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Conserved domains on  [gi|1826989924|gb|QIS40901|]
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extracellular solute-binding protein [Clavibacter capsici]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 65-334 1.19e-37

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.18  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIG-GDFKQKLVTTFTGRSGlPSITGVKGEDMPYFlSEDGLFEDLDQLGAKE--VADQYPEwKLKEATTKDG 141
Cdd:COG1653    60 PGIKVEVESVPyDDYRTKLLTALAAGNA-PDVVQVDSGWLAEF-AAAGALVPLDDLLDDDglDKDDFLP-GALDAGTYDG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 142 QLIGLPIDIGPTALYYRADVFQKAGLPsepadvaaATATWDDYFAFGKRLKAATGGAIFV---DASDVFTKSIGQGTTRF 218
Cdd:COG1653   137 KLYGVPFNTDTLGLYYNKDLFEKAGLD--------PPKTWDELLAAAKKLKAKDGVYGFAlggKDGAAWLDLLLSAGGDL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 219 VDEDGDYTGDSPEVKAAWDRAVLAYQEGLTAN--VTDGSPDWASAISNGSLPALLGASWYQADLKSATADTsgDWRVAPM 296
Cdd:COG1653   209 YDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPL 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1826989924 297 PGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQV 334
Cdd:COG1653   287 PGGPGGkkpasvLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQA 330
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 65-334 1.19e-37

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.18  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIG-GDFKQKLVTTFTGRSGlPSITGVKGEDMPYFlSEDGLFEDLDQLGAKE--VADQYPEwKLKEATTKDG 141
Cdd:COG1653    60 PGIKVEVESVPyDDYRTKLLTALAAGNA-PDVVQVDSGWLAEF-AAAGALVPLDDLLDDDglDKDDFLP-GALDAGTYDG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 142 QLIGLPIDIGPTALYYRADVFQKAGLPsepadvaaATATWDDYFAFGKRLKAATGGAIFV---DASDVFTKSIGQGTTRF 218
Cdd:COG1653   137 KLYGVPFNTDTLGLYYNKDLFEKAGLD--------PPKTWDELLAAAKKLKAKDGVYGFAlggKDGAAWLDLLLSAGGDL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 219 VDEDGDYTGDSPEVKAAWDRAVLAYQEGLTAN--VTDGSPDWASAISNGSLPALLGASWYQADLKSATADTsgDWRVAPM 296
Cdd:COG1653   209 YDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPL 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1826989924 297 PGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQV 334
Cdd:COG1653   287 PGGPGGkkpasvLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQA 330
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 43-418 3.49e-37

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 139.46  E-value: 3.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  43 LDLWIWPDGLSQTVLDQVPDA----VPGTTLNVSTIG-GDFKQKLVTTFTGRSgLPSITGVKGEDMPYFlSEDGLFEDLD 117
Cdd:cd13585     2 LTFWDWGQPAETAALKKLIDAfekeNPGVKVEVVPVPyDDYWTKLTTAAAAGT-APDVFYVDGPWVPEF-ASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 118 QLGAKEVADQYPEWKLKEATTKDGQLIGLPIDIGPTALYYRADVFQKAGLPSEPAdvaaatATWDDYFAFGKRLKAATGG 197
Cdd:cd13585    80 DYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPP------WTWDELLEAAKKLTDKKGG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 198 ------AIFVDASDVFTKSIGQGTTRFVDED-GDYTGDSPEVKAAWDRAVLAYQEGLT-ANVTDGSPDWASAISNGSLPA 269
Cdd:cd13585   154 qygfalRGGSGGQTQWYPFLWSNGGDLLDEDdGKATLNSPEAVEALQFYVDLYKDGVApSSATTGGDEAVDLFASGKVAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 270 LLGASWYQADLKSATADtsGDWRVAPMPGGPA-----NIGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFP 344
Cdd:cd13585   234 MIDGPWALGTLKDSKVK--FKWGVAPLPAGPGgkrasVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAA 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1826989924 345 SATAAYDAPKLQEGDPFFggqstVGIFADAAAKMPTAYTSPYDNQVQAAFVTELQNVTS--LGKDPDQAWTDAVAA 418
Cdd:cd13585   312 LAAAAASAAAPDAKPALA-----LAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLgaLGKSPEEALKEAAKE 382
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 66-357 6.99e-19

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 86.31  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  66 GTTLNVSTIG-GDFKQKLVTTFTGRSGLPSITGVKGEDMPYFLSEDGLFEDLDQlgakeVADQYPEWKLKEATTKDGQLI 144
Cdd:pfam13416  11 GVTVEVEPQAsNDLQAKLLAAAAAGNAPDLDVVWIAADQLATLAEAGLLADLSD-----VDNLDDLPDALDAAGYDGKLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 145 GLPIDIG-PTALYYRADVFQKAGLPSepadvaaatATWDDYFAFGKRLKAATGGAIFVDASDVFTKSIGQGTTrfvDEDG 223
Cdd:pfam13416  86 GVPYAAStPTVLYYNKDLLKKAGEDP---------KTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDL---TDDG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 224 DYTGDSPEVKAAWDRAVLAYQegltanVTDGSPDWASAISNGSLPALLGASWYQADLKSAtadtSGDWRVAPMPGGPAnI 303
Cdd:pfam13416 154 KGVEALDEALAYLKKLKDNGK------VYNTGADAVQLFANGEVAMTVNGTWAAAAAKKA----GKKLGAVVPKDGSF-L 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826989924 304 GGSFLSIPAGTKDPE-AAFAVIKDVLSEDNQVTAYADKGIFPSATAAYDAPKLQE 357
Cdd:pfam13416 223 GGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKA 277
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
139-428 5.01e-04

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 42.09  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 139 KDGQLIGLPIDIGPTALYYRADVFQKAGL-PSEPADvaaataTWDDYFAFGKRLKA-------ATG-------------- 196
Cdd:PRK10974  133 KTGHLLSQPFNSSTPVLYYNKDAFKKAGLdPEQPPK------TWQDLAAYAAKLRAagmkcgyASGwqgwiqlenfsawh 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 197 GAIFV---------DASDVFTKSIGQGTTRFVDE---DGDYTGDSPEvkaawDRAVLAYQEGLTANVTDGSPDWASAISN 264
Cdd:PRK10974  207 GLPFAsknngfdgtDAVLEFNKPEQVKHIALLEEmnkKGDFTYVGRK-----DESTEKFYNGDCAITTASSGSLANIRKY 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 265 GSLPALLGASWYQADLKSATADtsgdwrvapmpggpANIGGSFLSIPAGtKDPEAAFAVIK--DVLSE-DNQVTAYADKG 341
Cdd:PRK10974  282 AKFNYGVGMMPYDADVKGAPQN--------------AIIGGASLWVMQG-KDKETYKGVAKflDFLAKpENAAEWHQKTG 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 342 IFPSATAAYDAPKlQEGdpFFGGQSTvgifADAAA-----KMPTAYTS----PYDNQVQAAFVTELQNVTSLGKDPDQAW 412
Cdd:PRK10974  347 YLPITTAAYDLTR-EQG--FYEKNPG----ADTATrqmlnKPPLPFTKglrlGNMPQIRTIVDEELESVWTGKKTPQQAL 419

                         330
                  ....*....|....*.
gi 1826989924 413 TDAVAAGEAALRTAKQ 428
Cdd:PRK10974  420 DSAVERGNQLLRRFEK 435
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 65-334 1.19e-37

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.18  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIG-GDFKQKLVTTFTGRSGlPSITGVKGEDMPYFlSEDGLFEDLDQLGAKE--VADQYPEwKLKEATTKDG 141
Cdd:COG1653    60 PGIKVEVESVPyDDYRTKLLTALAAGNA-PDVVQVDSGWLAEF-AAAGALVPLDDLLDDDglDKDDFLP-GALDAGTYDG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 142 QLIGLPIDIGPTALYYRADVFQKAGLPsepadvaaATATWDDYFAFGKRLKAATGGAIFV---DASDVFTKSIGQGTTRF 218
Cdd:COG1653   137 KLYGVPFNTDTLGLYYNKDLFEKAGLD--------PPKTWDELLAAAKKLKAKDGVYGFAlggKDGAAWLDLLLSAGGDL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 219 VDEDGDYTGDSPEVKAAWDRAVLAYQEGLTAN--VTDGSPDWASAISNGSLPALLGASWYQADLKSATADTsgDWRVAPM 296
Cdd:COG1653   209 YDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPL 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1826989924 297 PGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQV 334
Cdd:COG1653   287 PGGPGGkkpasvLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQA 330
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 43-418 3.49e-37

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 139.46  E-value: 3.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  43 LDLWIWPDGLSQTVLDQVPDA----VPGTTLNVSTIG-GDFKQKLVTTFTGRSgLPSITGVKGEDMPYFlSEDGLFEDLD 117
Cdd:cd13585     2 LTFWDWGQPAETAALKKLIDAfekeNPGVKVEVVPVPyDDYWTKLTTAAAAGT-APDVFYVDGPWVPEF-ASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 118 QLGAKEVADQYPEWKLKEATTKDGQLIGLPIDIGPTALYYRADVFQKAGLPSEPAdvaaatATWDDYFAFGKRLKAATGG 197
Cdd:cd13585    80 DYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPP------WTWDELLEAAKKLTDKKGG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 198 ------AIFVDASDVFTKSIGQGTTRFVDED-GDYTGDSPEVKAAWDRAVLAYQEGLT-ANVTDGSPDWASAISNGSLPA 269
Cdd:cd13585   154 qygfalRGGSGGQTQWYPFLWSNGGDLLDEDdGKATLNSPEAVEALQFYVDLYKDGVApSSATTGGDEAVDLFASGKVAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 270 LLGASWYQADLKSATADtsGDWRVAPMPGGPA-----NIGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFP 344
Cdd:cd13585   234 MIDGPWALGTLKDSKVK--FKWGVAPLPAGPGgkrasVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAA 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1826989924 345 SATAAYDAPKLQEGDPFFggqstVGIFADAAAKMPTAYTSPYDNQVQAAFVTELQNVTS--LGKDPDQAWTDAVAA 418
Cdd:cd13585   312 LAAAAASAAAPDAKPALA-----LAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLgaLGKSPEEALKEAAKE 382
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 43-423 3.08e-36

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. 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.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 136.67  E-value: 3.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  43 LDLWIWPDGLSQTVLDQVPD----AVPGTTLNVSTIG-GDFKQKLVTTFTGRSGlPSITGVKGEDMPYFLSEDGLfEDL- 116
Cdd:cd14747     2 LTVWAMGNSAEAELLKELADefekENPGIEVKVQVLPwGDAHTKITTAAASGDG-PDVVQLGNTWVAEFAAMGAL-EDLt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 117 DQLGAKEVADQYPEWkLKEATTKDGQLIGLPIDIGPTALYYRADVFQKAGLPSEPAdvaaataTWDDYFAFGKRLKAATG 196
Cdd:cd14747    80 PYLEDLGGDKDLFPG-LVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPK-------TWDELEAAAKKIKADGP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 197 G--AIFVDASDVFTKSI-----GQGTTRFVDEDGDYTGDSPEVKAAWDRAVLAYQEGLT-ANVTDGSPDWASAISNGSLP 268
Cdd:cd14747   152 DvsGFAIPGKNDVWHNAlpfvwGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSpKSTLENSADVEQAFANGKVA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 269 ALLGASWYQADLKSATADTSGDWRVAPMPGGPA-----NIGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIF 343
Cdd:cd14747   232 MIISGPWEIGAIREAGPDLAGKWGVAPLPGGPGggspsFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGML 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 344 PSATAAYDAPKLQEgDPFFGGqstvgiFADAaakMPTAYTSPYD---NQVQAAFVTELQNVTSL-GKDPDQAWTDAVAAG 419
Cdd:cd14747   312 PANTSAWDDPSLAN-DPLLAV------FAEQ---LKTGKATPATpewGEIEAELVLVLEEVWIGvGADVEDALDKAAAEI 381


                  ....
gi 1826989924 420 EAAL 423
Cdd:cd14747   382 NEIL 385
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 65-418 1.13e-30

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. 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.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 121.63  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIGG--DFKQKLVTTFTGRSGlPSITGVKGEDMPYFlSEDGLFEDLDQLGAKEV--ADQYPEwKLKEATTKD 140
Cdd:cd14748    28 PDIKVKAVYQGSydDTLTKLLAALAAGTA-PDVAQVDASWVAQL-ADSGALEPLDDYIDKDGvdDDDFYP-AALDAGTYD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 141 GQLIGLPIDIGPTALYYRADVFQKAGLpsepaDVAAATATWDDYFAFGKRLKAATGG------AIFVDASDVFTKSIGQG 214
Cdd:cd14748   105 GKLYGLPFDTSTPVLYYNKDLFEEAGL-----DPEKPPKTWDELEEAAKKLKDKGGKtgrygfALPPGDGGWTFQALLWQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 215 T-TRFVDEDGDYTG-DSPEVKAAWDRAV-LAYQEGLTANVTDGSPDWasAISNGSLPALLGASWYQADLKSATADTsgDW 291
Cdd:cd14748   180 NgGDLLDEDGGKVTfNSPEGVEALEFLVdLVGKDGVSPLNDWGDAQD--AFISGKVAMTINGTWSLAGIRDKGAGF--EY 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 292 RVAPMPGGP-----ANIGGSFLSIPAG-TKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSATAAYDAPKlqegdPFFGGQ 365
Cdd:cd14748   256 GVAPLPAGKgkkgaTPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPE-----EFLAEN 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1826989924 366 STVGIFADAAAKM-PTAYTSPYDNQVQAAFVTELQNVTSLGKDPDQAWTDAVAA 418
Cdd:cd14748   331 PNYKVAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
107-423 3.54e-27

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 111.97  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 107 LSEDGLFEDLDQlgAKEVADQYPEwKLKEATTKDGQLIGLPIDIGPTALYYRADVFqkaglPSEPAdvaaatATWDDYFA 186
Cdd:COG2182   105 LAEAGLLAPLDD--DLADKDDFLP-AALDAVTYDGKLYGVPYAVETLALYYNKDLV-----KAEPP------KTWDELIA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 187 FGKRLKAATGGAIFVDASD------VFTKSIGQGTTRFVDEDGDYTGDSPEVKAAwdravLAYQEGLTAN-VTDGSPDWA 259
Cdd:COG2182   171 AAKKLTAAGKYGLAYDAGDayyfypFLAAFGGYLFGKDGDDPKDVGLNSPGAVAA-----LEYLKDLIKDgVLPADADYD 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 260 SAIS---NGSLPALLGASWYQADLKSATADtsgDWRVAPMPGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLSE 330
Cdd:COG2182   246 AADAlfaEGKAAMIINGPWAAADLKKALGI---DYGVAPLPTLAGGkpakpfVGVKGFGVSAYSKNKEAAQEFAEYLTSP 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 331 DNQVTAYADKGIFPSATAAYDAPKLQEgDPFFGGQSTVgifADAAAKMPtayTSPYDNQVQAAFVTELQNVTSLGKDPDQ 410
Cdd:COG2182   323 EAQKALFEATGRIPANKAAAEDAEVKA-DPLIAAFAEQ---AEYAVPMP---NIPEMGAVWTPLGTALQAIASGKADPAE 395

                         330
                  ....*....|...
gi 1826989924 411 AWTDAVAAGEAAL 423
Cdd:COG2182   396 ALDAAQKQIEAAI 408
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 76-418 7.72e-22

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. 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.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 96.59  E-value: 7.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  76 GDFKQKLVTTFTGRSGLPSITGVKGEDMPYFlSEDGLFEDLDQLGAKEVADQYPEWKLkEATTKDGQLIGLPIDIGPTAL 155
Cdd:cd14750    42 DDQRQQLVTALAAGSSAPDVLGLDVIWIPEF-AEAGWLLPLTEYLKEEEDDDFLPATV-EANTYDGKLYALPWFTDAGLL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 156 YYRADVFQKAGlpsepadvAAATATWDDYFAFGKRLKA------------ATGGAIFVDASDVFTksiGQGTTRFVDEDG 223
Cdd:cd14750   120 YYRKDLLEKYG--------PEPPKTWDELLEAAKKRKAgepgiwgyvfqgKQYEGLVCNFLELLW---SNGGDIFDDDSG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 224 DYTGDSPEVKAAWDRAVLAYQEGLTANVTDGspdWASAISNGSLP---ALLGASW-YQADLKSATADT-SGDWRVAPMPG 298
Cdd:cd14750   189 KVTVDSPEALEALQFLRDLIGEGISPKGVLT---YGEEEARAAFQagkAAFMRNWpYAYALLQGPESAvAGKVGVAPLPA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 299 GPAN-----IGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSATAAYDAPKLQEGDPFFggQSTVGIFAD 373
Cdd:cd14750   266 GPGGgsastLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPPTRRALYDDPEVLEAYPFL--PALLEALEN 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1826989924 374 AAAKMPTaytsPYDNQVQAAFVTELQNVTSLGKDPDQAWTDAVAA 418
Cdd:cd14750   344 AVPRPVT----PKYPEVSTAIQIALSAALSGQATPEEALKQAQEK 384
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 66-357 6.99e-19

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 86.31  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  66 GTTLNVSTIG-GDFKQKLVTTFTGRSGLPSITGVKGEDMPYFLSEDGLFEDLDQlgakeVADQYPEWKLKEATTKDGQLI 144
Cdd:pfam13416  11 GVTVEVEPQAsNDLQAKLLAAAAAGNAPDLDVVWIAADQLATLAEAGLLADLSD-----VDNLDDLPDALDAAGYDGKLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 145 GLPIDIG-PTALYYRADVFQKAGLPSepadvaaatATWDDYFAFGKRLKAATGGAIFVDASDVFTKSIGQGTTrfvDEDG 223
Cdd:pfam13416  86 GVPYAAStPTVLYYNKDLLKKAGEDP---------KTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDL---TDDG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 224 DYTGDSPEVKAAWDRAVLAYQegltanVTDGSPDWASAISNGSLPALLGASWYQADLKSAtadtSGDWRVAPMPGGPAnI 303
Cdd:pfam13416 154 KGVEALDEALAYLKKLKDNGK------VYNTGADAVQLFANGEVAMTVNGTWAAAAAKKA----GKKLGAVVPKDGSF-L 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826989924 304 GGSFLSIPAGTKDPE-AAFAVIKDVLSEDNQVTAYADKGIFPSATAAYDAPKLQE 357
Cdd:pfam13416 223 GGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKA 277
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 65-411 3.56e-18

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. 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.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 85.51  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIGGD-FKQKLVTTFTGRSGlPSITGVKGEDMPYFLSEDGLFEDLDqlgakEVADQYPEWK-----LKEATT 138
Cdd:cd14749    29 PNIKVKVVVFPYDnYKTKLKTAVAAGEG-PDVFNLWPGGWLAEFVKAGLLLPLT-----DYLDPNGVDKrflpgLADAVT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 139 KDGQLIGLPIDIGPTALYYRADVFQKAGlPSEPAdvaaatATWDDYFAFGKRLKAATGGA--IFVDASDVFTKSIGQGTT 216
Cdd:cd14749   103 FNGKVYGIPFAARALALFYNKDLFEEAG-GVKPP------KTWDELIEAAKKDKFKAKGQtgFGLLLGAQGGHWYFQYLV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 217 RFvdEDGDYTGDSPEVKAAW-DRAVLAYQEGLTANVTDGS--PDWASAISNGSLPA--------LLGASWYQADLKSATA 285
Cdd:cd14749   176 RQ--AGGGPLSDDGSGKATFnDPAFVQALQKLQDLVKAGAfqEGFEGIDYDDAGQAfaqgkaamNIGGSWDLGAIKAGEP 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 286 DtsGDWRVAPMPGGPAN-----IGGSF--LSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPsatAAYDAPKLQEG 358
Cdd:cd14749   254 G--GKIGVFPFPTVGKGaqtstIGGSDwaIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLP---AKEVVAKDEDP 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826989924 359 DPFfggqSTVGIFADAA-AKMPTAYTSPYDNQvQAAFVTEL-QNVTSLGKDPDQA 411
Cdd:cd14749   329 DPV----AILGPFADVLnAAGSTPFLDEYWPA-AAQVHKDAvQKLLTGKIDPEQV 378
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 95-418 1.73e-16

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. 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.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 80.50  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  95 ITGVKGEDMPYFLSED----------GLFEDLDQL-GAKEVADQYPEwklKEATTK-DGQLIGLPIDIGPTALYYRADVF 162
Cdd:cd14751    47 KTAAAGGQAPDVMRADiawvpefaklGYLQPLDGTpAFDDIVDYLPG---PMETNRyNGHYYGVPQVTNTLALFYNKRLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 163 QKAGLPsepadvaaATATWDDYFAFGKRLKAATGGAIFVDASDV------FTKSIGQGttrFVDEDG-DYTGDSPEVKAA 235
Cdd:cd14751   124 EEAGTE--------VPKTMDELVAAAKAIKKKKGRYGLYISGDGpywllpFLWSFGGD---LTDEKKaTGYLNSPESVRA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 236 WDRAVLAYQEGLTAN-VTDGSPDWASAISNGSLPALLGASWYQADLKSATADTSGD-WRVAPMPGGPAN----IGGSFLS 309
Cdd:cd14751   193 LETIVDLYDEGAITPcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEFKDPDnLGIAPVPAGPGGsgspVGGEDLV 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 310 IPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSATAAYDAPKLQeGDPFfggqstVGIFADAAAKMPTAYTSPYDNQ 389
Cdd:cd14751   273 IFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVA-NNPM------VAAFKPALETAVPRPPIPEWGE 345

                         330       340
                  ....*....|....*....|....*....
gi 1826989924 390 VQAAFVTELQNVTSLGKDPDQAwTDAVAA 418
Cdd:cd14751   346 LFEPLTLAFAKVLRGEKSPREA-LDEAAK 373
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 45-418 1.67e-13

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 71.29  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  45 LWIWPDGLS----QTVLDQVPDAVPGTTLNVSTIGGD-FKQKLVTTFTGRSGLPSITGVKGEDMPYFLSedGLFEDLDQL 119
Cdd:cd13522     4 VWHQYDTGEnqavNELIAKFEKAYPGITVEVTYQDTEaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAA--GLLAPLDEY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 120 GAKEVADQYPEWKlkeATTKDGQLIGLPIDIGPTALYYRadvfqKAGLPSEPAdvaaatATWDDYFAFGKRLKAATGGAI 199
Cdd:cd13522    82 VSKSGKYAPNTIA---AMKLNGKLYGVPVSVGAHLMYYN-----KKLVPKNPP------KTWQELIALAQGLKAKNVWGL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 200 FVDASDVF---TKSIGQGTTRFVDEDGDY--TGDSPEVKAAWDRAV-LAYQEGLTANVTDGSPDwASAISNGSLPALLGA 273
Cdd:cd13522   148 VYNQNEPYffaAWIGGFGGQVFKANNGKNnpTLDTPGAVEALQFLVdLKSKYKIMPPETDYSIA-DALFKAGKAAMIING 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 274 SWYQADLKSATADTSGdwrVAPMPGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSAT 347
Cdd:cd13522   227 PWDLGDYRQALKINLG---VAPLPTFSGTkhaapfVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANL 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1826989924 348 AAYDAPKLQEGDPFFGgqstvgiFADAAAK---MPTAytsPYDNQVQAAFVTELQNVTSLGKDPDQAWTDAVAA 418
Cdd:cd13522   304 QAYESPAVQNKPAQKA-------SAEQAAYgvpMPNI---PEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 107-418 2.76e-13

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 70.79  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 107 LSEDGLFEDLDQLGAKEVADQYPEWKlkeATTKDGQLIGLPIDIGPTALYYRADvfqkagLPSEPAdvaaatATWDDYFA 186
Cdd:cd13586    67 LAAAGLLAPIPEYLAVKIKNLPVALA---AVTYNGKLYGVPVSVETIALFYNKD------LVPEPP------KTWEELIA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 187 FGKRLKAATGGAI-----FVDASDVFTKSIGQGTTRFVDEDGDYTG---DSPEVKAA--WDRAVLAYQEGLTANVTDGSP 256
Cdd:cd13586   132 LAKKFNDKAGGKYgfaydQTNPYFSYPFLAAFGGYVFGENGGDPTDiglNNEGAVKGlkFIKDLKKKYKVLPPDLDYDIA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 257 DwaSAISNGSLPALLGASWYQADLKsatadTSG-DWRVAPMPGGPAN------IGGSFLSIPAGTKDPEAAFAVIKDVLS 329
Cdd:cd13586   212 D--ALFKEGKAAMIINGPWDLADYK-----DAGiNFGVAPLPTLPGGkqaapfVGVQGAFVSAYSKNKEAAVEFAEYLTS 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 330 EDNQVTAYADKGIFPSATAAYDAPKLQEgDPFFGGqstvgiFADAAAK---MPtayTSPYDNQVQAAFVTELQNVTSLGK 406
Cdd:cd13586   285 DEAQLLLFEKTGRIPALKDALNDAAVKN-DPLVKA------FAEQAQYgvpMP---NIPEMAAVWDAMGNALNLVASGKA 354

                         330
                  ....*....|..
gi 1826989924 407 DPDQAWTDAVAA 418
Cdd:cd13586   355 TPEEAAKDAVAA 366
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 76-414 3.25e-12

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 68.12  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  76 GDFKQKLVTTFTgrSG-LPSITGVKGEDMPYFLSEDGLFEDLDQLGAKEVAD--QYPEWKLKEATTKDGQLIGLP---ID 149
Cdd:cd13580    44 SSYDEKLNLALA--SGdLPDIVVVNDPQLSITLVKQGALWDLTDYLDKYYPNlkKIIEQEGWDSASVDGKIYGIPrkrPL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 150 IGPTALYYRADVFQKAGLPsepadvaaATATWDDYF----AF--------GKRLK---AATGGAIFVDASDVFTKSIGQG 214
Cdd:cd13580   122 IGRNGLWIRKDWLDKLGLE--------VPKTLDELYevakAFtekdpdgnGKKDTyglTDTKDLIGSGFTGLFGAFGAPP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 215 TTRFVDEDGDYTGDS--PEVKAAWDRAVLAYQEGLTAN--VTDGSPDWASAISNGSLPALLGASWYQADLKSA--TADTS 288
Cdd:cd13580   194 NNWWKDEDGKLVPGSiqPEMKEALKFLKKLYKEGLIDPefAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASlkKNDPD 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 289 GDWRVAPMPGGPA--------NIGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQVTAY-----------ADKGIFPSATAA 349
Cdd:cd13580   274 AEWVAVPIPSGPDgkygvwaeSGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQKLLDygiegvhytvkDGGPVNIIPPDK 353

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1826989924 350 YDAPKLQEGDPFFGGQSTVGIFADAAAKMPTAYTSPYDNQVQAAFVTELQN------VTSLGKDPDQAWTD 414
Cdd:cd13580   354 QEVGDATLDYFQGSLALEKYKLTNNGERKSDAKKEALDERVVNANDEENENiavgppTETLVSPTEKYGAT 424
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 65-333 7.68e-11

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 62.82  E-value: 7.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924  65 PGTTLNVSTIG-GDFKQKLVTTFTGRSGLPSITGVKGEDMPYFLSEdGLFEDLDQLGAKEVADQYPewklkeattkdgQL 143
Cdd:pfam01547  22 PGIKVEVESVGsGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKA-GLLLPLDDYVANYLVLGVP------------KL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 144 IGLPIDIGPTALYYRADVFQKAGLPSEPadvaaataTWDDYFAFGKRLKAATGGAIFV-------DASDVFTKSIGQGTT 216
Cdd:pfam01547  89 YGVPLAAETLGLIYNKDLFKKAGLDPPK--------TWDELLEAAKKLKEKGKSPGGAgggdasgTLGYFTLALLASLGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 217 RFVDEDGDYTGDSPEVKAAW---DRAVLAYQEGLTANVTDGSPDWASA---ISNGSLPALLGASWY---------QADLK 281
Cdd:pfam01547 161 PLFDKDGGGLDNPEAVDAITyyvDLYAKVLLLKKLKNPGVAGADGREAlalFEQGKAAMGIVGPWAalaankvklKVAFA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1826989924 282 SATADTSGDWRVAPMPGGP-ANIGGSFLSIPAGTKDPEAAFAVIKDVLSEDNQ 333
Cdd:pfam01547 241 APAPDPKGDVGYAPLPAGKgGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 107-416 3.86e-10

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 60.96  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 107 LSEDGLFEDLDQlgAKEVADQYPEWKLKeATTKDGQLIGLPIDIGPTALYYRADVFQKAglPSEPADVAAAT-------- 178
Cdd:cd13658    67 AVLQGLLSPIKL--SKDKKKGFTDQALK-ALTYDGKLYGLPAAVETLALYYNKDLVKNA--PKTFDELEALAkdltkekg 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 179 ------ATWDD-YFAFGkrLKAATGGAIFV-DASDVFTKSIGqgttrfVDEDGDYTGdSPEVKAAWDRAVLAyqEGLTAN 250
Cdd:cd13658   142 kqygflADATNfYYSYG--LLAGNGGYIFKkNGSDLDINDIG------LNSPGAVKA-VKFLKKWYTEGYLP--KGMTGD 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 251 VTDGspdwasAISNGSLPALLGASWYQADLKSATAdtsgDWRVAPMPGGPAN------IGGSFLSIPAGTKDPEAAFAVI 324
Cdd:cd13658   211 VIQG------LFKEGKAAAVIDGPWAIQEYQEAGV----NYGVAPLPTLPNGkpmapfLGVKGWYLSAYSKHKEWAQKFM 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 325 KDVLSEDNQVTAYADKGIFPSATAAYDAPKLQEgDPFFggqSTVGIFADAAAKMPTAytsPYDNQVQAAFVTELQNVTSL 404
Cdd:cd13658   281 EFLTSKENLKKRYDETNEIPPRKDVRSDPEIKN-NPLT---SAFAKQASRAVPMPNI---PEMGAVWEPANNALFFILSG 353

                         330
                  ....*....|..
gi 1826989924 405 GKDPDQAWTDAV 416
Cdd:cd13658   354 KKTPKQALNDAV 365
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 109-418 4.31e-07

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 51.61  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 109 EDGLFEDLDQLGAKEVADQYPEWKLkEATTKDGQLIGLPIDIGPTALYYRADVfqkaglpsepadVAAATATWDDYFAFG 188
Cdd:cd13657    71 EAGLLVPISDYLSEDDFENYLPTAV-EAVTYKGKVYGLPEAYETVALIYNKAL------------VDQPPETTDELLAIM 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 189 KRLKAATGG--AIFVDASDV-FTKSIGQGT-TRFVDEDGDYTG-DSPEVKAAwdravLAYQEGLTANVTDGSPDWASAIS 263
Cdd:cd13657   138 KDHTDPAAGsyGLAYQVSDAyFVSAWIFGFgGYYFDDETDKPGlDTPETIKG-----IQFLKDFSWPYMPSDPSYNTQTS 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 264 ---NGSLPALLGASWYQADLKSATAdtsgDWRVAPMPGGPANIG--------GSFLSIPAGTKDPEAAFAVIKDVLSEDN 332
Cdd:cd13657   213 lfnEGKAAMIINGPWFIGGIKAAGI----DLGVAPLPTVDGTNPprpysgveGIYVTKYAERKNKEAALDFAKFFTTAEA 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 333 QVtAYADK-GIFPSATAAYDAPKLQeGDPffggqsTVGIFADAAAK---MPtayTSPYDNQVQAAFVTELQNVTSLGKDP 408
Cdd:cd13657   289 SK-ILADEnGYVPAATNAYDDAEVA-ADP------VIAAFKAQAEHgvpMP---NSPEMASVWGPVTLALAAVYQGGQDP 357

                         330
                  ....*....|
gi 1826989924 409 DQAWTDAVAA 418
Cdd:cd13657   358 QEALAAAQQE 367
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 125-351 9.14e-06

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 46.91  E-value: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 125 ADQYPEWKLKEATTKDGQLIGLPIDIGPTALYYRADVFQkaglpsePADVAAATATWDDYFAfGKRlkaatggAIFVDAS 204
Cdd:cd13588    80 ANIDPRLRNLPWLTVDGKVYGVPYDWGANGLAYNTKKVK-------TPPTSWLALLWDPKYK-GRV-------AARDDPI 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 205 DVFtksigQGTTRFVDEDGDYTGDSPEVKAAWDraVLAYQEGLTANVTDGSPDWASAISNGSlpALLGASW-YQAD-LKS 282
Cdd:cd13588   145 DAI-----ADAALYLGQDPPFNLTDEQLDAVKA--KLREQRPLVRKYWSDGAELVQLFANGE--VVAATAWsGQVNaLQK 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1826989924 283 ATADTSGdwrVAPMPGGPANIGGsfLSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSATAAYD 351
Cdd:cd13588   216 AGKPVAY---VIPKEGATGWVDT--WMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEACA 279
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 126-301 1.50e-05

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 46.97  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 126 DQYPEWK-LKEATTKDGQLI---GLPIDIGP-TALYYRADVFQKAGLPsEPadvaaatATWDDYFAFGKRLKAATG---- 196
Cdd:cd13583    96 EKWGLGKeLATGRQSDGKYYslpGLHEDPGVqYSFLYRKDIFEKAGIK-IP-------TTWDEFYAALKKLKEKYPdsyp 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 197 -------GAIFVDASDVF-TKSIGQGTTRFVDEDGD---YTGDSPEVKAAWDRAVLAYQEGLTA--NVTDGSPDW-ASAI 262
Cdd:cd13583   168 ysdrwnsNALLLIAAPAFgTTAGWGFSNYTYDPDTDkfvYGATTDEYKDMLQYFNKLYAEGLLDpeSFTQTDDQAkAKFL 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1826989924 263 SNGSLPALLGASWYQADLKSATADTSGDWRVAPM--PGGPA 301
Cdd:cd13583   248 NGKSFVITTNPQTVDELQRNLRAADGGNYEVVSItpPAGPA 288
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 212-349 4.02e-05

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. 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.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 45.41  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 212 GQGTTRFVDEDGDYTGDSpeVKAAWDRAVLAYQEGLTAN---VTDGSPDWASAISNGSLPALLGASWYQADLKSATADTS 288
Cdd:cd13655   159 GAGCKLFGNNGGDTAGCD--FNNEKGVAVTNYLVDLVANpkfVNDADGDAISGLKDGTLGAGVSGPWDAANLKKALGDNY 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1826989924 289 GdwrVAPMPggPANIGG------SF-----LSIPAGTKDPEAAFAVIKDVLSEDNQVTAYADKGIFPSATAA 349
Cdd:cd13655   237 A---VAKLP--TYTLGGkdvqmkSFagykaIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIGPTNKEA 303
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
139-428 5.01e-04

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 42.09  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 139 KDGQLIGLPIDIGPTALYYRADVFQKAGL-PSEPADvaaataTWDDYFAFGKRLKA-------ATG-------------- 196
Cdd:PRK10974  133 KTGHLLSQPFNSSTPVLYYNKDAFKKAGLdPEQPPK------TWQDLAAYAAKLRAagmkcgyASGwqgwiqlenfsawh 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 197 GAIFV---------DASDVFTKSIGQGTTRFVDE---DGDYTGDSPEvkaawDRAVLAYQEGLTANVTDGSPDWASAISN 264
Cdd:PRK10974  207 GLPFAsknngfdgtDAVLEFNKPEQVKHIALLEEmnkKGDFTYVGRK-----DESTEKFYNGDCAITTASSGSLANIRKY 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 265 GSLPALLGASWYQADLKSATADtsgdwrvapmpggpANIGGSFLSIPAGtKDPEAAFAVIK--DVLSE-DNQVTAYADKG 341
Cdd:PRK10974  282 AKFNYGVGMMPYDADVKGAPQN--------------AIIGGASLWVMQG-KDKETYKGVAKflDFLAKpENAAEWHQKTG 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 342 IFPSATAAYDAPKlQEGdpFFGGQSTvgifADAAA-----KMPTAYTS----PYDNQVQAAFVTELQNVTSLGKDPDQAW 412
Cdd:PRK10974  347 YLPITTAAYDLTR-EQG--FYEKNPG----ADTATrqmlnKPPLPFTKglrlGNMPQIRTIVDEELESVWTGKKTPQQAL 419

                         330
                  ....*....|....*.
gi 1826989924 413 TDAVAAGEAALRTAKQ 428
Cdd:PRK10974  420 DSAVERGNQLLRRFEK 435
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
107-351 7.96e-04

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 41.43  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 107 LSEDGLFEDLDqlgakevADQYPEWK-----LKEATTKDGQLIGLPIDIGPTALYYRADVFQKAglpsepadvaaaTATW 181
Cdd:COG0687    91 LIKAGLLQPLD-------KSKLPNLAnldprFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP------------PTSW 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 182 DDYF--AFGKRLkaatggAIFVDASDVFT---KSIGqgttrfvdedGDYTGDSP-EVKAAWDraVLAYQEGLTANVTDGS 255
Cdd:COG0687   152 ADLWdpEYKGKV------ALLDDPREVLGaalLYLG----------YDPNSTDPaDLDAAFE--LLIELKPNVRAFWSDG 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 256 PDWASAISNGSLPAllgASWYQADLKSATADtSGDWR-VAPMPGGPANIGGsfLSIPAGTKDPEAAFAVIKDVLSEDNQV 334
Cdd:COG0687   214 AEYIQLLASGEVDL---AVGWSGDALALRAE-GPPIAyVIPKEGALLWFDN--MAIPKGAPNPDLAYAFINFMLSPEVAA 287

                         250
                  ....*....|....*..
gi 1826989924 335 TAYADKGIFPSATAAYD 351
Cdd:COG0687   288 ALAEYVGYAPPNKAARE 304
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 107-354 2.07e-03

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 39.92  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 107 LSEDGLFEDLDQlgakEVADQYPEWklkeATTKDGQLIGlpIDIGPTALYYRADVFQKAGLPSEPADVAAATatWDDYFA 186
Cdd:COG1840    50 LANEGLLQPYKS----PELDAIPAE----FRDPDGYWFG--FSVRARVIVYNTDLLKELGVPKSWEDLLDPE--YKGKIA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 187 FGKRLKAATGGAIFvdasdvftksigqgtTRFVDEDGDytgdspevKAAWDravlaYQEGLTAN---VTDGSPDWASAIS 263
Cdd:COG1840   118 MADPSSSGTGYLLV---------------AALLQAFGE--------EKGWE-----WLKGLAANgarVTGSSSAVAKAVA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826989924 264 NGSLPALLGASWYQADLKSATADTSGdwrVAPMPGGPANIGGsfLSIPAGTKDPEAAFAVIKDVLSEDNQvTAYADKGIF 343
Cdd:COG1840   170 SGEVAIGIVNSYYALRAKAKGAPVEV---VFPEDGTLVNPSG--AAILKGAPNPEAAKLFIDFLLSDEGQ-ELLAEEGYE 243

                         250
                  ....*....|.
gi 1826989924 344 PSATAAYDAPK 354
Cdd:COG1840   244 YPVRPDVEPPE 254
 
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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