YhfZ proteins from Escherichia coli and Shigella flexneri.


Pssm-ID: 433998  Cd Length: 236  Bit Score: 307.67  E-value: 1.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199   70 DYVRLWQLGYQRPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAH 149
Cdd:pfam14503   1 DYKKLWELAGLGNLVGAMPLPYSRRYEGLATGLKAQFEDLGIPFNFAYMRGADVRLEALKEGRYDFAVVSRLAAERYLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  150 GFTATMVLALGAYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDA 229
Cdd:pfam14503  81 GPGLEIALELGPGTYVSAHVLLLRDGEKTEIKDGMRVGIDSNSADQRILTEAEFEGKDVEFVEIPYMQLLELLLAGDIDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199  230 VVW--TDLNTPALPDNITITPLTTDDDPMLSALSEAVLVVDPARPASAHLLQALLDVPALLEIQNEVIHRTRIPSY 303
Cdd:pfam14503 161 VVWnlDEVQDPLELGLRALPLTSLDARPIVEQASEAVLVIRKDNPGLKALLRNLIDVEAVLEIQKKVLEGERIPSY 236
YhfZ_full NF041241
GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional ...
1-303 2.23e-105

GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional regulator YhfZ from Escherichia coli, with an N-terminal GntR-like domain, are quite divergent. See PF14503 (YhfZ_C) for the broader family. This HMM identifies a subset in which the motif MPLPYxxxYEGLA and the C-terminal PxY motifs are both well conserved, suggesting orthology with conserved function.


Pssm-ID: 469143 [Multi-domain]  Cd Length: 304  Bit Score: 309.47  E-value: 2.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199   1 MTRQGQAILALARVLADAKPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAAQLEARGRLGTFVAALDYVRLWQLGYQ 80
Cdd:NF041241   4 LKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLVKIDYKKLLELAGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  81 RPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAHGFTATMVLALG 160
Cdd:NF041241  84 GTIVGAMPLPYSRLYEGLATGLYAAFEKAGIPLNLAYMRGAKVRIEALLNGRYDFAVVSKLAAEQYIEEGEDLEIALDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 161 AYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDAVVWtdlNTPAL 240
Cdd:NF041241 164 PGSYVSEHVLLFRDGEKKEIRDGMRVGIDSSSLDQKILTEAEFEGKDVELVELSYNQLLDALAKGEIDAAVW---NLDEI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199 241 PDN---ITITPLTtdDDPMLSALSEAVLVVDPARPASAHLLQALLDVPALLEIQNEVIHRTRIPSY 303
Cdd:NF041241 241 KDKklgLNYQPLK--SEKANKDASEAVIVVRKDNEEIKALLRKLIDVEKVLAIQKKVLEGEIIPSY 304
PBP2_Yhfz cd13533
Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 ...
70-292 2.01e-70

Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 periplasmic-binding protein fold; This subfamily contains periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270251  Cd Length: 222  Bit Score: 217.53  E-value: 2.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  70 DYVRLWQLGYQRPVVGALPLPYSRHVEGLATALHAQFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAH 149
Cdd:cd13533    1 DYKKLLEIAGIGSLVGAMPLPYSRRYEGLATGLYAQFEELKIPFNLAYMRGADNRIEALLEGRYDFAVVSRLAAEQAVDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 150 GFTATMVLALGAYTYLAGHVLLLRDPMTHTLRDGHRLGVDFLSADHTYISRAVSRGKHVELVSIQYDQALELLAAGAIDA 229
Cdd:cd13533   81 GKDIEIVLELGPGTYVSQHVLLFRDPEDKEIQDGMRVGIDPSSADQRILTHRECEGKKVELVEINYNQLLQLLKSGEIDA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381384199 230 VVWTDLNTPALPDNITITPLTTDDDPMLSAlSEAVLVVDPARPASAHLLQALLDVPALLEIQN 292
Cdd:cd13533  161 AIWNLDEIQSKNLGLNYVPLKDEDARALRA-TEAVIVIRKGNPFLKRLLRALIDFPEVLEIQK 222
HTH_41 pfam14502
Helix-turn-helix domain;
19-66 1.80e-11

Helix-turn-helix domain;


Pssm-ID: 433997 [Multi-domain]  Cd Length: 48  Bit Score: 58.27  E-value: 1.80e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 381384199   19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAAQLEARGRLGTFV 66
Cdd:pfam14502   1 KAGERLPTISEYSHKFELSVGTVQKALKKLEDMKAIQLERRGHNGTYL 48
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
67-270 2.00e-08

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 54.63  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  67 AALDYVRLwQLGYQrPVVGALPLPYSRHvEGLatalhaqFAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETA 146
Cdd:COG0715   17 AAAEKVTL-RLGWL-PNTDHAPLYVAKE-KGY-------FKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 147 HAHGFTATMVLALGAYTYLAghVLLLRDPMTHTLRD--GHRLGVDFLSADHTYISRAVSRG----KHVELVSIQYDQALE 220
Cdd:COG0715   87 RAKGAPVKAVAALSQSGGNA--LVVRKDSGIKSLADlkGKKVAVPGGSTSHYLLRALLAKAgldpKDVEIVNLPPPDAVA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 381384199 221 LLAAGAIDAVVWTDLNTPALPDNITITPLTTDDDpMLSALSEAVLVVDPA 270
Cdd:COG0715  165 ALLAGQVDAAVVWEPFESQAEKKGGGRVLADSAD-LVPGYPGDVLVASED 213
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
19-68 6.02e-06

DNA-binding transcriptional regulator YhcF, GntR family [Transcription];


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 44.40  E-value: 6.02e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 381384199  19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFVAA 68
Cdd:COG1725   29 KPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGL--IETRRGKGTFVAE 76
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
19-67 2.98e-05

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 41.28  E-value: 2.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 381384199  19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFVA 67
Cdd:cd07377   20 KPGDRLPSERELAEELGVSRTTVREALRELEAEGL--VERRPGRGTFVA 66
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
98-231 8.89e-05

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 43.04  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  98 LATALhaqFAEAGVELTLRFMRgSSQRLQALAQGAVDWAllsrfaaetahAHGFTATM----VLALGAYTYLAGHVLLLR 173
Cdd:COG0834   28 LARAI---AKRLGLKVEFVPVP-WDRLIPALQSGKVDLI-----------IAGMTITPerekQVDFSDPYYTSGQVLLVR 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381384199 174 --DPMTHTLRD--GHRLGVdflSADHTYISRAVSRGKHVELVSIQ-YDQALELLAAGAIDAVV 231
Cdd:COG0834   93 kdNSGIKSLADlkGKTVGV---QAGTTYEEYLKKLGPNAEIVEFDsYAEALQALASGRVDAVV 152
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
106-231 1.11e-04

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 42.61  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 106 FAEAGVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAHGFTATMVLALgayTYLAGHVLLLRDPMTHTLRD--G 183
Cdd:cd13563   24 FKKEGLDVELVWFESYSDSMAALASGQIDAAATTLDDALAMAAKGVPVKIVLVL---DNSNGADGIVAKPGIKSIADlkG 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 381384199 184 HRLGVDFLSADHTYISRAVSRG----KHVELVSIQYDQALELLAAGAIDAVV 231
Cdd:cd13563  101 KTVAVEEGSVSHFLLLNALEKAglteKDVKIVNMTAGDAGAAFIAGQVDAAV 152
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
83-259 1.42e-04

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 42.18  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199  83 VVGALPLPysrHVEGLATALHAQFAEA-GVELTLRFMRGSSQRLQALAQGAVDWALLSR-FAAETAHAHGFTATMVLAlg 160
Cdd:cd00648    3 TVASIGPP---PYAGFAEDAAKQLAKEtGIKVELVPGSSIGTLIEALAAGDADVAVGPIaPALEAAADKLAPGGLYIV-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 161 AYTYLAGHVLLLRDP------MTHTLRDGHRLGVDFLSADHT-----YISRAVSRGKHVELVSIQ-YDQALELLAAGAID 228
Cdd:cd00648   78 PELYVGGYVLVVRKGssikglLAVADLDGKRVGVGDPGSTAVrqarlALGAYGLKKKDPEVVPVPgTSGALAAVANGAVD 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 381384199 229 A-VVWTDLNTPALPDNITITPLTTDDDPMLSA 259
Cdd:cd00648  158 AaIVWVPAAERAQLGNVQLEVLPDDLGPLVTT 189
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
19-66 2.08e-04

Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 38.75  E-value: 2.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 381384199   19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFV 66
Cdd:pfam00392  19 RPGDKLPSERELAAEFGVSRTTVREALRRLEAEGL--VERRQGRGTFV 64
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-68 8.56e-04

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 40.58  E-value: 8.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381384199   9 LALARVLADA------KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGaaQLEARGRLGTFVAA 68
Cdd:COG1167   15 LQLADALREAilsgrlPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEG--LIESRPGSGTFVAA 78
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-66 2.42e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 35.63  E-value: 2.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 381384199    19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFV 66
Cdd:smart00345  15 RPGDKLPSERELAAQLGVSRTTVREALSRLEAEGL--VQRRPGSGTFV 60
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
106-251 2.69e-03

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 38.42  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381384199 106 FAEA--GVELTLRFMRGSSQRLQALAQGAVDWALLSRFAAETAHAHGFTATMVLALGAYTYLAGhVLLLRDPMTHTLRD- 182
Cdd:cd01008   24 FEKEkeGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLAAAGGVPVVLIAALSRSPNGNG-IVVRKDSGITSLADl 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381384199 183 -GHRLGVDFLSADHTYISRAVSRG----KHVELVSIQYDQALELLAAGAIDAVVWTDLNTPALPDNITITPLTT 251
Cdd:cd01008  103 kGKKIAVTKGTTGHFLLLKALAKAglsvDDVELVNLGPADAAAALASGDVDAWVTWEPFLSLAEKGGDARIIVD 176
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
19-68 7.67e-03

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 37.15  E-value: 7.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 381384199  19 KPGDRLLPVQDYADLFHVGAGTVQHALDYLQDSGAaqLEARGRLGTFVAA 68
Cdd:COG2188   24 PPGDRLPSERELAEEFGVSRMTVRKALDELVEEGL--LERRQGRGTFVAE 71
 
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