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Conserved domains on  [gi|446531836|ref|WP_000609182|]
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substrate-binding domain-containing protein [Bacillus cereus]

Protein Classification

HTH_17 and YvgK domain-containing protein( domain architecture ID 10578548)

HTH_17 and YvgK domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
17-314 1.02e-93

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


:

Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 281.12  E-value: 1.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  17 TAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQSKTGSLKNSAQLsekhnltNAIVISGQDMALDI 96
Cdd:COG1910   37 VKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELPLL-------TLVIIGSHDPLLDI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  97 LGKYMESSM-GERMLRAYDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYIIFNLLLRNVGFYVQKGN 175
Cdd:COG1910  110 LLRLLEKREsGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLINLARREQGLIVAKGN 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 176 PKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAMNKADVGIGIENVANITK 255
Cdd:COG1910  190 PKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGEADVGLGIEAAARAFG 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531836 256 VEFVPLIKEQYDLIILKNEHTVKIINEIKEILHSTEFKQELESIGGYDLTLTGETIYES 314
Cdd:COG1910  270 LDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYEA 328
 
Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
17-314 1.02e-93

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 281.12  E-value: 1.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  17 TAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQSKTGSLKNSAQLsekhnltNAIVISGQDMALDI 96
Cdd:COG1910   37 VKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELPLL-------TLVIIGSHDPLLDI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  97 LGKYMESSM-GERMLRAYDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYIIFNLLLRNVGFYVQKGN 175
Cdd:COG1910  110 LLRLLEKREsGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLINLARREQGLIVAKGN 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 176 PKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAMNKADVGIGIENVANITK 255
Cdd:COG1910  190 PKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGEADVGLGIEAAARAFG 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531836 256 VEFVPLIKEQYDLIILKNEHTVKIINEIKEILHSTEFKQELESIGGYDLTLTGETIYES 314
Cdd:COG1910  270 LDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYEA 328
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 97-273 5.09e-68

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 210.51  E-value: 5.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836   97 LGKYMESSMGERMLRAYDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYIIFNLLLRNVGFYVQKGNP 176
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPGIPVVLINLAYREQGLVVAPGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  177 KNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAMNKADVGIGIENVA-NITK 255
Cdd:pfam12727  81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAArALGG 160

                         170
                  ....*....|....*...
gi 446531836  256 VEFVPLIKEQYDLIILKN 273
Cdd:pfam12727 161 LDFIPLARERYDLVIPKE 178
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 83-299 7.88e-57

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 193.89  E-value: 7.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  83 NAIVISG-QDMALDILGKYMessmGERMLRA---YDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYI 158
Cdd:PRK14498 417 PTLVIIGsHDPGLDLLLDLL----ARRGLRLrslHVGSMGGLMALKRGEADIAGIHLLDPETGEYNIPYIKKYLLGEDAV 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 159 IFNLLLRNVGFYVQKGNPKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAM 238
Cdd:PRK14498 493 LVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERINGYDREEKTHMAVAAAVAQ 572

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531836 239 NKADVGIGIENVANITKVEFVPLIKEQYDLIILKnEHTVK-IINEIKEILHSTEFKQELESI 299
Cdd:PRK14498 573 GRADAGLGIRAAAKALGLDFIPLAEEEYDLLIPK-ERLEKpAVRAFLEALKSPEFKAALEEL 633
excise TIGR01764
DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein ...
 16-63 3.07e-13

DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376). [Unknown function, General]


Pssm-ID: 200128  Cd Length: 49  Bit Score: 63.00  E-value: 3.07e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446531836   16 YTAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQ 63
Cdd:TIGR01764   2 LTVEEAAEYLGVSKSTVYRLIEEGELPAYRVGRHYRIPREDVDEYLEQ 49
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 167-193 3.29e-05

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP 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 CysP 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: 270226  Cd Length: 307  Bit Score: 45.00  E-value: 3.29e-05
                         10        20
                 ....*....|....*....|....*..
gi 446531836 167 VGFYVQKGNPKNIKAWEDLCREDVKIV 193
Cdd:cd01005   97 IVFLVRKGNPKGIRDWDDLVKPGVSVI 123
 
Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
17-314 1.02e-93

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 281.12  E-value: 1.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  17 TAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQSKTGSLKNSAQLsekhnltNAIVISGQDMALDI 96
Cdd:COG1910   37 VKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELPLL-------TLVIIGSHDPLLDI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  97 LGKYMESSM-GERMLRAYDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYIIFNLLLRNVGFYVQKGN 175
Cdd:COG1910  110 LLRLLEKREsGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLINLARREQGLIVAKGN 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 176 PKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAMNKADVGIGIENVANITK 255
Cdd:COG1910  190 PKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGEADVGLGIEAAARAFG 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531836 256 VEFVPLIKEQYDLIILKNEHTVKIINEIKEILHSTEFKQELESIGGYDLTLTGETIYES 314
Cdd:COG1910  270 LDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYEA 328
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 97-273 5.09e-68

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 210.51  E-value: 5.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836   97 LGKYMESSMGERMLRAYDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYIIFNLLLRNVGFYVQKGNP 176
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPGIPVVLINLAYREQGLVVAPGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  177 KNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAMNKADVGIGIENVA-NITK 255
Cdd:pfam12727  81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAArALGG 160

                         170
                  ....*....|....*...
gi 446531836  256 VEFVPLIKEQYDLIILKN 273
Cdd:pfam12727 161 LDFIPLARERYDLVIPKE 178
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 83-299 7.88e-57

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 193.89  E-value: 7.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  83 NAIVISG-QDMALDILGKYMessmGERMLRA---YDGSLTSLIRLYKGEGSIVSLHLFDGDTKEYNVPYTKRILTNSQYI 158
Cdd:PRK14498 417 PTLVIIGsHDPGLDLLLDLL----ARRGLRLrslHVGSMGGLMALKRGEADIAGIHLLDPETGEYNIPYIKKYLLGEDAV 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 159 IFNLLLRNVGFYVQKGNPKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIHRKKIKGYDYEESSHFSIATSVAM 238
Cdd:PRK14498 493 LVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERINGYDREEKTHMAVAAAVAQ 572

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531836 239 NKADVGIGIENVANITKVEFVPLIKEQYDLIILKnEHTVK-IINEIKEILHSTEFKQELESI 299
Cdd:PRK14498 573 GRADAGLGIRAAAKALGLDFIPLAEEEYDLLIPK-ERLEKpAVRAFLEALKSPEFKAALEEL 633
HTH_17 pfam12728
Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.
 16-65 2.89e-14

Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.


Pssm-ID: 463684 [Multi-domain]  Cd Length: 51  Bit Score: 65.94  E-value: 2.89e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446531836   16 YTAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQSK 65
Cdd:pfam12728   2 LTVEEAAELLGVSRRTVYRLIRSGELPAAKIGRRWRIRKSDLEEWLERRR 51
excise TIGR01764
DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein ...
 16-63 3.07e-13

DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376). [Unknown function, General]


Pssm-ID: 200128  Cd Length: 49  Bit Score: 63.00  E-value: 3.07e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446531836   16 YTAEEAAKKLKISKLTVYELIKRGELPSYRIGRQVRIDVEDLQKYIEQ 63
Cdd:TIGR01764   2 LTVEEAAEYLGVSKSTVYRLIEEGELPAYRVGRHYRIPREDVDEYLEQ 49
AlpA COG3311
DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];
16-68 2.41e-09

DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];


Pssm-ID: 442540 [Multi-domain]  Cd Length: 64  Bit Score: 52.62  E-value: 2.41e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446531836  16 YTAEEAAKKLKISKLTVYELIKRGELP-SYRIG-RQVRIDVEDLQKYIEQSKTGS 68
Cdd:COG3311    9 LRLKEVAELLGVSRSTIYRLIKKGEFPkPVKLGgRSVRWRESEVEAWLAARIAAS 63
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 162-264 4.39e-07

Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443645  Cd Length: 232  Bit Score: 49.98  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 162 LLLRNVGFYVQKGNPKNIKAWEDLCREDVKIVNREvGAGIR-VLLDEQLRIHNIH-----RKKIKgyDYEESSHFSIATS 235
Cdd:COG4588   81 LYLRPAAILVRPGNPKNIKGFEDLLKPGVKIVVVN-GAGQTgVWEDIAGRTGDIEtvqafRSNIV--AYAPNSGAARKAW 157

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446531836 236 VAMNKADVGI--GIENVANITKVEFVPLIKE 264
Cdd:COG4588  158 TQDPDIDAWItwNIWQKANPDLADLVEIEPD 188
PRK10852 PRK10852
thiosulfate ABC transporter substrate-binding protein CysP;
168-193 1.40e-06

thiosulfate ABC transporter substrate-binding protein CysP;


Pssm-ID: 236775  Cd Length: 338  Bit Score: 48.98  E-value: 1.40e-06
                         10        20
                 ....*....|....*....|....*.
gi 446531836 168 GFYVQKGNPKNIKAWEDLCREDVKIV 193
Cdd:PRK10852 123 AFLVRKGNPKNIHDWNDLVRSDVKLI 148
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 169-193 6.47e-06

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441221  Cd Length: 340  Bit Score: 47.04  E-value: 6.47e-06
                         10        20
                 ....*....|....*....|....*
gi 446531836 169 FYVQKGNPKNIKAWEDLCREDVKIV 193
Cdd:COG1613  129 FLVRKGNPKGIKDWDDLVKPGVSVI 153
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 167-193 3.29e-05

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP 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 CysP 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: 270226  Cd Length: 307  Bit Score: 45.00  E-value: 3.29e-05
                         10        20
                 ....*....|....*....|....*..
gi 446531836 167 VGFYVQKGNPKNIKAWEDLCREDVKIV 193
Cdd:cd01005   97 IVFLVRKGNPKGIRDWDDLVKPGVSVI 123
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
 167-193 5.39e-05

sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions]


Pssm-ID: 130044  Cd Length: 315  Bit Score: 44.19  E-value: 5.39e-05
                          10        20
                  ....*....|....*....|....*..
gi 446531836  167 VGFYVQKGNPKNIKAWEDLCREDVKIV 193
Cdd:TIGR00971 105 IVFLVRKGNPKQIHDWNDLIKPGVSVI 131
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 162-264 1.04e-04

Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera.


Pssm-ID: 270237 [Multi-domain]  Cd Length: 227  Bit Score: 42.68  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 162 LLLRNVGFYVQKGNPKNIKAWEDLCREDVKIVNREVGAGIRVLLDEQLRIHNIH-----RKKIkgYDYEESSHFSIATSV 236
Cdd:cd13519   77 LYLRPSAILVRKGNPKKIKGLKDLLKPGVKILVVNGAGQTGLWEDMAGRTGDIEtvrafRKNI--VVFAKNSGAARKAWK 154

                         90       100       110
                 ....*....|....*....|....*....|
gi 446531836 237 AMNKADVGIG--IENVANITKVEFVPLIKE 264
Cdd:cd13519  155 QDPNIDAWITwnIWQKANPDIADFVELEKD 184
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
 171-265 2.49e-04

Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA 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: 270235 [Multi-domain]  Cd Length: 223  Bit Score: 41.44  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836 171 VQKGNPKNIKAWEDLCREDVKIV--NRE---VGAGIRVLLdEQLRIHNIHRKKIKGY--DYEEsshfsIATSVAMNKADV 243
Cdd:cd13517   84 VPKGNPKNITSLEDLAKPGVKVAlgDPKaaaIGKYAKKIL-EKNGLWEKVKKNVVVYtaTVNQ-----LLTYVLLGQVDA 157

                         90       100
                 ....*....|....*....|....
gi 446531836 244 GIGIENVA--NITKVEFVPLIKEQ 265
Cdd:cd13517  158 AIVWEDFAywNPGKVEVIPIPKEQ 181
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
 167-186 1.44e-03

Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 39.53  E-value: 1.44e-03
                         10        20
                 ....*....|....*....|
gi 446531836 167 VGFYVQKGNPKNIKAWEDLC 186
Cdd:cd01004   89 LGVLVAKGNPKKIKSPEDLC 108
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 171-261 1.48e-03

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 39.17  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531836  171 VQKGNPKNIKAWEDLCREDVKIV--NREVGAG---IRVLLDeqlRIHNIHRKKIKGYDYEESShFSIATSVAMNKADVGI 245
Cdd:pfam13531  84 VPKGNPKDISGLADLLKPGVRLAvaDPKTAPSgraALELLE---KAGLLKALEKKVVVLGENV-RQALTAVASGEADAGI 159

                          90       100
                  ....*....|....*....|
gi 446531836  246 GIENVA----NITKVEFVPL 261
Cdd:pfam13531 160 VYLSEAlfpeNGPGLEVVPL 179
 
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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