NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|496851394|ref|WP_009385603|]
View 

MULTISPECIES: GntR family transcriptional regulator YhfZ [Vibrio]

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_full NF041241
GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional ...
4-298 5.38e-148

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: 417.32  E-value: 5.38e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394   4 QYISKEGAAIMNIAQYLMTTAEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGAVVLSKQGRNGTFISQLNYRELVSCA 83
Cdd:NF041241   2 KFLKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLVKIDYKKLLELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  84 GINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELAS---GLVTAID 158
Cdd:NF041241  82 GIGTIVGAMPLPYSRLYEGLATGLYAAFekAGIPLNLAYMRGAKVRIEALLNGRYDFAVVSKLAAEQYIEegeDLEIALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 159 LGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDAVVWLPEAIE 235
Cdd:NF041241 162 FGPGSYVSEHVLLFRDGEKKEIrdgMRVGIDSSSLDQKILTEAEFEGKDVELVELSYNQLLDALAKGEIDAAVWNLDEIK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496851394 236 MEKYGLAEQSLSHLPACMDASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQAVVNGQLTPSY 298
Cdd:NF041241 242 DKKLGLNYQPLKSEKANKDASEAVIVVRKDNEEIKALLRKLIDVEKVLAIQKKVLEGEIIPSY 304
 
Name Accession Description Interval E-value
YhfZ_full NF041241
GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional ...
4-298 5.38e-148

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: 417.32  E-value: 5.38e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394   4 QYISKEGAAIMNIAQYLMTTAEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGAVVLSKQGRNGTFISQLNYRELVSCA 83
Cdd:NF041241   2 KFLKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLVKIDYKKLLELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  84 GINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELAS---GLVTAID 158
Cdd:NF041241  82 GIGTIVGAMPLPYSRLYEGLATGLYAAFekAGIPLNLAYMRGAKVRIEALLNGRYDFAVVSKLAAEQYIEegeDLEIALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 159 LGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDAVVWLPEAIE 235
Cdd:NF041241 162 FGPGSYVSEHVLLFRDGEKKEIrdgMRVGIDSSSLDQKILTEAEFEGKDVELVELSYNQLLDALAKGEIDAAVWNLDEIK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496851394 236 MEKYGLAEQSLSHLPACMDASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQAVVNGQLTPSY 298
Cdd:NF041241 242 DKKLGLNYQPLKSEKANKDASEAVIVVRKDNEEIKALLRKLIDVEKVLAIQKKVLEGEIIPSY 304
YhfZ_C pfam14503
YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix ...
75-298 1.31e-90

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: 269.15  E-value: 1.31e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394   75 NYRELVSCAGINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAK-ELAS 151
Cdd:pfam14503   1 DYKKLWELAGLGNLVGAMPLPYSRRYEGLATGLKAQFedLGIPFNFAYMRGADVRLEALKEGRYDFAVVSRLAAErYLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  152 G--LVTAIDLGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDA 226
Cdd:pfam14503  81 GpgLEIALELGPGTYVSAHVLLLRDGEKTEIkdgMRVGIDSNSADQRILTEAEFEGKDVEFVEIPYMQLLELLLAGDIDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496851394  227 VVW----LPEAIEMEKYGLAEQSLSHLPACMDASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQAVVNGQLTPSY 298
Cdd:pfam14503 161 VVWnldeVQDPLELGLRALPLTSLDARPIVEQASEAVLVIRKDNPGLKALLRNLIDVEAVLEIQKKVLEGERIPSY 236
PBP2_Yhfz cd13533
Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 ...
75-287 3.65e-69

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: 214.06  E-value: 3.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  75 NYRELVSCAGINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELAS- 151
Cdd:cd13533    1 DYKKLLEIAGIGSLVGAMPLPYSRRYEGLATGLYAQFeeLKIPFNLAYMRGADNRIEALLEGRYDFAVVSRLAAEQAVDe 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 152 --GLVTAIDLGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDA 226
Cdd:cd13533   81 gkDIEIVLELGPGTYVSQHVLLFRDPEDKEIqdgMRVGIDPSSADQRILTHRECEGKKVELVEINYNQLLQLLKSGEIDA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496851394 227 VVWLPEAIEMEKYGLAEQSLSHLPACM-DASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQ 287
Cdd:cd13533  161 AIWNLDEIQSKNLGLNYVPLKDEDARAlRATEAVIVIRKGNPFLKRLLRALIDFPEVLEIQK 222
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
24-71 2.05e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 36.01  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 496851394    24 AEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGaVVLSKQGRnGTFI 71
Cdd:smart00345  15 RPGDKLPSERELAAQLGVSRTTVREALSRLEAEG-LVQRRPGS-GTFV 60
 
Name Accession Description Interval E-value
YhfZ_full NF041241
GntR family transcriptional regulator YhfZ; Full-length homologs of the transcriptional ...
4-298 5.38e-148

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: 417.32  E-value: 5.38e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394   4 QYISKEGAAIMNIAQYLMTTAEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGAVVLSKQGRNGTFISQLNYRELVSCA 83
Cdd:NF041241   2 KFLKKNGLAIIKLARELLSLKEGDRIPTISELAEKFGVSRGTVQNALKYLEESGAIKLESRGHLGTFLVKIDYKKLLELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  84 GINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELAS---GLVTAID 158
Cdd:NF041241  82 GIGTIVGAMPLPYSRLYEGLATGLYAAFekAGIPLNLAYMRGAKVRIEALLNGRYDFAVVSKLAAEQYIEegeDLEIALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 159 LGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDAVVWLPEAIE 235
Cdd:NF041241 162 FGPGSYVSEHVLLFRDGEKKEIrdgMRVGIDSSSLDQKILTEAEFEGKDVELVELSYNQLLDALAKGEIDAAVWNLDEIK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496851394 236 MEKYGLAEQSLSHLPACMDASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQAVVNGQLTPSY 298
Cdd:NF041241 242 DKKLGLNYQPLKSEKANKDASEAVIVVRKDNEEIKALLRKLIDVEKVLAIQKKVLEGEIIPSY 304
YhfZ_C pfam14503
YhfZ C-terminal domain; This domain is often found in association with the helix-turn-helix ...
75-298 1.31e-90

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: 269.15  E-value: 1.31e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394   75 NYRELVSCAGINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAK-ELAS 151
Cdd:pfam14503   1 DYKKLWELAGLGNLVGAMPLPYSRRYEGLATGLKAQFedLGIPFNFAYMRGADVRLEALKEGRYDFAVVSRLAAErYLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  152 G--LVTAIDLGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDA 226
Cdd:pfam14503  81 GpgLEIALELGPGTYVSAHVLLLRDGEKTEIkdgMRVGIDSNSADQRILTEAEFEGKDVEFVEIPYMQLLELLLAGDIDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496851394  227 VVW----LPEAIEMEKYGLAEQSLSHLPACMDASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQAVVNGQLTPSY 298
Cdd:pfam14503 161 VVWnldeVQDPLELGLRALPLTSLDARPIVEQASEAVLVIRKDNPGLKALLRNLIDVEAVLEIQKKVLEGERIPSY 236
PBP2_Yhfz cd13533
Substrate-binding domain of uncharacterized protein Yhfz from Shigella Flexneri; the type 2 ...
75-287 3.65e-69

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: 214.06  E-value: 3.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  75 NYRELVSCAGINNVVCAMPLPYTRHYEGLASGLKAQL--GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELAS- 151
Cdd:cd13533    1 DYKKLLEIAGIGSLVGAMPLPYSRRYEGLATGLYAQFeeLKIPFNLAYMRGADNRIEALLEGRYDFAVVSRLAAEQAVDe 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 152 --GLVTAIDLGAHTYSHEHRLIYRQGQYDQI---LRVGVDPDSPDQKILTSQAFADKSIEIVEIHYGESLTHLLNGDIDA 226
Cdd:cd13533   81 gkDIEIVLELGPGTYVSQHVLLFRDPEDKEIqdgMRVGIDPSSADQRILTHRECEGKKVELVEINYNQLLQLLKSGEIDA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496851394 227 VVWLPEAIEMEKYGLAEQSLSHLPACM-DASEAVMLVNGNAEHITLLLRKLLQLTPLLQHQQ 287
Cdd:cd13533  161 AIWNLDEIQSKNLGLNYVPLKDEDARAlRATEAVIVIRKGNPFLKRLLRALIDFPEVLEIQK 222
HTH_41 pfam14502
Helix-turn-helix domain;
25-71 2.17e-14

Helix-turn-helix domain;


Pssm-ID: 433997 [Multi-domain]  Cd Length: 48  Bit Score: 65.98  E-value: 2.17e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 496851394   25 EGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGAVVLSKQGRNGTFI 71
Cdd:pfam14502   2 AGERLPTISEYSHKFELSVGTVQKALKKLEDMKAIQLERRGHNGTYL 48
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
87-240 5.87e-09

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: 54.89  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394  87 NVVCAMPLPYtrHYEGLASGLKAQL---GGLPLYFAHMRGASVRAECLKNGTYDVAIMSKLAAKELASGLVTAIDLGAH- 162
Cdd:cd00648    1 TLTVASIGPP--PYAGFAEDAAKQLakeTGIKVELVPGSSIGTLIEALAAGDADVAVGPIAPALEAAADKLAPGGLYIVp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496851394 163 -TYSHEHRLIYRQG---------QYDQILRVGVDPDSPDQKILTSQAFA-----DKSIEIVEI-HYGESLTHLLNGDIDA 226
Cdd:cd00648   79 eLYVGGYVLVVRKGssikgllavADLDGKRVGVGDPGSTAVRQARLALGayglkKKDPEVVPVpGTSGALAAVANGAVDA 158
                        170
                 ....*....|....*
gi 496851394 227 -VVWLPEAIEMEKYG 240
Cdd:cd00648  159 aIVWVPAAERAQLGN 173
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
24-72 3.36e-04

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: 38.20  E-value: 3.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 496851394  24 AEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGaVVLSKQGRnGTFIS 72
Cdd:cd07377   20 KPGDRLPSERELAEELGVSRTTVREALRELEAEG-LVERRPGR-GTFVA 66
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
24-71 2.05e-03

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 36.01  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 496851394    24 AEGDRLRTIDSLSDDYSVSVGFIQKALTTIEQRGaVVLSKQGRnGTFI 71
Cdd:smart00345  15 RPGDKLPSERELAAQLGVSRTTVREALSRLEAEG-LVQRRPGS-GTFV 60
 
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