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Conserved domains on  [gi|2527612588|ref|WP_288612734|]
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MetQ/NlpA family ABC transporter substrate-binding protein, partial [uncultured Lactiplantibacillus sp.]

Protein Classification

MetQ/NlpA family ABC transporter substrate-binding protein( domain architecture ID 10003704)

MetQ/NlpA family ABC transporter substrate-binding protein ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including methionine; belongs to the type 2 periplasmic binding fold protein superfamily (PBP2)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NlpA COG1464
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ...
1-181 1.94e-67

ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];


:

Pssm-ID: 441073 [Multi-domain]  Cd Length: 270  Bit Score: 206.50  E-value: 1.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588   1 MKRLAWWLIGIAAIVGI--CVGlheiTSYSARAQQSATITVGSMGSDY-EVWQHIAKsqDAKKMGLTIKVKQITDGVQLN 77
Cdd:COG1464     1 MKKLLALLLALALALALaaCGS----SSAAAAAADKKTIKVGATPGPHaEILEVVKP--ELAKKGIDLEIVEFTDYVQPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  78 KATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKA 157
Cdd:COG1464    75 EALADGEIDANYFQHIPYLDNFNKEN-GYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKA 153
                         170       180
                  ....*....|....*....|....
gi 2527612588 158 GLIKLAANFGVLGSVKDITSNPRH 181
Cdd:COG1464   154 GLIKLKDGVGLLATVKDITENPKN 177
 
Name Accession Description Interval E-value
NlpA COG1464
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ...
1-181 1.94e-67

ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];


Pssm-ID: 441073 [Multi-domain]  Cd Length: 270  Bit Score: 206.50  E-value: 1.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588   1 MKRLAWWLIGIAAIVGI--CVGlheiTSYSARAQQSATITVGSMGSDY-EVWQHIAKsqDAKKMGLTIKVKQITDGVQLN 77
Cdd:COG1464     1 MKKLLALLLALALALALaaCGS----SSAAAAAADKKTIKVGATPGPHaEILEVVKP--ELAKKGIDLEIVEFTDYVQPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  78 KATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKA 157
Cdd:COG1464    75 EALADGEIDANYFQHIPYLDNFNKEN-GYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKA 153
                         170       180
                  ....*....|....*....|....
gi 2527612588 158 GLIKLAANFGVLGSVKDITSNPRH 181
Cdd:COG1464   154 GLIKLKDGVGLLATVKDITENPKN 177
Lipoprotein_9 pfam03180
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ...
37-181 1.83e-56

NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. It contains several antigenic members, that may be involved in bacterial virulence. This entry includes the D-methionine binding lipoprotein MetQ, which is the substrate-binding component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Other members of this family, such as NlpA, have been identified as putative substrate-binding components of ABC transporters. NlpA, is an inner-membrane-anchored lipoprotein that has been shown to have a minor role in methionine import.


Pssm-ID: 427184  Cd Length: 236  Bit Score: 177.46  E-value: 1.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSMGSDYEVWQHIAKsQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNPKaKLAALGTTYL 116
Cdd:pfam03180   1 LKVGATPGPHAEILEVAK-PLLKKKGLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGL-DLVAVGNVHI 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527612588 117 EPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:pfam03180  79 EPMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGKGLLATVKDITENPKN 143
PBP2_lipoprotein_GmpC cd13596
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; ...
36-181 1.47e-52

The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; contains the type 2 periplasmic-binding protein fold; This group includes the membrane-associated lipoprotein-9 from Staphylococcus aureus that binds the dipeptide glycylmethionine (GlyMet). The lipoprotein-9 has both structural and sequential homology to the MetQ family of substrate-binding protein. The GlyMet binding protein belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270314  Cd Length: 230  Bit Score: 167.54  E-value: 1.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  36 TITVGSMGSDYEVWQHIAksQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTY 115
Cdd:cd13596     1 TVKIGVTGEDTDIWDKIV--EEAEEAGIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKN-NADLTAIGDTV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527612588 116 LEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:cd13596    78 IAPMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFPTVNDITENPKN 143
metQ PRK11063
D-methionine ABC transporter substrate-binding protein MetQ;
37-181 1.45e-30

D-methionine ABC transporter substrate-binding protein MetQ;


Pssm-ID: 182939 [Multi-domain]  Cd Length: 271  Bit Score: 112.16  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSM-GSDYEVWQhIAKSQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYqtyNQQ--NPKAKLAALGT 113
Cdd:PRK11063   33 IKVGVIvGAEQQVAE-VAQKVAKEKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYL---DQQikDRGYKLVAVGN 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527612588 114 TYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:PRK11063  109 TFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDIVENPKN 176
 
Name Accession Description Interval E-value
NlpA COG1464
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ...
1-181 1.94e-67

ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];


Pssm-ID: 441073 [Multi-domain]  Cd Length: 270  Bit Score: 206.50  E-value: 1.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588   1 MKRLAWWLIGIAAIVGI--CVGlheiTSYSARAQQSATITVGSMGSDY-EVWQHIAKsqDAKKMGLTIKVKQITDGVQLN 77
Cdd:COG1464     1 MKKLLALLLALALALALaaCGS----SSAAAAAADKKTIKVGATPGPHaEILEVVKP--ELAKKGIDLEIVEFTDYVQPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  78 KATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKA 157
Cdd:COG1464    75 EALADGEIDANYFQHIPYLDNFNKEN-GYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKA 153
                         170       180
                  ....*....|....*....|....
gi 2527612588 158 GLIKLAANFGVLGSVKDITSNPRH 181
Cdd:COG1464   154 GLIKLKDGVGLLATVKDITENPKN 177
Lipoprotein_9 pfam03180
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ...
37-181 1.83e-56

NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. It contains several antigenic members, that may be involved in bacterial virulence. This entry includes the D-methionine binding lipoprotein MetQ, which is the substrate-binding component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Other members of this family, such as NlpA, have been identified as putative substrate-binding components of ABC transporters. NlpA, is an inner-membrane-anchored lipoprotein that has been shown to have a minor role in methionine import.


Pssm-ID: 427184  Cd Length: 236  Bit Score: 177.46  E-value: 1.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSMGSDYEVWQHIAKsQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNPKaKLAALGTTYL 116
Cdd:pfam03180   1 LKVGATPGPHAEILEVAK-PLLKKKGLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGL-DLVAVGNVHI 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527612588 117 EPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:pfam03180  79 EPMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGKGLLATVKDITENPKN 143
PBP2_lipoprotein_GmpC cd13596
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; ...
36-181 1.47e-52

The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; contains the type 2 periplasmic-binding protein fold; This group includes the membrane-associated lipoprotein-9 from Staphylococcus aureus that binds the dipeptide glycylmethionine (GlyMet). The lipoprotein-9 has both structural and sequential homology to the MetQ family of substrate-binding protein. The GlyMet binding protein belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270314  Cd Length: 230  Bit Score: 167.54  E-value: 1.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  36 TITVGSMGSDYEVWQHIAksQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTY 115
Cdd:cd13596     1 TVKIGVTGEDTDIWDKIV--EEAEEAGIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKN-NADLTAIGDTV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527612588 116 LEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:cd13596    78 IAPMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFPTVNDITENPKN 143
PBP2_lipoprotein_MetQ_like cd13526
The periplasmic-binding component of ABC-type methionine uptake transporter system and its ...
36-181 3.04e-48

The periplasmic-binding component of ABC-type methionine uptake transporter system and its related lipoproteins; the type 2 periplasmic-binding protein fold; This family represents the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ) and its related homologs. Members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270244  Cd Length: 228  Bit Score: 156.32  E-value: 3.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  36 TITVGSMGSDYEVWQHIAKsQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTY 115
Cdd:cd13526     1 KLKIGVTAGPSADVVEAAK-KEAKKKGYELELVVFTDYVAPNEALNDGSIDANFFQHVPFLDQFNKER-NGDLVKVGKTV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527612588 116 LEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:cd13526    79 IAPIGLYSKKYKSLDELPDGARIAIPNDPSNGARALLLLEDAGLIKLKDGVGLFATVLDITENPKN 144
PBP2_lipoprotein_Tp32 cd13597
The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum ...
47-181 5.75e-46

The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum binds L-methionine; the type 2 periplasmic-binding protein fold; This group includes the lipoprotein Tp32, a periplasmic component of a methionine uptake transporter system, and its closely related homologs. The Tp32 has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus it belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270315  Cd Length: 236  Bit Score: 150.89  E-value: 5.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  47 EVWQHIAKsqDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTYLEPMGIYSKKY 126
Cdd:cd13597    13 EILEFIKP--ELKKQGIDLEIVEFTDYVQPNTALADGELDANYFQHVPYLESFNKEK-GYDLVAVAGVHLEPMGLYSKKY 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2527612588 127 QSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:cd13597    90 KSLEDLPDGATIAIPNDPTNQGRALLLLEEAGLITLKDGAGLTATVKDIVKNPKN 144
PBP2_lipoprotein_IlpA_like cd13598
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar ...
37-181 4.66e-41

Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar lipoproteins; the type 2 periplasmic binding protein fold; This group includes the IlpA protein which has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270316  Cd Length: 227  Bit Score: 137.87  E-value: 4.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSM-GSDYEVWQHIAKSqdAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSwsyyQTYNQQNPKA---KLAALG 112
Cdd:cd13598     2 IKVGVIrGPDAQIWEVVQKV--AKEKGLDVELVTFNDYAQPNEALAAGDLDANAFQH----KPYLDAQIKArgyKLVIVG 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527612588 113 TTYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:cd13598    76 NTFVYPIGLYSKKIKSLAELPNGATVAIPNDPSNEGRALLLLQKEGLIKLKDGVGLLATVRDIAENPKK 144
PBP2_lipoprotein_Gna1946 cd13599
The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 ...
36-181 7.79e-35

The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 periplasmic binding protein fold; Gna1946 shares significant structural and sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270317  Cd Length: 228  Bit Score: 122.12  E-value: 7.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  36 TITVGSMGSDYE--VWQHIAKSQDAKkmGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGT 113
Cdd:cd13599     1 TIVIGFTPGPYGdmVKNGVAPYLEKK--GYEVKLKEFTDYVQPNNALANGEIDANVFQHKPYLDAFNKEN-GLDLVGIVQ 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527612588 114 TYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVL-GSVKDITSNPRH 181
Cdd:cd13599    78 VPTPPMGLYSNKHKSLEEVKDGATVAIPNDPSNLARALVMLQDLGWITLKDNIDPLkASVNDIAENPKN 146
PBP2_lipoprotein_like_1 cd13600
Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; ...
36-180 2.67e-31

Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; the type 2 periplasmic binding protein fold; This subgroup shares significant sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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 PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270318  Cd Length: 228  Bit Score: 112.81  E-value: 2.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  36 TITVGS-MGSDYEVWQHIAksQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNPkAKLAALGTT 114
Cdd:cd13600     1 TLKVATnSGPMTEILEYIA--AELAPDGITIEPVQVSDYVQANRAVAAGEIDANFFQHQPFMEQFNEANG-FELVAVQPI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527612588 115 YLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVL-GSVKDITSNPR 180
Cdd:cd13600    78 YHWAFGFYSKKYKSVEDLPDGAKVAIPNDPANQARALLLLQRAGLITLKPGVDPTtATLADIVTNPK 144
metQ PRK11063
D-methionine ABC transporter substrate-binding protein MetQ;
37-181 1.45e-30

D-methionine ABC transporter substrate-binding protein MetQ;


Pssm-ID: 182939 [Multi-domain]  Cd Length: 271  Bit Score: 112.16  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSM-GSDYEVWQhIAKSQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYqtyNQQ--NPKAKLAALGT 113
Cdd:PRK11063   33 IKVGVIvGAEQQVAE-VAQKVAKEKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYL---DQQikDRGYKLVAVGN 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527612588 114 TYLEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:PRK11063  109 TFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDIVENPKN 176
PRK09861 PRK09861
lipoprotein NlpA;
37-181 1.01e-29

lipoprotein NlpA;


Pssm-ID: 182119  Cd Length: 272  Bit Score: 110.11  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  37 ITVGSM-GSDYEVWQhIAKSQDAKKMGLTIKVKQITDGVQLNKATADGNVDVNAFQSWSYYQTYNQQNpKAKLAALGTTY 115
Cdd:PRK09861   34 IKVGVInGAEQDVAE-VAKKVAKEKYGLDVELVGFSGSLLPNDATNHGELDANVFQHRPFLEQDNQAH-GYKLVAVGNTF 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527612588 116 LEPMGIYSKKYQSVDEIPDGATIAIADNPSQASRGLLLLQKAGLIKLAANFGVLGSVKDITSNPRH 181
Cdd:PRK09861  112 VFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRH 177
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
26-159 3.74e-04

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 39.99  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527612588  26 SYSARAQQSATITVGSMGSDYEVWQHIAKSQDA-KKMGLTIKVKQITDGVQLNKATADGNVDVNAfqsWSYYQTYNQQNP 104
Cdd:COG0715    13 SAAAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYfKKEGLDVELVEFAGGAAALEALAAGQADFGV---AGAPPALAARAK 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2527612588 105 KAKLAALGTTYL-EPMGIYSKKYQSVDEIPD--GATIAIADNPSQASRGLLLLQKAGL 159
Cdd:COG0715    90 GAPVKAVAALSQsGGNALVVRKDSGIKSLADlkGKKVAVPGGSTSHYLLRALLAKAGL 147
 
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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