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Conserved domains on  [gi|15831026|ref|NP_309799|]
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porcine attaching-effacing associated protein Paa/adherence factor AdfO [Escherichia coli O157:H7 str. Sakai]

Protein Classification

AcfC family protein( domain architecture ID 10790690)

AcfC family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 15-249 1.79e-127

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


:

Pssm-ID: 443645  Cd Length: 232  Bit Score: 360.45  E-value: 1.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  15 AAYADINLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNADILFGASEQSALAIIRDHKDSFSEKDIQP 94
Cdd:COG4588   1 AAAAVINVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGAFDSKDVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  95 LYLRKSILLVKKGNPKNIRSIDDLTRPGIGVIVNDGGGTsntsgTGVWEDIAGRKGNIETVAAIRKNIILYAPNSGTARK 174
Cdd:COG4588  81 LYLRPAAILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQ-----TGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831026 175 ALENQPGADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQD--ANDETRRFAEWLQTDEAAPAFKKYGWTR 249
Cdd:COG4588 156 AWTQDPDIDAWITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKgkADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
 
Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 15-249 1.79e-127

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


Pssm-ID: 443645  Cd Length: 232  Bit Score: 360.45  E-value: 1.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  15 AAYADINLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNADILFGASEQSALAIIRDHKDSFSEKDIQP 94
Cdd:COG4588   1 AAAAVINVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGAFDSKDVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  95 LYLRKSILLVKKGNPKNIRSIDDLTRPGIGVIVNDGGGTsntsgTGVWEDIAGRKGNIETVAAIRKNIILYAPNSGTARK 174
Cdd:COG4588  81 LYLRPAAILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQ-----TGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831026 175 ALENQPGADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQD--ANDETRRFAEWLQTDEAAPAFKKYGWTR 249
Cdd:COG4588 156 AWTQDPDIDAWITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKgkADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 19-247 6.25e-118

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: 336.21  E-value: 6.25e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  19 DINLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNADILFGASEQSALAIIRDHKDSFSEKDIQPLYLR 98
Cdd:cd13519   1 EINLYGPGGPAPAMKEAAKKFEKKTGVKVNVTAGPQPTWEDKAKQDADIIYGGSEQMMTDFISALPKLFDSSDIKPLYLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  99 KSILLVKKGNPKNIRSIDDLTRPGIGVIVNDGggtsnTSGTGVWEDIAGRKGNIETVAAIRKNIILYAPNSGTARKALEN 178
Cdd:cd13519  81 PSAILVRKGNPKKIKGLKDLLKPGVKILVVNG-----AGQTGLWEDMAGRTGDIETVRAFRKNIVVFAKNSGAARKAWKQ 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831026 179 QPGADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQDA--NDETRRFAEWLQTDEAAPAFKKYGW 247
Cdd:cd13519 156 DPNIDAWITWNIWQKANPDIADFVELEKDYVIYRDMNVALTKKGlqNPEAQEFIDYLSSKEAQAIFKKWGW 226
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 21-248 6.11e-34

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 121.99  E-value: 6.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    21 NLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNA--DILFGASEqSALAIIRDhKDSFSEKDIQPLYLR 98
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKQIANGApaDVFISADS-AWLDKLAA-AGLVVPGSRVPLAYS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    99 KSILLVKKGNPKNIRSIDDLTRPGIGVIVndggGTSNTSGTGV-WEDIAGRKGNIEtvaAIRKNIILYAPNSGTARKALE 177
Cdd:pfam13531  79 PLVIAVPKGNPKDISGLADLLKPGVRLAV----ADPKTAPSGRaALELLEKAGLLK---ALEKKVVVLGENVRQALTAVA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831026   178 nQPGADVWITWADWA--ASNPEIGDVVEIAPDYVIWRD--MNITVRQDANDETRRFAEWLQTDEAAPAFKKYGWT 248
Cdd:pfam13531 152 -SGEADAGIVYLSEAlfPENGPGLEVVPLPEDLNLPLDypAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 94-133 8.61e-05

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 43.28  E-value: 8.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15831026   94 PLYLRKSILLVKKGNPKNIRSIDDLTRPGIgVIVN--DGGGT 133
Cdd:PRK14498 495 KGYRREQGLVVRKGNPKGIEGIEDLVRKDV-RFVNrqRGSGT 535
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
 96-245 1.61e-04

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: 42.26  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    96 YLRKSILLVKKGNPKNIRSIDDLTRPGIGVIVNDgggtSNTSGTGVWEDIA----------GRKGNIET-VAAIRKNIIL 164
Cdd:TIGR00971 101 YTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPN----PKSSGGARWNYLAawgyalhhnnGDQAKAQQfVTALLKNVEV 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026   165 YAPNSGTARKALENQPGADVWITWADWA--ASNPEIGDVVEI--------APDYVIWRDMNITvRQDANDETRRFAEWLQ 234
Cdd:TIGR00971 177 LDSGARGATNTFVERGIGDVLIAWENEAllARKELGKDKFEIvtpsesilAEPTVSVVDKVVE-KKGTKKVAEAYLKYLY 255

                         170
                  ....*....|.
gi 15831026   235 TDEAAPAFKKY 245
Cdd:TIGR00971 256 SPEGQEIAAKN 266
 
Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 15-249 1.79e-127

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


Pssm-ID: 443645  Cd Length: 232  Bit Score: 360.45  E-value: 1.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  15 AAYADINLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNADILFGASEQSALAIIRDHKDSFSEKDIQP 94
Cdd:COG4588   1 AAAAVINVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGAFDSKDVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  95 LYLRKSILLVKKGNPKNIRSIDDLTRPGIGVIVNDGGGTsntsgTGVWEDIAGRKGNIETVAAIRKNIILYAPNSGTARK 174
Cdd:COG4588  81 LYLRPAAILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQ-----TGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831026 175 ALENQPGADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQD--ANDETRRFAEWLQTDEAAPAFKKYGWTR 249
Cdd:COG4588 156 AWTQDPDIDAWITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKgkADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 19-247 6.25e-118

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: 336.21  E-value: 6.25e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  19 DINLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNADILFGASEQSALAIIRDHKDSFSEKDIQPLYLR 98
Cdd:cd13519   1 EINLYGPGGPAPAMKEAAKKFEKKTGVKVNVTAGPQPTWEDKAKQDADIIYGGSEQMMTDFISALPKLFDSSDIKPLYLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  99 KSILLVKKGNPKNIRSIDDLTRPGIGVIVNDGggtsnTSGTGVWEDIAGRKGNIETVAAIRKNIILYAPNSGTARKALEN 178
Cdd:cd13519  81 PSAILVRKGNPKKIKGLKDLLKPGVKILVVNG-----AGQTGLWEDMAGRTGDIETVRAFRKNIVVFAKNSGAARKAWKQ 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831026 179 QPGADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQDA--NDETRRFAEWLQTDEAAPAFKKYGW 247
Cdd:cd13519 156 DPNIDAWITWNIWQKANPDIADFVELEKDYVIYRDMNVALTKKGlqNPEAQEFIDYLSSKEAQAIFKKWGW 226
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 21-248 6.11e-34

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 121.99  E-value: 6.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    21 NLYGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQNKWNEDAKKNA--DILFGASEqSALAIIRDhKDSFSEKDIQPLYLR 98
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKQIANGApaDVFISADS-AWLDKLAA-AGLVVPGSRVPLAYS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    99 KSILLVKKGNPKNIRSIDDLTRPGIGVIVndggGTSNTSGTGV-WEDIAGRKGNIEtvaAIRKNIILYAPNSGTARKALE 177
Cdd:pfam13531  79 PLVIAVPKGNPKDISGLADLLKPGVRLAV----ADPKTAPSGRaALELLEKAGLLK---ALEKKVVVLGENVRQALTAVA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831026   178 nQPGADVWITWADWA--ASNPEIGDVVEIAPDYVIWRD--MNITVRQDANDETRRFAEWLQTDEAAPAFKKYGWT 248
Cdd:pfam13531 152 -SGEADAGIVYLSEAlfPENGPGLEVVPLPEDLNLPLDypAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
 22-246 5.97e-18

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: 79.57  E-value: 5.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  22 LYGPGGPHTALLDAAKLYAEKTGIIVNVHYG------PQNKwnedAKKNADILFGASEqSALAIIRDHKDSFSEKDIQpl 95
Cdd:cd13517   4 VYAGAGLKKPMEEIAKLFEKKTGIKVEVTYGgsgqllSQIE----TSKKGDVFIPGSE-DYMEKAKEKGLVETVKIVA-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  96 YLRKSILlVKKGNPKNIRSIDDLTRPGIGVIVNDGGGTSNTSGT-------GVWEDiagrkgnietvaaIRKNIILYAPN 168
Cdd:cd13517  77 YHVPVIA-VPKGNPKNITSLEDLAKPGVKVALGDPKAAAIGKYAkkileknGLWEK-------------VKKNVVVYTAT 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026 169 -SGTARKALENQpgADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQDAN--DETRRFAEWLQTDEAAPAFKKY 245
Cdd:cd13517 143 vNQLLTYVLLGQ--VDAAIVWEDFAYWNPGKVEVIPIPKEQNRIKTIPIAVLKSSKnkELAKKFVDFVTSDEGKEIFKKY 220


                .
gi 15831026 246 G 246
Cdd:cd13517 221 G 221
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 101-246 2.46e-13

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: 68.11  E-value: 2.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026 101 ILLVKKGNPKNIRSIDDLTRPGIGVIvndgggTSN--TSGTGVWEDIAG-----RKGNIET-----VAAIRKNIILYaPN 168
Cdd:cd01005  98 VFLVRKGNPKGIRDWDDLVKPGVSVI------TPNpkTSGGARWNYLAAwgyalKKGGSEAkakefVTSLYKNVPVL-DS 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026 169 SG-TARKALENQPGADVWITWADWA--ASNPEIGDVVEIA-PDYVIWRDMNITVrQDANDE---TRR----FAEWLQTDE 237
Cdd:cd01005 171 GArEATTTFVKRGIGDVLITWENEAilANKELGGDKFEIVyPSVSILAEPPVAV-VDKNVDkhgTREvaeaYLEFLYSPE 249


                ....*....
gi 15831026 238 AAPAFKKYG 246
Cdd:cd01005 250 AQEIAAKNG 258
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 4-246 3.21e-12

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 64.51  E-value: 3.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026   4 IMAGFLIFLSSAAYAD-INLYGPGGPHTALLDAAKLY-AEKTGIIVNVHYGP----QNKWNEDAKknADILFGASE-QSA 76
Cdd:COG0725  10 LLALLLAGASAAAAAAeLTVFAAASLKEALEELAAAFeKEHPGVKVELSFGGsgalARQIEQGAP--ADVFISADEkYMD 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  77 LAIIRDHKDSFSEKDiqplYLRKSI-LLVKKGNPKNIRSIDDLTRPGIGVIVndggGTSNT--SG---------TGVWED 144
Cdd:COG0725  88 KLAKKGLILAGSRVV----FATNRLvLAVPKGNPADISSLEDLAKPGVRIAI----GDPKTvpYGkyakealekAGLWDA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026 145 IAGRkgnietvaairkniILYAPNSGTARKALENqpG-ADVWITWADWAASNPEIGDVVEIAPDYVIWRDMNITVRQDA- 222
Cdd:COG0725 160 LKPK--------------LVLGENVRQVLAYVES--GeADAGIVYLSDALAAKGVLVVVELPAELYAPIVYPAAVLKGAk 223

                       250       260
                ....*....|....*....|....*
gi 15831026 223 -NDETRRFAEWLQTDEAAPAFKKYG 246
Cdd:COG0725 224 nPEAAKAFLDFLLSPEAQAILEKYG 248
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 23-207 1.11e-08

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: 53.73  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  23 YGPGGPHTALLDAAKLYAEKTGIIVNVHYGPQ-NKWNE-DAKKNADILFGASEQSALAIirdhKDSFSEKDI---QPLYL 97
Cdd:cd00648   7 IGPPPYAGFAEDAAKQLAKETGIKVELVPGSSiGTLIEaLAAGDADVAVGPIAPALEAA----ADKLAPGGLyivPELYV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026  98 RKSILLVKKGNPKNIRsIDDLTRPGIGVIVNDGGGTSNTSGTGVWEDIAGRKGNIETVAairkniilYAPNSGTARKALE 177
Cdd:cd00648  83 GGYVLVVRKGSSIKGL-LAVADLDGKRVGVGDPGSTAVRQARLALGAYGLKKKDPEVVP--------VPGTSGALAAVAN 153

                       170       180       190
                ....*....|....*....|....*....|
gi 15831026 178 NQpgADVWITWADWAASNPEIGDVVEIAPD 207
Cdd:cd00648 154 GA--VDAAIVWVPAAERAQLGNVQLEVLPD 181
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 102-142 7.49e-08

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


Pssm-ID: 441221  Cd Length: 340  Bit Score: 52.05  E-value: 7.49e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15831026 102 LLVKKGNPKNIRSIDDLTRPGIGVIvndgggTSN--TSGTGVW 142
Cdd:COG1613 129 FLVRKGNPKGIKDWDDLVKPGVSVI------TPNpkTSGGARW 165
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
95-133 4.72e-06

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


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 46.92  E-value: 4.72e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 15831026  95 LYLRKSILLVKKGNPKNIRSIDDLTRPGIgVIVN--DGGGT 133
Cdd:COG1910 176 LARREQGLIVAKGNPKGIKGLEDLARPDL-RFVNrqKGSGT 215
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 94-139 4.05e-05

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: 43.33  E-value: 4.05e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15831026    94 PLYLRKSILLVKKGNPKNIRSIDDLTRPGIgVIVNDGGGtsntSGT 139
Cdd:pfam12727  65 NLAYREQGLVVAPGNPKGITGWEDLARPGL-RFVNRQRG----SGT 105
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 94-133 8.61e-05

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 43.28  E-value: 8.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15831026   94 PLYLRKSILLVKKGNPKNIRSIDDLTRPGIgVIVN--DGGGT 133
Cdd:PRK14498 495 KGYRREQGLVVRKGNPKGIEGIEDLVRKDV-RFVNrqRGSGT 535
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
 96-245 1.61e-04

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: 42.26  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026    96 YLRKSILLVKKGNPKNIRSIDDLTRPGIGVIVNDgggtSNTSGTGVWEDIA----------GRKGNIET-VAAIRKNIIL 164
Cdd:TIGR00971 101 YTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPN----PKSSGGARWNYLAawgyalhhnnGDQAKAQQfVTALLKNVEV 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831026   165 YAPNSGTARKALENQPGADVWITWADWA--ASNPEIGDVVEI--------APDYVIWRDMNITvRQDANDETRRFAEWLQ 234
Cdd:TIGR00971 177 LDSGARGATNTFVERGIGDVLIAWENEAllARKELGKDKFEIvtpsesilAEPTVSVVDKVVE-KKGTKKVAEAYLKYLY 255

                         170
                  ....*....|.
gi 15831026   235 TDEAAPAFKKY 245
Cdd:TIGR00971 256 SPEGQEIAAKN 266
PRK10852 PRK10852
thiosulfate ABC transporter substrate-binding protein CysP;
103-140 7.54e-04

thiosulfate ABC transporter substrate-binding protein CysP;


Pssm-ID: 236775  Cd Length: 338  Bit Score: 40.12  E-value: 7.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15831026  103 LVKKGNPKNIRSIDDLTRPGIGVIVNDgggtSNTSGTG 140
Cdd:PRK10852 125 LVRKGNPKNIHDWNDLVRSDVKLIFPN----PKTSGNA 158
 
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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