|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_LIVBP-like |
cd06342 |
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ... |
32-368 |
2.01e-144 |
|
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine); This subgroup includes the type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems that are involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup also includes a leucine-specific binding protein (or LivK), which is very similar in sequence and structure to leucine-isoleucine-valine binding protein (LIVBP). ABC-type active transport systems are transmembrane proteins that function in the transport of diverse sets of substrates across extra- and intracellular membranes, including carbohydrates, amino acids, inorganic ions, dipeptides and oligopeptides, metabolic products, lipids and sterols, and heme, to name a few.
Pssm-ID: 380565 [Multi-domain] Cd Length: 334 Bit Score: 413.08 E-value: 2.01e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVGHWNTG 111
Cdd:cd06342 1 KIGVAGPLTGPNAALGQDIRNGAELAVDEINAKG---GGLGFKIELVAQDDACDPAQAVAAAQKLVADGVVAVIGHYNSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd06342 78 AAIAAAPIYAEAGIPMISPSATNPKLTEQGYKNFFRVVGTDDQQGPAAADYAAKTLKAKRVAVIHDGTAYGKGLADAFKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQKE 271
Cdd:cd06342 158 ALKALGGTVVGREGITPGTTDFSALLTKIKAANPDAVYFGGYYPEAGLLLRQLREAGLKAPFMGGDGIVSPDFIKAAGDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 272 GNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISYSGVTGQIA 351
Cdd:cd06342 238 AEGVYATTPGAPPEKLPAAKAFLKAYKAKFGEPPGAYAAYAYDAAQVLLAAIEKAGSTDRAAVAAALRATDFDGVTGTIS 317
|
330
....*....|....*..
gi 2294035498 352 FDKEGNLKSPTFTVYKV 368
Cdd:cd06342 318 FDAKGDLTGPAFTVYQV 334
|
|
| PBP1_ABC_HAAT-like |
cd06349 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
32-373 |
6.37e-89 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380572 [Multi-domain] Cd Length: 338 Bit Score: 271.75 E-value: 6.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd06349 1 KIGVSGPLTGDNAEYGQQFKNGVELAVDEINAAG---GVNGRKLELVVYDDQGDPKEAVNIAQKFVsDDKVVAVIGDFSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKqGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06349 78 SCSMAAAPIYEEAGLVQISPTASHPDFTK-GGDYVFRNSPTQAVEAPFLADYAVKKLGAKKIAIIYLNTDWGVSAADAFK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd06349 157 KAAKALGGEIVATEAYLPGTKDFSAQITKIKNANPDAIYLAAYYNDAALIAKQARQLGWDVQIFGSSSLYSPEFIELAGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISYSGVTGQI 350
Cdd:cd06349 237 AAEGVYLSSPFFPESPDPEVKEFVKAYKAKYGEDPDDFAARAYDAVNILAEAIEKAGTDREAIRDALANIKDFSGLTGTI 316
|
330 340
....*....|....*....|...
gi 2294035498 351 AFDKEGNLkSPTFTVYKVVDGKW 373
Cdd:cd06349 317 TFDENGDV-LKSLTILVVKDGKF 338
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
28-375 |
1.12e-84 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 259.86 E-value: 1.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 28 GETVTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVG 106
Cdd:COG0683 1 ADPIKIGVLLPLTGPYAALGQPIKNGAELAVEEINAAG---GVLGRKIELVVEDDASDPDTAVAAARKLIDQdKVDAIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 107 HWNTGTSIPAARVYHDAGIAQVAPVATGHAYTKQ-GFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGL 185
Cdd:COG0683 78 PLSSGVALAVAPVAEEAGVPLISPSATAPALTGPeCSPYVFRTAPSDAQQAEALADYLAKKLGAKKVALLYDDYAYGQGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 186 ADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMgaggfvsqtfl 265
Cdd:COG0683 158 AAAFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPLN----------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 266 qlaqkegngvvalepglpveqmpggKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISYSG 345
Cdd:COG0683 227 -------------------------KAFVKAYKAKYGREPSSYAAAGYDAALLLAEAIEKAGSTDREAVRDALEGLKFDG 281
|
330 340 350
....*....|....*....|....*....|.
gi 2294035498 346 VTGQIAFDKEGNLKSPtFTVYKVV-DGKWQP 375
Cdd:COG0683 282 VTGPITFDPDGQGVQP-VYIVQVKaDGKFVV 311
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-357 |
1.09e-73 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380570 [Multi-domain] Cd Length: 334 Bit Score: 232.43 E-value: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd06347 2 IGVIGPLTGEAAAYGQPALNGAELAVDEINAAG-GILGKKI--ELIVYDNKSDPTEAANAAQKLIDEdKVVAIIGPVTSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRT-AFGQGLADEFI 190
Cdd:cd06347 79 IALAAAPIAQKAKIPMITPSATNPLVTKGG-DYIFRACFTDPFQGAALAKFAYEELGAKKAAVLYDVSsDYSKGLAKAFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd06347 158 EAFEKLGGEIVAEETYTSGDTDFSAQLTKIKAANPDVIFLPGYYEEAALIIKQARELGITAPILGGDGWDSPELLELGGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVylpVLRAIS----YSGV 346
Cdd:cd06347 238 AVEGVYFTTHFSPDDPSPEVQEFVKAYKAKYGEPPNAFAALGYDAVMLLADAIKRAGSTDPEA---IRDALAktkdFEGV 314
|
330
....*....|.
gi 2294035498 347 TGQIAFDKEGN 357
Cdd:cd06347 315 TGTITFDPNGN 325
|
|
| PBP1_ABC_HAAT-like |
cd06344 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-359 |
9.89e-70 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380567 [Multi-domain] Cd Length: 332 Bit Score: 222.10 E-value: 9.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPltgpSARIGKDLENGAQLAIDDINKQhPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNTG 111
Cdd:cd06344 4 IGVAWP----FAPDGDLFLEGVELAVEEINAA-GGVLGRKI--RLVEYDDEASVDKGLAIAQRFAdNPDVVAVIGHRSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQtLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd06344 77 VAIPASIIYERAGLLMLSPGATAPKLTQHGFKYIFRNIPSDEDIARQLARYAAR-QGYKRIVIYYDDDSYGKGLANAFEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSK-NADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd06344 156 EARELGITIVDRRSYSSDEEDFRRLLSKWKALdFFDAIFLAGSMPEGAEFIKQARELGIKVPIIGGDGLDSPELIEIAGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISY-SGVTGQ 349
Cdd:cd06344 236 AAEGVVVATVFDPDDPRPEVRAFVEAFRKKYGREPDVWAAQGYDAVKLLAEAIEKAGSTVPAKIASALRFLENwEGVTGT 315
|
330
....*....|
gi 2294035498 350 IAFDKEGNLK 359
Cdd:cd06344 316 YSFDANGDVV 325
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
32-320 |
2.54e-67 |
|
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.
Pssm-ID: 380492 [Multi-domain] Cd Length: 298 Bit Score: 214.88 E-value: 2.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPtIGGKavTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd06268 1 KIGVVVPLTGPYADYGEEILRGVALAVEEINAAGG-INGR--KLELVIADDQGDPETAVAVARKLVdDDKVLAVVGHYSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06268 78 SVTLAAAPIYQEAGIPLISPGSTAPELTEGGGPYVFRTVPSDAMQAAALADYLAKKLKGKKVAILYDDYDYGKSLADAFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd06268 158 KALKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAANALKQARELGLKLPILGGDGLYSPELLKLGGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd06268 238 AAEGVVVAVPWHPDSPDPPKQAFVKAYKKKYGGPPSWRAATAYDATQALA 287
|
|
| PBP1_ABC_ligand_binding-like |
cd19980 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-365 |
2.55e-66 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380635 [Multi-domain] Cd Length: 334 Bit Score: 213.62 E-value: 2.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNTG 111
Cdd:cd19980 2 IGVIAPLSGPVAALGQQVLNGAKLAVEEINAKG---GVLGRKLELVVEDDKCPPAEGVAAAKKLItDDKVPAIIGAWCSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd19980 79 VTLAVMPVAERAKVPLVVEISSAPKITEGGNPYVFRLNPTNSMLAKAFAKYLADKGKPKKVAFLAENDDYGRGAAEAFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQKE 271
Cdd:cd19980 159 ALKAKGVKVVATEYFDQGQTDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLKQQLVGTGGTTSPDLIKLAGDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 272 GNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDP-AVYLPVLRAISYSGVTGQI 350
Cdd:cd19980 239 AEGVYGASIYAPTADNPANKAFVAAYKKKYGEPPDKFAALGYDAVMVIAEAIKKAGSTDPeKIRAAALKKVDYKGPGGTI 318
|
330
....*....|....*
gi 2294035498 351 AFDKEGNLKSPTFTV 365
Cdd:cd19980 319 KFDEKGQAHKNVVLV 333
|
|
| PRK15404 |
PRK15404 |
high-affinity branched-chain amino acid ABC transporter substrate-binding protein; |
2-367 |
2.84e-63 |
|
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
Pssm-ID: 237959 [Multi-domain] Cd Length: 369 Bit Score: 206.80 E-value: 2.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 2 KTAKISALSAAIVLSGFASSAAWsaagETVTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGKAVTFKLqseD 81
Cdd:PRK15404 1 MKSKGKTLLAGCIALALSHAALA----DDIKIAIVGPMSGPVAQYGDMEFTGARQAIEDINAKGGIKGDKLEGVEY---D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 82 DQSDPRTAVAVAQRLVDSGVAGVVGHWNTGTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQ 161
Cdd:PRK15404 74 DACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLIFRTIGLDSDQGPTAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 162 YAVQTLKAKRIAVIDDRTAFGQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLA 241
Cdd:PRK15404 154 YILEKVKPKRIAVLHDKQQYGEGLARSVKDGLKKAGANVVFFEGITAGDKDFSALIAKLKKENVDFVYYGGYHPEMGQIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 242 RRIKQMGISATLMGAGGFVSQTFLQLAQKEGNGVVALEPGlPVEQMPGGKAFEQAYQSRYHthiELHAPF---AYDATRV 318
Cdd:PRK15404 234 RQAREAGLKTQFMGPEGVGNKSLSNIAGPASEGMLVTLPK-RYDQDPANKAIVDAFKAKKQ---DPSGPFvwtTYAAVQS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2294035498 319 LAAAMEKADSVDPAVYLPVLRAISYSGVTGQIAFDKEGNLKSPTFTVYK 367
Cdd:PRK15404 310 LAAGINRAGSDDPAKVAKYLKANTFDTVIGPLSWDEKGDLKGFEFGVFE 358
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
33-331 |
7.63e-59 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380558 [Multi-domain] Cd Length: 348 Bit Score: 194.75 E-value: 7.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVD-SGVAGVVGHWNTG 111
Cdd:cd06335 2 IGVIGPLTGPSAELGESARRGVELAVEEINAAG-GILGRKI--ELVERDDEANPTKAVQNAQELIDkEKVVAIIGPTNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQG---FDTSFRVMGHDDDGGQFAGQYAVQTlKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06335 79 VALATIPILQEAKIPLIIPVATGTAITKPPakpRNYIFRVAASDTLQADFLVDYAVKK-GFKKIAILHDTTGYGQGGLKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLA 268
Cdd:cd06335 158 VEAALKKRGITPVATESFKIGDTDMTPQLLKAKDAGADVILVYGLGPDLAQILKAMEKLGWKVPLVGSWGLSMPNFIELA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2294035498 269 QKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFA---YDATRVLAAAMEKADSVDP 331
Cdd:cd06335 238 GPLAEGTIMTQTFIEDYLTPRAKKFIDAYKKKYGTDRIPSPVSAaqgYDAVYLLAAAIKQAGSTDG 303
|
|
| PBP1_ABC_HAAT-like |
cd19985 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-320 |
1.23e-57 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380640 [Multi-domain] Cd Length: 321 Bit Score: 190.56 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVGHWNTGT 112
Cdd:cd19985 2 IAVVGPMSGKSASKGKSMLRGAELYIDQINAA-GGINGKKV--KLDVFDDQNDPDAARKAAQIIVSDKALAVIGHYYSSA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 113 SIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIKS 192
Cdd:cd19985 79 SIAAGKIYKKAGIPAITPSATADAVTRDN-PWYFRVIFNDSLQGRFLANYAKKVLKKDKVSIIYEEDSYGKSLASVFEAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 193 LKAQGIDIVDRQYVDDKTVDFSAVLTAIRSK------NADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQ 266
Cdd:cd19985 158 ARALGLKVLKKWSFDTDSSQLDQNLDQIVDElkkapdEPGVIFLATHADEGAKLIKKLRDAGLKAPIIGPDSLASESFAQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2294035498 267 LAQKEG----------NGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19985 238 GFAEYPeekeepgyytDGIYATSPFIFDIANEKAQKFRDTYQKRYGEEPSWIAAFAYDAAMLAI 301
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-320 |
1.32e-57 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380643 [Multi-domain] Cd Length: 302 Bit Score: 189.79 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLVD-SGVAGVVGHWNTG 111
Cdd:cd19988 2 IGVFGPLSGDAAPYGQAMLQGAELAVEEINAAG---GILGIPIELVVEDDEGLPAASVSAAKKLIYqDKVWAIIGSINSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd19988 79 CTLAAIRVALKAGVPQINPGSSAPTITESGNPWVFRCTPDDRQQAYALVDYAFEKLKVTKIAVLYVNDDYGRGGIDAFKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQKE 271
Cdd:cd19988 159 AAKKYGIEVVVEESYNRGDKDFSPQLEKIKDSGAQAIVMWGQYTEGALIAKQARELGLKQPLFGSDGLVTPKFIELAGDA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2294035498 272 GNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19988 239 AEGAIATTPFLPDSDDPKVSAFVEKYKKRYGEEPDVFAAQAYDAMNILA 287
|
|
| PBP1_ABC_ligand_binding-like |
cd06345 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
32-356 |
9.92e-57 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380568 [Multi-domain] Cd Length: 356 Bit Score: 189.40 E-value: 9.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTgpsARIGKDLENGAQLAIDDINKQhPTIGGKavTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd06345 1 KIGVLGPLS---APAGEAMERGAELAVEEINAA-GGILGR--KVELVVADTQGKPEDGVAAAERLItEDKVDAIVGGFRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTS------FRVMGHDDDGGQ----FAGQYAVQTLKAKRIAVIDDRTA 180
Cdd:cd06345 75 EVVLAAMEVAAEYKVPFIVTGAASPAITKKVKKDYekykyvFRVGPNNSYLGAtvaeFLKDLLVEKLGFKKVAILAEDAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 181 FGQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGF- 259
Cdd:cd06345 155 WGRGIAEALKKLLPEAGLEVVGVERFPTGTTDFTPILSKIKASGADVIVTIFSGPGGILLVKQWAELGVPAPLVGINVPa 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 260 VSQTFLQLAQKEGNGVVALEPGLPVEQM-PGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVL 338
Cdd:cd06345 235 QDPEFWENTGGAGEYEITLAFAAPKAKVtPKTKPFVDAYKKKYGEAPNYTAYTAYDAIYILAEAIERAGSTDPDALVKAL 314
|
330
....*....|....*...
gi 2294035498 339 RAISYSGVTGQIAFDKEG 356
Cdd:cd06345 315 EKTDYEGVRGRIKFDKKD 332
|
|
| PBP1_ABC_ligand_binding-like |
cd06340 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
33-356 |
2.86e-54 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380563 [Multi-domain] Cd Length: 352 Bit Score: 182.76 E-value: 2.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQH--PTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWN 109
Cdd:cd06340 2 IGVLYPLSGPLALIGQEAKRGAELAVDEINAAGgiKSLGGAKI--ELVVADTQSDPEVAASEAERLItQEGVVAIIGAYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAV-----QTLKAKRIAVIDDRTAFGQG 184
Cdd:cd06340 80 SSVTLAASQVAERYGVPFVTASAVADEITERGFKYVFRTAPTASQFAEDAVDFLKelakkKGKKIKKVAIIYEDSAFGTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 185 LADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGIS--ATLMGAGGFVSQ 262
Cdd:cd06340 160 VAKGLKKAAKKAGLEVVLDEPYPAGATDLSSEVLKLKAAKPDVVFATSYTNDAILLLRTMKELGFKpkAIIGVGGGYSDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 263 TFLQLAQKEGNGVVALEPGLP--VEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVyLPVLRA 340
Cdd:cd06340 240 EFLKALGKDAEGVFSVVPWSPdlAKKKPGAKEVNERYKKKYGEDMTGHAARAYTAAWVLADALERAGSTDPEA-IRAAAA 318
|
330 340
....*....|....*....|..
gi 2294035498 341 ISYSGVTGQ------IAFDKEG 356
Cdd:cd06340 319 LTLDIPEGLimpgggVKFDEKG 340
|
|
| PBP1_ABC_ligand_binding-like |
cd19984 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
32-320 |
3.43e-54 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380639 [Multi-domain] Cd Length: 296 Bit Score: 180.88 E-value: 3.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPtIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNT 110
Cdd:cd19984 1 KIGVILPLTGDAASYGEDMKNGIELAVEEINAAGG-INGKKI--ELIYEDSKCDPKKAVSAANKLINVdKVKAIIGGVCS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKaKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd19984 78 SETLAIAPIAEQNKVVLISPGASSPEITKAG-DYIFRNYPSDAYQGKVLAEFAYNKLY-KKVAILYENNDYGVGLKDVFK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd19984 156 KEFEELGGKIVASESFEQGETDFRTQLTKIKAANPDAIFLPGYPKEGGLILKQAKELGIKAPILGSDGFEDPELLEIAGE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19984 236 AAEGVIFTYPAFDDSSEKKQKFFFYRYKEKYGKEPDIYAALAYDAVMILA 285
|
|
| PBP1_ABC_HAAT-like |
cd19981 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-325 |
4.67e-54 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380636 [Multi-domain] Cd Length: 297 Bit Score: 180.56 E-value: 4.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINkQHPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd19981 2 IGFFAPLTGPAAADGKSALHGAELAVEQIN-AAGGINGKKV--ELVVYDDQASPKQAVNIAQKLIEQdKVVAVVSGSYSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd19981 79 PTRAAAPIFQEAKVPMVSAYAVHPDITKAG-DYVFRVAFLGPVQGRAGAEYAVKDLGAKKVAILTIDNDFGKSLAAGFKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQKE 271
Cdd:cd19981 158 EAKKLGAEIVSEYAYALGDRDFRPILTKIKSANPDAIYASGYYAEAAPIVKQARELGIKVPIIGQEGYDSPKFIEIAGSA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2294035498 272 GNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEK 325
Cdd:cd19981 238 AEGVIITTSLNRDSDRPITQKFIKEYRKRYGIDPDMVAASTYDAVMVLAGEVQK 291
|
|
| PBP1_ABC_ligand_binding-like |
cd06338 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
32-371 |
5.48e-54 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380561 [Multi-domain] Cd Length: 347 Bit Score: 182.01 E-value: 5.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHP-TIGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWN 109
Cdd:cd06338 1 KIGASLSLTGPFAGEGKAQKRGYELWVEDVNAAGGvKGGGKKRPVELVYYDDQSDPATAVRLYEKLITEdKVDLLLGPYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAV-QTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06338 81 SGLTLAAAPVAEKYGIPMIAGGAASDSIFERGYKYVFGVLPPASDYAKGLLDLLAeLGPKPKTVAIVYEDDPFGKEVAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLA 268
Cdd:cd06338 161 AREAAKKAGLEVVYDESYPPGTTDFSPLLTKVKAANPDILLVGGYPPDAITLVRQMKELGYNPKAFFLTVGPAFPAFREA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 269 QKE-GNGVVAL---EPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISYS 344
Cdd:cd06338 241 LGKdAEGVLGPsqwEPSLPYKVFPGAKEFVKAYKEKFGEEPSYHAAAAYAAGQVLQQAIEKAGSLDPEKVRDALASLDFD 320
|
330 340
....*....|....*....|....*..
gi 2294035498 345 GVTGQIAFDKEGNLKSPTFTVYKVVDG 371
Cdd:cd06338 321 TVYGPIKFDETGLQIGKPMVVVQWQGG 347
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
30-371 |
8.64e-54 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 181.32 E-value: 8.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 30 TVTIGLAGPLTGPSARIGKDLENGAQLAIDDINKqHPTIGGKAVTfkLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHW 108
Cdd:pfam13458 1 PIKIGVLTPLSGPYASSGKSSRAGARAAIEEINA-AGGVNGRKIE--LVVADDQGDPDVAAAAARRLVDQdGVDAIVGGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 109 NTGTSIPAARVYHDAGIAQVAPVATghaYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:pfam13458 78 SSAVALAVAEVLAKKGVPVIGPAAL---TGEKCSPYVFSLGPTYSAQATALGRYLAKELGGKKVALIGADYAFGRALAAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISA---TLMGAGGFvSQTFL 265
Cdd:pfam13458 155 AKAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGADAVLLANAGADTVNLLKQAREAGLDAkgiKLVGLGGD-EPDLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 266 QLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRY-HTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAISYS 344
Cdd:pfam13458 234 ALGGDAAEGVYATVPFFPDLDNPATRAFVAAFAAKYgEAPPTQFAAGGYIAADLLLAALEAAGSPTREAVIAALRALPYD 313
|
330 340
....*....|....*....|....*..
gi 2294035498 345 GVTGQIAFDKEGNLKSPTFTVYKVVDG 371
Cdd:pfam13458 314 GPFGPVGFRAEDHQAVHCMYLVQVKAD 340
|
|
| PBP1_ABC_HAAT-like |
cd19986 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-320 |
7.04e-52 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380641 [Multi-domain] Cd Length: 297 Bit Score: 174.74 E-value: 7.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptiGG-KAVTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd19986 2 IGVVAPLTGPAALNGEYQKNGAQLALEEINAA----GGvLGRPLELVVEDDQGTNTGAVNAVNKLIsDDKVVAVIGPHYS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPvATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd19986 78 TQVLAVSPLVKEAKIPVITG-GTSPKLTEQGNPYMFRIRPSDSVSAKALAKYAVEELGAKKIAILYDNDDFGTGGADVVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQK 270
Cdd:cd19986 157 AALKALGLEPVAVESYNTGDKDFTAQLLKLKNSGADVIIAWGHDAEAALIARQIRQLGLDVPVIGSSSFATPTVLLLAGE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2294035498 271 EGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19986 237 ALEGIYSVTDFVPSDPDPKVQAFVKKYKAKYGEDPDLYSAWYYDAMYLLA 286
|
|
| PBP1_ABC_ligand_binding-like |
cd06346 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
32-368 |
4.65e-49 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380569 [Multi-domain] Cd Length: 314 Bit Score: 168.13 E-value: 4.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptiGG-KAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWN 109
Cdd:cd06346 1 KIGALLPLTGPLASLGPPMLAAAELAVEEINAA----GGvLGKKVELVVEDSQTDPTAAVDAARKLVDVeGVPAIVGAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGIAQVAPVATGHAYTKQGF-DTSFRVMGHDDDGGQFAGQYAvQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06346 77 SGVTLAVASVAVPNGVVQISPSSTSPALTTLEDkGYVFRTAPSDALQGVVLAQLA-AERGFKKVAVIYVNNDYGQGLADA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISAT-LMGAGGFVSQTFLQ- 266
Cdd:cd06346 156 FKKAFEALGGTVTASVPYEPGQTSYRAELAQAAAGGPDALVLIGYPEDGATILREALELGLDFTpWIGTDGLKSDDLVEa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 267 LAQKEGNGVVALEPGLPVEqmPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAmekadsvdpavylpvlraisYSGV 346
Cdd:cd06346 236 AGAEALEGMLGTAPGSPGS--PAYEAFAAAYKAEYGDDPGPFAANAYDAVMLLALA--------------------YEGA 293
|
330 340
....*....|....*....|..
gi 2294035498 347 TGQIAFDKEGNLkSPTFTVYKV 368
Cdd:cd06346 294 SGPIDFDENGDV-AGPYEIWKV 314
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-371 |
1.29e-45 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380571 [Multi-domain] Cd Length: 342 Bit Score: 159.71 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHptiGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd06348 2 IGVALSLTGPGALYGQSQKNGAQLAVEEINAAG---GVGGVKIELIVEDTAGDPEQAINAFQKLINQdKVLAILGPTLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVI----DDRTAFGqglAD 187
Cdd:cd06348 79 EAFAADPIAQQAKVPVVGISNTAPGITDIG-PYIFRNSLPEDKVIPPTVKAAKKKYGIKKVAVLydqdDAFTVSG---TK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 188 EFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQL 267
Cdd:cd06348 155 VFPAALKKNGVEVLDTETFQTGDTDFSAQLTKIKALNPDAIVISALAQEGALIVKQARELGLKGPIVGGNGFNSPDLIKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 268 AQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYL-----PVLRAIS 342
Cdd:cd06348 235 AGKAAEGVIVGSAWSPDNPDPKNQAFVAAYKEKYGKEPDQFAAQAYDAAYILAEAIKKAGSTTDRADLrdalaRILIAKD 314
|
330 340
....*....|....*....|....*....
gi 2294035498 343 YSGVTGQIAFDKEGNLKSPTFtVYKVVDG 371
Cdd:cd06348 315 FEGPLGPFSFDADRDGIQPPV-VLIVKDG 342
|
|
| PBP1_ABC_ligand_binding-like |
cd06336 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
33-332 |
1.45e-45 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380559 [Multi-domain] Cd Length: 345 Bit Score: 159.71 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHP-TIGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHwNT 110
Cdd:cd06336 2 IGFLGPLSGPAAAWGLPMLRGLELAADEINAAGGiKVGGKKYKVEVVSYDDKYTPAEAVAAARRLVSQdGVKFIFGP-GG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06336 81 SAIAAAVQPVTERNKVLLLTAAFSDPILGPDNPLLFRIPPTPYEYAPPFIKWLKKNGPIKTVALIAPNDATGKDWAAAFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVD-SQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQ 269
Cdd:cd06336 161 AAWKAAGGEVVAEEFYDRGTTDFYPVLTKILALKPDALDLGGSSpGPAGLIIKQARELGFKGPFVSEGGAKADEILKEVG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2294035498 270 KEG-NGVVALEPG-LPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPA 332
Cdd:cd06336 241 GEAaEGFIGVLPAdDDPIASPGAKAFVERYKKKYGEPPNSESALFYDAAYILVKAMEKAGTVDDT 305
|
|
| PBP1_ABC_RPA1789-like |
cd06333 |
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ... |
33-355 |
2.10e-44 |
|
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs; This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).
Pssm-ID: 380556 [Multi-domain] Cd Length: 342 Bit Score: 156.55 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd06333 2 IGAILSLTGPAASLGIPERNAVELLVEQINAA-GGINGRKL--ELIVYDDESDPTKAVTNARKLIEEdKVDAIIGPSTTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGhAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTlKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd06333 79 ESLAVAPIAEEAKVPLISLAGAA-AIVEPVRKWVFKTPQSDSLVAEAILDYMKKK-GIKKVALLGDSDAYGQSGRAALKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAQKE 271
Cdd:cd06333 157 LAPEYGIEIVADERFARTDTDMTAQLTKIRAAKPDAVLVWASGPPAALVAKNLRQLGYKGPIYQSHGAANQDFIKLAGKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 272 GNGVVALEPGLPV-EQMPGG-------KAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLRAIS- 342
Cdd:cd06333 237 AEGVILPAGKLLVaDQLPDSdpqkkvlLEFVKAYEAKYGEGPSTFAGHAYDALLLLVEAIEPAGGTDRAALRDALENTKg 316
|
330
....*....|...
gi 2294035498 343 YSGVTGQIAFDKE 355
Cdd:cd06333 317 LVGVTGVYNFSPT 329
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
33-320 |
2.05e-42 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380637 [Multi-domain] Cd Length: 302 Bit Score: 150.12 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhPTIGGKAVTFKLqsEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd19982 2 IGAILSLTGPFAPFGEMFKNGYEMALEEINAA-GGIKGKKLELVI--EDDQSKPQTALAAAEKLVSQdKVPLIVGGYSSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEFIK 191
Cdd:cd19982 79 ITLPVAAVAERQKIPLLVPTAADDDITKPGYKYVFRLNPPASIYAKALFDFFKELVKPKTIAILYENTAFGTSVAKAARR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 192 SLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLM--GAGGFVSQTFLQLAQ 269
Cdd:cd19982 159 FAKKRGIEVVADESYDKGATDFKPLLNKVKAANPDVVYMVSYLNDAILLMRQAKELGLNPKLFagGGAGFTIPEFLKQAG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2294035498 270 KEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19982 239 PLAEYVVTATLWSPDVKYPGAKEFYEKYKAKYGVEPSYHEAEAYAALYVAA 289
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
28-373 |
1.88e-39 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.
Pssm-ID: 380566 [Multi-domain] Cd Length: 355 Bit Score: 143.86 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 28 GETVTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptiGG-KAVTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVV 105
Cdd:cd06343 4 DDEIKIGTSLPLSGPAAAYGKPVRAGAAAYFDEVNAA----GGiNGRKIELIVEDDGYDPARAVAAVRKLVEQdKVFAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 106 GHWNTGTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGL 185
Cdd:cd06343 80 GGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKPYTFGVQPSYEDEGRILADYIVETLPAAKVAVLYQNDDFGKDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 186 ADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFL 265
Cdd:cd06343 160 LEGLKEALKAYGLEVVAEETYEPGDTDFSSQVLKLKAAGADVVVLGTLPKEAAAALKEAAKLGWKPTFLGSSVSADPTTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 266 QLAQKE-GNGVVALEPGLPVEQM--PGGKAFEQAYQSRYH-THIELHAPFAYDATRVLAAAMEKA-DSVDPAVYLPVLRA 340
Cdd:cd06343 240 AKAGGDaAEGVYSASYLKDPTDAddPAVKEFREAYKKYFPdDPPNAYALYGYAAAQVFVEALKRAgKDLTREGLIKALES 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 2294035498 341 ISYS---GVTGQIAFDKEGNLKSPTFTVYKVVDGKW 373
Cdd:cd06343 320 LKDFddgGPGPPVTFSPDDHRGIESMYLVQVDGGKW 355
|
|
| PBP1_ABC_HAAT-like |
cd19983 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
33-320 |
1.20e-38 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380638 [Multi-domain] Cd Length: 303 Bit Score: 140.41 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVGHWNTGT 112
Cdd:cd19983 2 IGFVGGLTGRYSDLGVQGRNGAQLAVEEINAAG-GINGRPV--ELIIRDDQQDPEAAKAADRELIAGGVVAIIGHMTSAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 113 SIPAARVYHDAGIAQVAPVATGHAYTKQGfDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRT--AFGQGLADEFI 190
Cdd:cd19983 79 TVAVLPVINEAKVLMISPTVSTPELSGKD-DYFFRVTPTTRESAQALARYAYNRGGLRRVAVIYDLSnrAYSESWLDNFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIV-DRQYVDDKTVDFSAVLTAIRSKNADLIFF--GGVDsqAAPLARRIKQMGISATLMGAGGFVSQTFLQL 267
Cdd:cd19983 158 SEFEALGGRIVaEIPFSSGADVDFSDLARRLLASKPDGLLLvaSAVD--TAMLAQQIRKLGSKIPLFSSAWAATEELLEL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2294035498 268 AQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19983 236 GGKAVEGMLFSQAYDRNSSNPRYLAFKEAYEERFGREPSFAAAYAYEAAMVLA 288
|
|
| PBP1_aromatic_compounds-like |
cd06332 |
type 1 periplasmic binding proteins of active transport systems predicted to be involved in ... |
32-368 |
1.76e-38 |
|
type 1 periplasmic binding proteins of active transport systems predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; This group includes the type 1 periplasmic binding proteins of active transport systems that are predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; their substrate specificities are not well characterized, however. Members also exhibit close similarity to active transport systems for short chain amides and/or urea found in bacteria and archaea.
Pssm-ID: 380555 [Multi-domain] Cd Length: 336 Bit Score: 140.81 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKqhpTIGGKAVTFKLqsEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNT 110
Cdd:cd06332 1 KIGLLAPLTGPFAALGEDMVRGFELALEEVGG---EVAGRKVELVV--EDDAGDPDTAVTKARKLVEQdKVDVLIGPLSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMGHDDDGGQFA-GQYAVQTLKAKRIAVIDDRTAFGQGLADEF 189
Cdd:cd06332 76 DEGLAVAPYAKEPGVPFINPVAGADDLTQRAKAPNFFRTSFTGSQWSAPlGDYAYKELGYKKVATIGSDYAFGYEQAAGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 190 IKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSkNADLIFFGGVDSQAAPLARRIKQMGI--SATLMGAGGFVSQTFLQL 267
Cdd:cd06332 156 KRGFEAAGGEVVQEIWVPLGTTDFSPYIAQIPS-ADDAVFAFLGGADAVRFLKQYREFGLkdKIPLIGGGTTVDESVLPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 268 AQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKA--DSVDPAVYLPVLRAISYSG 345
Cdd:cd06332 235 MGDAALGIISASHYAEGLDNPENKKFVAAYKKKFGKLPSLYAAGGYDGAQAILEALEAVggDVSDKQALAAALRKVKFDS 314
|
330 340
....*....|....*....|...
gi 2294035498 346 VTGQIAFDKEGNLKSPTFtVYKV 368
Cdd:cd06332 315 PRGPFSFDENRNPVQNVY-IREV 336
|
|
| PBP1_alkylbenzenes-like |
cd06360 |
type 1 periplasmic binding component of active transport systems predicted be involved in ... |
32-375 |
1.68e-34 |
|
type 1 periplasmic binding component of active transport systems predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; This group includes the type 1 periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; their substrate specificity is not well characterized, however.
Pssm-ID: 380583 [Multi-domain] Cd Length: 357 Bit Score: 130.49 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptIGGKAVTFKLqsEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNT 110
Cdd:cd06360 1 KIGVLLPLTGPLAVNGEDVRDGFELYFDEIGNQ---VAGRKIELIV--EDDEGKPDVGLTKARKLVERdKVHVLAGIVSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIpAARVY-HDAGIAQVAPVATGHAYT-KQGFDTSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06360 76 AVAY-AVRDYvVEQKIPLVISNAGAAPLTqELASPYIFRTSFSNGQYDAPFGQYAYEKLGYRRIAVMASDYAAGHEQAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISAT--LMGAGGFVSQTFLQ 266
Cdd:cd06360 155 FARTFKQAGGKVVQEIYPPLGTADFAPYLARIQQDAADAVWAFFAGADAIRFVKQYDEYGLKGKlpLVGIGGLVDDAILP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 267 LAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAME--KADSVDPAVYLPVLRAISYS 344
Cdd:cd06360 235 EQGDAALGIVSYLHYSAALDTPENKAFVQAYRKKYGRDPGLYAEGGYVAARAIAEALEavKGNVEDKEAFLEALRKVRFE 314
|
330 340 350
....*....|....*....|....*....|...
gi 2294035498 345 GVTGQIAFDKEGNLKSPTFtVYKV--VDGKWQP 375
Cdd:cd06360 315 APRGPFRFDPYQQAVVTTY-IRRVekVDGKLVN 346
|
|
| PBP1_AmiC-like |
cd06331 |
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system ... |
33-357 |
1.82e-32 |
|
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF); This group includes the type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF), found in bacteria and Archaea. AmiC controls expression of the amidase operon by a ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon is induced. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems.
Pssm-ID: 380554 [Multi-domain] Cd Length: 333 Bit Score: 124.64 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd06331 2 IGLLTPLSGPASVYGRAIANGAELAVEEINAAG-GVLGRPV--ELVVEDDASDPATAVAAARRLIQQdKVDAIVGPITSA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVAT-GHAYTKQGFDTsfrvmghdddgGQFAGQY------AVQTLKAKRIAVIDDRTAFGQG 184
Cdd:cd06331 79 TRNAVAPVAERAKVPLLYPTFYeGGECSPYLFCF-----------GEVPNQQldplipWLMEEYGKKFYLIGSDYVWPRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 185 LADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTF 264
Cdd:cd06331 148 MNDAARRVIEAHGGEVVGEEYLPLGTTDFSSVIEKIKASGADVVLSTLVGADAVTFLKQFAAAGLRRKVRIAALLFDENT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 265 LQLAQ-KEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYhthiELHAPF-------AYDATRVLAAAMEKADSVDPAVYLP 336
Cdd:cd06331 228 LAGLGaEAAEGIYSVLSYFQSLDTPENKAFVAAYRKKF----GEDAPPitslseaAYEAVHLYAAAVEKAGSTDPEAVIA 303
|
330 340
....*....|....*....|.
gi 2294035498 337 VLRAISYSGVTGQIAFDKEGN 357
Cdd:cd06331 304 ALPGVSFDGPQGPVTMDPDNH 324
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
32-357 |
9.31e-32 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.
Pssm-ID: 380553 [Multi-domain] Cd Length: 342 Bit Score: 122.67 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPtIGGKavTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNT 110
Cdd:cd06330 1 KIGVITPLSGAAAVYGEPARNGAELAVEEINAAGG-ILGR--KIELVVRDDKGKPDEAVRAARELVLQeGVDFLIGTISS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYTKQGF-DTSFRVMGHDD-DGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06330 78 GVALAVAPVAEELKVLFIATDAATDRLTEENFnPYVFRTSPNTYmDAVAAALYAAKKPPDVKRWAGIGPDYEYGRDSWAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGID--IVDRQYVDDKTVDFSAVLTAIRSKNADLIFFG--GVD-----SQAAP--LARRIKqmgisATLMGAG 257
Cdd:cd06330 158 FKAALKKLKPDveVVGELWPKLGATDYTAYITALLAAKPDGVFSSlwGGDlvtfvKQAKPygLFDKTK-----VVSGLGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 258 GFVSQTFLQLAQKEGNGVVALEP-GLPVEqmPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLP 336
Cdd:cd06330 233 GSEVLQALGKEMPEGLIGGGRYPfGWPDT--PLNKAFVEAYRAKYGEYPTYWAYEAYAAVMALKAAIEKAGSTDTDKVIA 310
|
330 340
....*....|....*....|.
gi 2294035498 337 VLRAISYSGVTGQIAFDKEGN 357
Cdd:cd06330 311 ALEGLTFDTPGGKITIRAEDH 331
|
|
| PBP1_RPA0668_benzoate-like |
cd20014 |
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the ... |
33-372 |
4.12e-31 |
|
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).
Pssm-ID: 380667 [Multi-domain] Cd Length: 346 Bit Score: 121.19 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptIGGKAVTfkLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd20014 2 IGLLLPYSGVYAALGEDIRNGFQLYLDEHGGK---LGGRPIE--LVKEDDEADPDVALQKARKLIEQdKVDVLVGPVSSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYT-KQGFDTSFRVMGHDDDGGQFAGQYAVQTLKaKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd20014 77 VALAIRDVVEQAKVPLIVANAGANALTrAACSPYIFRTSFSNWQLGYALGKYAAENVG-KTVVTIASDYAAGREVVAGFK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVD-DKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISAT--LMGAGGFVSQTFLQl 267
Cdd:cd20014 156 EGFEAAGGKVVGEIWTPlGTTTDFSPYLTQIAASGPDAVYAFFAGADAVRFVKQYAEFGLKGKipLYGPGFLTDEDVLP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 268 AQKE-GNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKA--DSVDPAVYLPVLRAISYS 344
Cdd:cd20014 235 ALGEaAEGIITVLHYAPTLDNPANRAFVAAYQAKYGRLPDVYAVQGYDAAQVIDAALEAVggDTSDKDILAAALELGSID 314
|
330 340 350
....*....|....*....|....*....|
gi 2294035498 345 GVTGQIAFDKEGNlkSPTFTVY--KVVDGK 372
Cdd:cd20014 315 SPRGPFRFDPTTH--NPIQNIYlrEVVKGG 342
|
|
| PBP1_ABC_ligand_binding-like |
cd06326 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
31-276 |
2.38e-26 |
|
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however.
Pssm-ID: 380549 [Multi-domain] Cd Length: 339 Bit Score: 107.63 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 31 VTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVD-SGVAGVVGHWN 109
Cdd:cd06326 1 IVIGQSAPLSGPLAELGREYLAGAKAYFDQVNAAG-GINGRKI--RLVTLDDGYDPARTVENTRQLIEqDKVVALFGYVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVM-GHDDDGGQFAGQyaVQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06326 78 TANVEAVLPLLEEAGVPLVGPLTGADSLREPGNPYVFHVRaSYADEVEKIVRH--LATLGLKRIAVVYQDDPFGKEGLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLA 268
Cdd:cd06326 156 AEAALAARGLEPVATAAVARNAADVAAAAAALAAAKPQAVVLIAAGKAAAAFIKALRAAGGAAQFYGLSVVGAAALAKAL 235
|
....*...
gi 2294035498 269 QKEGNGVV 276
Cdd:cd06326 236 GDAARGVV 243
|
|
| PBP1_SBP-like |
cd19989 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
32-320 |
4.96e-26 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380644 [Multi-domain] Cd Length: 299 Bit Score: 106.21 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQhPTIGGKAVTFKlqSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd19989 1 KIGVLTPLSGPYAALGEEARRGAQLAVEEINAA-GGILGRPVELV--VEDTEGKPATAVQKARKLVeQDGVDFLTGAVSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVATGHAYT-KQGFDTSFRVmGHDDDGGQFAGQYAVQTLKAKRIAVIDDRTAFGQGLADEF 189
Cdd:cd19989 78 AVALAVAPKAAELKVPYLVTVAADDELTgENCNRYTFRV-NTSDRMIARALAPWLAENGGKKWYIVYADYAWGQSSAEAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 190 IKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGG---FVSQTFLQ 266
Cdd:cd19989 157 KEAIEELGGEVVGTLFAPLGTTDFSSYITQISDSGADGLLLALAGSDAVNFLKQAGQFGLGKKYKIVGGilsIEPLALPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2294035498 267 LAQK-EG-NGVVALEPGLPVEQMpggKAFEQAYQSRYHTHIELHAPFAYDATRVLA 320
Cdd:cd19989 237 LGDAaEGvYGGVRYPPTLDTPAN---RAFVEAYEKEYGEAPDNFAGEAYEAMQALA 289
|
|
| PBP1_ABC_ligand_binding-like |
cd19978 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
31-328 |
5.84e-26 |
|
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in the uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however.
Pssm-ID: 380633 [Multi-domain] Cd Length: 341 Bit Score: 106.89 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 31 VTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPtIGGKavTFKLQSEDDQSDPRTAVAVAQRLVDS----GVAGVVG 106
Cdd:cd19978 1 IRLGMSAALSGPAAELGNEMKRGIEAAFNEVNAQGG-VNGR--KIKLIALDDGYEPDRTVKNTKKLIEEdkvfALIGYVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 107 hwnTGTSIPAARVYHDAGIAQVAPvATGHAYTKQGFDTS-FRVMGHDDDGGQFAGQYAVQTLKAKRIAVI--DDrtAFGQ 183
Cdd:cd19978 78 ---TPTALAALPLANEKKIPLFGP-FTGAEFLRTPFLPYvFNLRASYADETEALVDYLVKTLGPKRIAIFyqND--AFGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 184 GLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMgAGGFV-SQ 262
Cdd:cd19978 152 AGLEGAKKALKKRGLTPVAEGSYTRNTLDVEEALAKILKAKPEAIILVGTYAPAAEFIRLARAAGLNPLFA-NVSFVgSE 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 263 TFLQLAQKEGNGVVALE--PGLPVEQMPGGKAFEQAYQsRYHTHIEL-HAPF-AYDATRVLAAAMEKADS 328
Cdd:cd19978 231 ALALELGDYGEGVIVSQvvPDPNDSSLPIVKEYREAMK-KYGPNAPPdFVSLeGYLAARLLVEALKKAGP 299
|
|
| PBP1_Nba-like |
cd06359 |
type 1 periplasmic binding component of active transport systems predicted to be involved in ... |
33-354 |
2.57e-23 |
|
type 1 periplasmic binding component of active transport systems predicted to be involved in 2-nitrobenzoic acid degradation pathway; This group includes the type 1 periplasmic binding component of active transport systems that are predicted to be involved in 2-nitrobenzoic acid degradation pathway; their substrate specificities are not well characterized.
Pssm-ID: 380582 [Multi-domain] Cd Length: 333 Bit Score: 99.25 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNTG 111
Cdd:cd06359 2 IGFITTLSGPAAVLGQDMRDGFNLALEQLGGK---LGGLPV--EVVVEDDQLKPDVAKQAAERLIERdKVDFVTGIIFSN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTSFRVMG-HDDDGGQFAGQYAvQTLKAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06359 77 VMLAVVKPVVDSKVFYISANAGPSDLAGKGCNPNFFVTSwQNDQLHEAAGKYA-NDKGYKRVYLLAPNYQAGKDALAGFK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQgidIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISAT--LMGAgGFVSQTFLQLA 268
Cdd:cd06359 156 RTYKGE---VVGEIYTPLGQLDFSAELAQIRAAKPDAVFAFYPGGMGVNFVKQYAQAGLKKKipLYTV-GTLDDEDLLPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 269 QKEG----NGVVALEPGLPVeqmPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKA--DSVDPAVYLPVLRAIS 342
Cdd:cd06359 232 MGDAalgvLSVSQWSPDLDN---PENKRFVAAFRKKYGRPPSNYAAQGYDAALLIDAAVKAVggDLSDKDALRAALRKAD 308
|
330
....*....|..
gi 2294035498 343 YSGVTGQIAFDK 354
Cdd:cd06359 309 FKSVRGAFRFNN 320
|
|
| PBP1_ABC_transporter_GPCR_C-like |
cd04509 |
Family C of G-protein coupled receptors and their close homologs, the type 1 ... |
32-280 |
1.70e-21 |
|
Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.
Pssm-ID: 380490 Cd Length: 306 Bit Score: 93.52 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTG--PSARIGKDL--ENGAQ------LAIDDINKQHPTIggKAVTFKLQSEDDQSDPRTAVAVAQRLVDS-- 99
Cdd:cd04509 1 KVGVLFAVHGkgPSGVPCGDIvaQYGIQrfeameQALDDINADPNLL--PNNTLGIVIYDDCCDPKQALEQSNKFVNDli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 100 ---------------------GVAGVVGHWNTGTSIPAARVYHDAGIAQVAPVATGHAYT-KQGFDTSFRVMGHDDDGGQ 157
Cdd:cd04509 79 qkdtsdvrctngeppvfvkpeGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSdDRGYQLFLRVVPLDSDQAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 158 FAGQYaVQTLKAKRIAVIDDRTAFGQGLADEFIKSLKAQGIDIV--DRQYVDDKTVDFSAVLTAIRSKN-ADLIFFGGVD 234
Cdd:cd04509 159 AMADI-VKEKVWQYVSIVHDEGQYGEGGARAFQDGLKKGGLCIAfsDGITAGEKTKDFDRLVARLKKENnIRFVVYFGYH 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2294035498 235 SQAAPLARRIKQMGISA--TLMGAGGFVSQTF-LQLAQKEGNGVVALEP 280
Cdd:cd04509 238 PEMGQILRAARRAGLVGkfQFMGSDGWANVSLsLNIAEESAEGLITIKP 286
|
|
| PBP1_YraM_LppC_lipoprotein-like |
cd06339 |
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ... |
32-356 |
1.75e-21 |
|
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).
Pssm-ID: 380562 [Multi-domain] Cd Length: 331 Bit Score: 93.87 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIggkavTFKlqsedDQSDPRTAVAVAQRLVDSGVAGVVGHWNTG 111
Cdd:cd06339 1 RIALLLPLSGPYAAAGQAIRDGIELALFDAGGSRPEL-----RVY-----DTGGPEGAAAAYQQAVAEGADLIIGPLLKS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFdtsFRvMGHD-DDGGQFAGQYAVQTLKaKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06339 71 SVAALAAAAQALGVPVLALNNDESATAGPGL---FQ-FGLSpEDEARQAARYAVQQGL-RRFAVLAPDNAYGQRVANAFR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAI----------------------RSKNADLIFFGGVDSQAAPLARRIKQMG 248
Cdd:cd06339 146 EAWQALGGTVVAVESYDPDETDFSAAIRRLlgvdqsearirqlgellefeprRRQDFDAIFLPAGPEQARLIAPQLAFYG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 249 IS-ATLMGAGGFVSQTFLQLAQKEGNGVVALEPglPVeqMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKAD 327
Cdd:cd06339 226 AGdVPLLGTSLWYSGKLNLLRDPDLNGAWFADP--PW--LLSPRAFPLRYRLAYGWPPPRLAALGYDAYRLAARLARLGG 301
|
330 340
....*....|....*....|....*....
gi 2294035498 328 SVDPAVYlpvlraisYSGVTGQIAFDKEG 356
Cdd:cd06339 302 GLTPGAG--------FSGLTGLLRLDPDG 322
|
|
| PBP1_SBP-like |
cd20378 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
32-348 |
2.91e-21 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380668 [Multi-domain] Cd Length: 357 Bit Score: 93.95 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDdinkQHPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWNT 110
Cdd:cd20378 1 TLGGLVSMSGAFAAAGKLADRGMRLAVE----EYGGALGRPL--KYITRDTEGKPGTGVRKVQEAIAQdGARFFIGGTLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIAQVAPVA----TGHAYTKQGFDTSFRVMGhdddggqfAGQYAVQTL-----KAKRIAVIDDRTAF 181
Cdd:cd20378 75 SVALAVSEEAEKAGGVYITSGGadeiTGSRCNRSTFRWSVPTYG--------AIRQTVRPVikampKAKRWYTITPQYVF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 182 GQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGIS--ATLMGAGGF 259
Cdd:cd20378 147 GESLLKNAKEVLKEKGIEHVGNSYHSLGEREFSGYLTKAMAARPDVLLILNFGSQAVDALRQAVSFGLKrkMKILVAWSS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 260 VSQTFLQLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYLPVLR 339
Cdd:cd20378 227 GLDQFQELGPDICEGVYFGAQYWHDVDTPANKALVKVYQAKFKETPSYALAAGYACTRMLLDAIDKAGSTDPAAVIKALE 306
|
....*....
gi 2294035498 340 AISYSGVTG 348
Cdd:cd20378 307 GLKYDGITG 315
|
|
| ANF_receptor |
pfam01094 |
Receptor family ligand binding region; This family includes extracellular ligand binding ... |
51-370 |
3.02e-21 |
|
Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.
Pssm-ID: 460062 [Multi-domain] Cd Length: 347 Bit Score: 93.60 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 51 ENGAQLAIDDINKQHPTIGGkaVTFKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVGHWNTGTSIPAARVYHDAGIAQVAP 130
Cdd:pfam01094 3 LLAVRLAVEDINADPGLLPG--TKLEYIILDTCCDPSLALAAALDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 131 VATGHAYT-KQGFDTSFRVMGHDDDGGQFAGQyAVQTLKAKRIAVIDDRTAFGQGLADEFIKSLKAQGIDIVDRQYVDdK 209
Cdd:pfam01094 81 GSTSPALSdLNRYPTFLRTTPSDTSQADAIVD-ILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIP-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 210 TVDFSAVLTAIRSKNAD-----LIFFGGVDSQAA-PLARRIKQMGISATLMGAGGFVSQ--TFLQLAQKEGNGVVALEPg 281
Cdd:pfam01094 159 AQDDDEIARKLLKEVKSrarviVVCCSSETARRLlKAARELGMMGEGYVWIATDGLTTSlvILNPSTLEAAGGVLGFRL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 282 lpveQMPGGKAFEQAYQSRYHTHIEL----------HAPFAYDATRVLAAAMEKADSVDPAVY--------------LPV 337
Cdd:pfam01094 238 ----HPPDSPEFSEFFWEKLSDEKELyenlgglpvsYGALAYDAVYLLAHALHNLLRDDKPGRacgalgpwnggqklLRY 313
|
330 340 350
....*....|....*....|....*....|...
gi 2294035498 338 LRAISYSGVTGQIAFDKEGNLKSPTFTVYKVVD 370
Cdd:pfam01094 314 LKNVNFTGLTGNVQFDENGDRINPDYDILNLNG 346
|
|
| PBP1_AmiC |
cd06357 |
periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding ... |
33-357 |
1.02e-20 |
|
periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family; This group includes the periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family. AmiC controls expression of the amidase operon by the ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon are induced.
Pssm-ID: 380580 [Multi-domain] Cd Length: 357 Bit Score: 92.26 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKqHPTIGGKavTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGhwnTG 111
Cdd:cd06357 2 VGLLFSQTGVTAIIEQSMLNGALLAIEEINA-AGGVNGR--PIEPVVYDPASDPDRYRELAERLLlEDGVRHIFG---CY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSipAARVyhdagiaQVAPVATGH----AYTKQ--GFDTSFRVMGhdddGGQFAGQYAVQTLK------AKRIAVIDDRT 179
Cdd:cd06357 76 TS--ASRK-------AVLPVVERHnallWYPTPyeGFEYSPNVIY----TGAVPNQHLLPLARyllahfGKRVFLVGSNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 180 AFGQ---GLADEFIKslkAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLM-- 254
Cdd:cd06357 143 VYPWesnRVARELIE---ASGGEVVGERYVPLGDTDFAEIIEEIKSLKPDVVFSTLVGDSIYAFYRAYAEAGLDPADMpi 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 255 -----------------GAGGFVSQTFLQLAQKEGNgvvalepglpveqmpggKAFEQAYQSRYHTHIELHAPF--AYDA 315
Cdd:cd06357 220 aslttseaevaaigaeaAAGHYTSAPYFQSIDTPEN-----------------RAFVEAYRARFGDDAVTSAVAeaAYFQ 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2294035498 316 TRVLAAAMEKADSVDPAVYLPVLRAISYSGVTGQIAFDKEGN 357
Cdd:cd06357 283 VHLLARAIERAGSDDPEAIRAALYGQEFDAPQGPVRIDPDNN 324
|
|
| PBP1_ABC_ligand_binding-like |
cd19979 |
amino acid amide ABC transporter substrate binding protein haat family; This subgroup includes ... |
33-333 |
2.28e-20 |
|
amino acid amide ABC transporter substrate binding protein haat family; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380634 [Multi-domain] Cd Length: 350 Bit Score: 91.13 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGKavtFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNTG 111
Cdd:cd19979 2 IGLDADLSGGSAASGEAIKRGIQLAIDEINAAGGLLGRK---LELVAKDHRGNPARGVDNLREFAaDPDVLAVFGGLHSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDTS--FRVMGHDDDGGQFAGQYAVQTlKAKRIAVIDDRTAFGQGLADEF 189
Cdd:cd19979 79 VLLAELDFIHELKIPYLVPWAAATPITRNGYSPNyiFRLSVDDSLAGPFLVEYALKK-GCKRPALLLENTGWGRSNLKAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 190 IKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLAq 269
Cdd:cd19979 158 TKALAKKGLQPVGVEWFNWGDTDAKPQLRALKAAGADAILLVANAPEGAAIVKALAALPERLPIISHWGITGGDFPELP- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2294035498 270 KEGNGVVALE-----PGLPVEQMPGGKAFEQAYQSRY---HTHIELHAPF----AYDATRVLAAAMEKADSVDPAV 333
Cdd:cd19979 237 REALSKIDLRfiqtfSFFDANQSPRGKQVLARYKRRYpveDPESDIPAPVgfahAYDLTHLLALAIEQAGSTDRAA 312
|
|
| PBP1_ABC_ligand_binding-like |
cd06341 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
32-296 |
3.58e-18 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380564 [Multi-domain] Cd Length: 340 Bit Score: 84.67 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINkQHPTIGGKAVTfkLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHwNT 110
Cdd:cd06341 1 KIGLIYPDTGPGAASFSAARAGAEARFGLAN-AAGGINGRKVE--YVWCDDQSDPATNLQAARQLVEDeKVFALVGS-SS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAGIaqvaPVATGHAYTKQGFDTSFRVMGHDDDGG--QFAGQYAVQTLKAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06341 77 AASGSANDYLAQAGI----PVVGGAGVSVWCFRNMFSNFFSLGGGGstTTYGQYAAALGGTKAAVVVTDIPAASQQLAQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQLA 268
Cdd:cd06341 153 LAASLRAAGVEVVGTAPYAAAAPDYTAVAQAAKAAGADAVVGVLDPDVAARVLKAARAQGLDLKVALSPSGYDPSVLAAY 232
|
250 260
....*....|....*....|....*....
gi 2294035498 269 QKEGNGVVALEPGLPVE-QMPGGKAFEQA 296
Cdd:cd06341 233 GAALAGVSVASTFLPFEaDTPAVKAYRAA 261
|
|
| PBP1_SBP-like |
cd06328 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
33-355 |
3.86e-18 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in gram-negative and gram-positive bacteria. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380551 [Multi-domain] Cd Length: 336 Bit Score: 84.66 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNTG 111
Cdd:cd06328 2 IGVITSLTGPLAAYGKQTERGFELGLEYATDGTMEVDGRKI--EVIVKDDQGDPDTAKAAATELIgDDGVDILVGTVSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 112 TSIPAARVYHDAGIAQVAPVATGHAYTKQGFDT-SFRVMGHDDDGGQFAGQYAVQTLkAKRIAVIDDRTAFGQGLADEFI 190
Cdd:cd06328 80 VALALAPVAEQNKKILIVGPAAADSITGENWNKyTFRTSRNSWQDAIAGAKALADPL-GKSVAFLAQDYAFGQDGVAAFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 191 KSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGI-SATLMGAGGFVSQTFLQL-- 267
Cdd:cd06328 159 KALEAKGGKIVGEELVPVTTTDFTPYLQRILDAKPDVLFVAWAGTGALTLWQQLADQGVlDDIKVVTGGPDIATLAALgd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 268 AQKEGNGVVALEPGLPveQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPAVYL-PVLRAISYSGV 346
Cdd:cd06328 239 ALPGIEGLTYYYYGLP--KNPVNDWLVKAHKERYNAPPDLFTAGGFAAAQAVVRALEKAGGDTDVEKLiAALEGLTFETP 316
|
....*....
gi 2294035498 347 TGQIAFDKE 355
Cdd:cd06328 317 KGKMTIRAE 325
|
|
| PBP1_SBP-like |
cd06329 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
33-355 |
2.52e-17 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380552 [Multi-domain] Cd Length: 343 Bit Score: 82.32 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptIGGKAVTFKLQSEDDQSDPRTAVAVAQRLVDSG---VAGVVGHWN 109
Cdd:cd06329 2 IAFIDPLSGPFASVGEIYLKGLQFAIEEINAG---GGLLGRKIELVPFDNKGSPQEALIQLKKAIDQGirfVLQGNSSAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYH----DAGI-----AQVAPVATG---HAYtkqgfdtSFRVMGHDDDGGQFAGQYAVQTLKAKRIAVIDD 177
Cdd:cd06329 79 AGALIDAIEKHNqrnpDKRVlflnyGAEAPELTGakcSFW-------HFRFDANADMKMAALADYMKKDGSIKKVYLINQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 178 RTAFGQGLADEFIKSLKAQGIDIvdrQYVDD------KTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISA 251
Cdd:cd06329 152 DYSFGRDVAAAAKKNLKKKRPDI---EIVGEdlhplgKVKDFSPYIAKIKASGADTVITGNWGNDLTLLMKAARDSGLKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 252 TLMGAGGFVSQTFLQLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDP 331
Cdd:cd06329 229 PFYTYYADGPGAPAAIGEAGVGRLVAVAYWHPNPKTPELEKFAEAFRAKYGRYPDFNIGRTYMGVEMLAAAIKKAGSTDP 308
|
330 340
....*....|....*....|....
gi 2294035498 332 AVYLPVLRAISYSGVTGQIAFDKE 355
Cdd:cd06329 309 EKVAKALEGLSFDTPGGPVTMRAD 332
|
|
| PBP1_SBP-like |
cd19987 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
32-332 |
2.61e-17 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380642 [Multi-domain] Cd Length: 353 Bit Score: 82.38 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGKAV---------TFKLQSEDDQSDPRTAVAVAQRLV-DSGV 101
Cdd:cd19987 1 TIGLNVPLSGPYAPQGEDQRRGFELAVDHLNNGGGLVDKDSRlsgdgilgkKVELVTADTETKADTAVDNAKRLIeQDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 102 AGVVGHWNTGTSIPAARVYHDAGIAQVAPVATGHAYT-KQGFDTSFRVMGHDDDGGQFAGQYAVQTL-KAKRIAVIDDRT 179
Cdd:cd19987 81 VMITGGSSSAVAVAAQKLAQKEGVLYFAGLSHSNDTTgKDCHRYGFRECFNAHMSAKALAPYLVEKFgKDRKYFYLTADY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 180 AFGQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISATLMGAGGF 259
Cdd:cd19987 161 TWGHSTEQSMREYTEAHGWKTVGNPATPLGETDFSAALLNAADSGADVLVLVLFGRDMVNALKQAKQFGLLKKMDIVVPL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2294035498 260 VSQTFLQLAQKEG-NGVVALE---PGLPVEqMPGGKAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPA 332
Cdd:cd19987 241 LTAFMAESVGPEImEGVLGTVnwhWSLPDD-YSYAFGKAEAFEKEYGAYPSQAAASAYVQVLQYAAAVERAGSFDPP 316
|
|
| PBP1_ABC_ligand_binding-like |
cd06334 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
32-375 |
1.36e-16 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380557 [Multi-domain] Cd Length: 360 Bit Score: 80.36 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptiGGKA-VTFKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGhWN 109
Cdd:cd06334 1 KIGLLTDLTGPTADVGKPYAQGVRDYLNYVNEE----GGINgVKIELEECDTGYKVPRAVACYKRLKAQdGVVAILG-WG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTS-----------IPAARVYHDAGIAQVAPVatghaytkqgFDTSFRVMGHDDDGGQFAGQYAVQ----TLKAKRIAV 174
Cdd:cd06334 76 TGDTealaprvakdkIPYISASYGRSLADDGKV----------FPYNFFVGATYSSQARALLKYIAQewggKLKGPKVAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 175 IDDRTAFGQgladEFIKSLKAQ----GIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGIS 250
Cdd:cd06334 146 VYHDSPFGR----EPIPALKAYakelGFEVVAEQVPSPGALDATAQWLRIRRAGPDYVIIQGTGGSVAVIIKDAKRLGLK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 251 ATLMGAGGFVSQTFLQLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRYHTHI-ELHAPFAYD----ATRVLAAAMEK 325
Cdd:cd06334 222 TKFIGNIWGGDEDLIKLAGDAAEGYVGVSPFAFGTDDPPGKEIVEEVAKKGKGDGpEEVGTVYYNrgwaTAMLAVEAIRR 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2294035498 326 ADSVDPAVYLPV--------LRAISYSGVTGQIAFDKEGNLKSPTFTVYKVVDGKWQP 375
Cdd:cd06334 302 ADKAGGGTGLGNklkaglerLKDFDLGGLAPPVTFTPTDHRGGGVVRIYQWDGGKWVP 359
|
|
| PBP1_GABAb_receptor |
cd06366 |
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ... |
32-362 |
1.47e-12 |
|
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.
Pssm-ID: 380589 [Multi-domain] Cd Length: 404 Bit Score: 68.43 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSAR-IGKDLENGAQLAIDDINkQHPTIGgKAVTFKLQSEDDQSDPRTAVAVAQRLVDSG---------- 100
Cdd:cd06366 1 YIGGLFPLSGSKGWwGGAGILPAAEMALEHIN-NRSDIL-PGYNLELIWNDTQCDPGLGLKALYDLLYTPppkvmllgpg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 101 -------VAGVVGHWNtgtsipaarvyhdagIAQVApVATGHAY--TKQGFDTSFRVMGHDDDggqfagQYA--VQTLKA 169
Cdd:cd06366 79 cssvtepVAEASKYWN---------------LVQLS-YAATSPAlsDRKRYPYFFRTVPSDTA------FNParIALLKH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 170 ---KRIAVIDDRTAFGQGLADEFIKSLKAQGIDIVDRQYVddKTVDFSAVLTAIRSKNADlIFFGGVDsqaAPLARRI-- 244
Cdd:cd06366 137 fgwKRVATIYQNDEVFSSTAEDLEELLEEANITIVATESF--SSEDPTDQLENLKEKDAR-IIIGLFY---EDAARKVfc 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 245 ------------------------------------KQMgisatLMGAGGFVSQTFLQLAQKEGNGVvalePGLPVEQmp 288
Cdd:cd06366 211 eayklgmygpkyvwilpgwyddnwwdvpdndvnctpEQM-----LEALEGHFSTELLPLNPDNTKTI----SGLTAQE-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 289 ggkaFEQAYQSR---YHTHIELHAPFAYDATRVLAAAMEKA-----------------DSVDPAVYLPVLRAISYSGVTG 348
Cdd:cd06366 280 ----FLKEYLERlsnSNYTGSPYAPFAYDAVWAIALALNKTieklaeynktledftynDKEMADLFLEAMNSTSFEGVSG 355
|
410
....*....|....
gi 2294035498 349 QIAFDKEGNLKSPT 362
Cdd:cd06366 356 PVSFDSKGDRLGTV 369
|
|
| PBP1_FmdD-like |
cd06355 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
33-357 |
1.16e-11 |
|
periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF); This group includes the periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF), found in Methylophilus methylotrophus, and its homologs from other bacteria. FmdD, a type 1 periplasmic binding protein, is induced by short-chain amides and urea and repressed by excess ammonia, while FmdE and FmdF are hydrophobic transmembrane proteins. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems.
Pssm-ID: 380578 [Multi-domain] Cd Length: 347 Bit Score: 65.29 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQhptiGG------KAVTfklqsEDDQSDPRTAVAVAQRLVDS-GVAGVV 105
Cdd:cd06355 2 VGILHSLSGTMAISERPLVDATLLAIDEINAA----GGllgrkiEPVI-----EDGASDWPTFAEKAEKLITQdKVAVIF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 106 GHWntgTSipAARvyhdagiAQVAPVATGH------AYTKQGFDTSFRVMGhddDGG------QFAGQYAVQTLkAKRIA 173
Cdd:cd06355 73 GCW---TS--ASR-------KAVLPVIEKYngllfyPVQYEGLEQSPNIVY---TGAtpnqqiLPAIDWLLENL-GKRFF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 174 VIDDRTAFGQgLADEFIKS-LKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGISAT 252
Cdd:cd06355 137 LVGSDYVFPR-TANKIIRDqLKALGGEVVGEEYVPLGGTDFDAIVAKIKAFKPDVIVNTLNGDSNIAFFKQLAAAGITAS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 253 ---LMGaggfVSQTFLQLAQKEGNGVV---ALEPGLPVEQMPGGKAFEQAYQSRYHTHIELHAPF--AYDATRVLAAAME 324
Cdd:cd06355 216 dlpVLS----FSVSEAELRAIGPEELAghyAAWNYFQSLDTPENQAFVEAFKAKYGADRVTSDPMeaAYLGVYLWAQAVE 291
|
330 340 350
....*....|....*....|....*....|...
gi 2294035498 325 KADSVDPAVYLPVLRAISYSGVTGQIAFDKEGN 357
Cdd:cd06355 292 KAGSFDPDAVRAALKGQSFEAPGGTVTVDPENH 324
|
|
| PBP1_ABC_ligand_binding-like |
cd06337 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
32-357 |
4.35e-11 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380560 [Multi-domain] Cd Length: 354 Bit Score: 63.47 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGKAVTFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWNT 110
Cdd:cd06337 1 KIGRVSPLTGPLAAFGEADPWVLEQIREAFADGGIKVGGKKYPVEIVVRDSQSDPNRAGEAARDLIlRDKVDLMLASGTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARVYHDAG------IAQVAPVATGHAYT-KQGFDTSFRV-MGHDDDGGQFAGQY-AVQTlkAKRIAVIDDRTAF 181
Cdd:cd06337 81 DTVNPVADQCEANGvpcistDAPWQAWFFGRGGDpAKGFKWTFHFfWGLEDIAANFLGMWdQVPT--NKVVGLLWPNDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 182 GQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGIS---ATLMGAGG 258
Cdd:cd06337 159 GTAFADAFLGLPAAAGYTLVDPGRFPPGTDDFSSIINAFKKAGVEIVTGVMIPPDFATFWRQAAQQGFKpkvVTIGKALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 259 FVSQtfLQLAQKEGNGV---VALEPGLPVEQMPGG---KAFEQAYQSRYHTHIELHAPFAYDATRVLAAAMEKADSVDPA 332
Cdd:cd06337 239 FPSA--VAALGDLGDGLsteVWWSPAHPFKSSLTGqtaAELADAYEKATGKQWTQPLGYAHALFEVAVDALKRAGSPDDE 316
|
330 340
....*....|....*....|....*
gi 2294035498 333 VYLPVLRAISYSGVTGQIAFDKEGN 357
Cdd:cd06337 317 AVRAALADTDLDTIVGPVDFTSGPV 341
|
|
| PBP1_RPA0985_benzoate-like |
cd20013 |
type 1 periplasmic binding-protein component of an ABC system (RPA0985), involved in the ... |
33-374 |
1.69e-10 |
|
type 1 periplasmic binding-protein component of an ABC system (RPA0985), involved in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0985 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0985 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).
Pssm-ID: 380666 [Multi-domain] Cd Length: 356 Bit Score: 61.89 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIddinKQH-PTIGGKAVTFKLQseDDQ-SDPRTAVAVAQRL-VDSGVAGVVGHWN 109
Cdd:cd20013 2 VGVIGPFSGPFADYGKQFDRGIDLYL----KLHgDKVGGRKVEVIYR--DDGgPNPAVAKRLAQELiVRDKVQILIGFGF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGIAQVAPVATGHAYTKQG---FDTSFRVMGHDDDGGQFAGQyavQTLKAKRIAVIDdrTAFGQGLA 186
Cdd:cd20013 76 TPNALAVAPVATEAKTPTVIMNAATSSITRKSpyfVRTSFTMWQVAYPMGKWAAK---NGIKKAYTAVAD--YAPGHDAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 187 DEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFF---GGVDSQA---APLARRIKQMGIsaTLMGAGGFV 260
Cdd:cd20013 151 TAFKKAFEAAGGKIVGSIRVPLATPDFAPFMQRIKDAKPDAVFVfvpAGAPSIGflkAYAERGLKEAGI--KLLGTGDAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 261 SQTFLQLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRY--HTHIELHAPFAYDATRVLAAAMEK-ADSVDPAVYLPV 337
Cdd:cd20013 229 DDDDLPAMGDAALGLITAGHYSAALDSPENKAFVAAYQKAYgpDARPDFMAVAAYDGMALIYKMIKAtGGKFDGDKAMAA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2294035498 338 LRAISYSGVTGQIAFDKEGnlKSPTFTVY----KVVDGKWQ 374
Cdd:cd20013 309 VKGLKWESPRGPISIDPET--RDIVQNVYirrvEKVDGKLQ 347
|
|
| Peripla_BP_5 |
pfam13433 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
31-355 |
5.14e-09 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins.
Pssm-ID: 463875 [Multi-domain] Cd Length: 363 Bit Score: 57.22 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 31 VTIGLAGPLTGPSARIGKDLENGAQLAIDDINKQHPTIGGK--AVTfklqsEDDQSDPRTAVAVAQRLV-DSGVAGVVGH 107
Cdd:pfam13433 1 IKVGVLHSLTGTMAISERSLKDATLMAIEEINAAGGVLGRKiePVV-----VDPASDWPLFAEKARKLIdQDKVRVVFGC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 108 WntgTSipAARvyhdagiAQVAPVATGHA----YTKQ--GFDTSFRVMGhdddGGQFAGQYAVQTLK------AKRIAVI 175
Cdd:pfam13433 76 W---TS--ASR-------KAVLPVFERHNgllfYPVQyeGFESSRNIFY----TGAAPNQQAIPAVDyllselGKRFFLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 176 DD-----RTAfGQGLADEfiksLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFFGGVDSQAAPLARRIKQMGIS 250
Cdd:pfam13433 140 GSdyvypRTT-NRILRAY----LKAKGGEVVGERYLPLGSSDWQSIVAKIKAAGPDVVFSTINGDSNVAFYRALRAAGIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 251 ATLMGAGGF-VSQTFLQlaqkegngvvALEPGLPVEQM-----------PGGKAFEQAYQSRYHTHIELHAPF--AYDAT 316
Cdd:pfam13433 215 AEDIPVMSFsVAEEELA----------GMGPEPLVGHLaawnyfqsldtPENKAFVAAFKARYGDDRVTNDPMeaAYIGV 284
|
330 340 350
....*....|....*....|....*....|....*....
gi 2294035498 317 RVLAAAMEKADSVDPAVYLPVLRAISYSGVTGQIAFDKE 355
Cdd:pfam13433 285 HLWAQAVEKAGTDDPDAVRQAMLGQEFDAPQGPVKIDPE 323
|
|
| PBP1_amide_urea_BP-like |
cd06356 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
39-353 |
5.56e-09 |
|
periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF); This group includes the type 1 periplasmic-binding proteins that are predicted to have a function similar to that of an active transport system for short chain amides and/or urea in bacteria and Archaea, by sequence comparison and phylogenetic analysis.
Pssm-ID: 380579 [Multi-domain] Cd Length: 334 Bit Score: 56.93 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 39 LTGPSARIGKDLENGAQLAIDDINKQHPTIGGKavtFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGHWnTGTSIPAA 117
Cdd:cd06356 8 LSGGLNIYGKPMVHAMKLAVEEINAAGGLLGRQ---IELVAYDTQSDMQKYTQYAQQLIlRDKVDVVFGGI-TSASREAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 118 R-VYHDAGIAQVAPVA-TGHAYTKQGFDTsfrvmghdddgGQFAGQ-------YAVQTLkAKRIAVIDDRTAFGQGLADE 188
Cdd:cd06356 84 RpILRRNKILYFYNTQyEGGVCDKNTFCT-----------GSTPEQqvsplieWAIKKY-GKKVYIIAADYNFGQISADW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 189 FIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLI---FFGGVDSQ------AAPLarrIKQMGISATLMGAGGF 259
Cdd:cd06356 152 VKKYAKKNGGEVVGEEFFPLDVTDFGPTIQKIQAAKPDFVvslLVGGNHISfyrqwaAAGL---KKKIPIVSTVFGAGNE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 260 vsqtFLQLAQKEGNGVVALEPGLPVEQMPGGKAFEQAYQSRY--HTHIELHAPFAYDATRVLAAAMEKADSVDPAvylPV 337
Cdd:cd06356 229 ----HKVLSPPELEGMYVSYSYFEELDTPANKAFVAKWRAKYgdEPYINQEAVGVYNAVYLWAEAVEKAGSTERE---AV 301
|
330 340
....*....|....*....|
gi 2294035498 338 LRA----ISYSGVTGQIAFD 353
Cdd:cd06356 302 IAAlesgISFDGPSGTVTVD 321
|
|
| PBP1_GABAb_receptor_plant |
cd19990 |
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ... |
43-373 |
2.10e-08 |
|
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close homologs in other plants; This group includes the ligand-binding domain of Arabidopsis thaliana glutamate receptors, which have sequence similarity with animal ionotropic glutamate receptor and its close homologs in other plants. The ligand-binding domain of GABAb receptors are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.
Pssm-ID: 380645 [Multi-domain] Cd Length: 373 Bit Score: 55.31 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 43 SARIGKDLENGAQLAIDDINKQHPTIGGKavtFKLQSEDDQSDPRTAVAVAQRLV-DSGVAGVVGhwnTGTSIPAARVYH 121
Cdd:cd19990 9 NSRVGKEAKVAIEMAVSDFNSDSSSYGTK---LVLHVRDSKGDPLQAASAALDLIkNKKVEAIIG---PQTSEEASFVAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 122 DAGIAQV------APVATGHAYTKQGFdtsFRvMGHDDDGgQFAGQYA-VQTLKAKRIAVIDDRTAFGQGLADEFIKSLK 194
Cdd:cd19990 83 LGNKAQVpiisfsATSPTLSSLRWPFF---IR-MTHNDSS-QMKAIAAiVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 195 AQGIDIVDR----QYVDDKTVdfSAVLTAIRSKNADlIFfggVDSQAAPLARRI----KQMG---------ISATLMGAG 257
Cdd:cd19990 158 EVGSRIEYRvalpPSSPEDSI--EEELIKLKSMQSR-VF---VVHMSSLLASRLfqeaKKLGmmekgyvwiVTDGITNLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 258 GFVSQTFLQLAQkegnGVVALEPGLPVEQMPggKAFEQAYQSRYH---THIELHAP-----FAYDATRVLAAAMEKADSV 329
Cdd:cd19990 232 DSLDSSTISSMQ----GVIGIKTYIPESSEF--QDFKARFRKKFRseyPEEENAEPniyalRAYDAIWALAHAVEKLNSS 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2294035498 330 DPAVYLPV-----LRAISYS---GVTGQIAFDKEGNLKSPTFTVYKVVDGKW 373
Cdd:cd19990 306 GGNISVSDsgkklLEEILSTkfkGLSGEVQFVDGQLAPPPAFEIVNVIGKGY 357
|
|
| PBP1_NPR_GC-like |
cd06352 |
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ... |
32-379 |
2.02e-07 |
|
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.
Pssm-ID: 380575 [Multi-domain] Cd Length: 391 Bit Score: 52.36 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGPSARIGKDLENGA-QLAIDDINKQHPTIGGKAVTFKLQSEDDQSDpRTAVAVAQRLVDSGVAGVVGHWNT 110
Cdd:cd06352 1 KVGVLAPSNSQSLPVGYARSAPAiDIAIERINSEGLLLPGFNFEFTYRDSCCDES-EAVGAAADLIYKRNVDVFIGPACS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 111 GTSIPAARV--YHDAGIAQVAPVATGhAYTKQGFDTSFRVMGHDDDGGQFagqyAVQTLKA---KRIAVI-DDRTAFGQG 184
Cdd:cd06352 80 AAADAVGRLatYWNIPIITWGAVSAS-FLDKSRYPTLTRTSPNSLSLAEA----LLALLKQfnwKRAAIIySDDDSKCFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 185 LADEFIKSLKAQG---IDIVDRQYVDDkTVDFSAVLTAIRsKNADLIFFGGVDSQAAPLARRIKQMGisatlMGAGGFV- 260
Cdd:cd06352 155 IANDLEDALNQEDnltISYYEFVEVNS-DSDYSSILQEAK-KRARIIVLCFDSETVRQFMLAAHDLG-----MTNGEYVf 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 261 -----------SQTFLQLAQKEGNGVVALEPG-------LPVEQMPGGKAFEQAYQSR--------YHTHIELHAPFA-- 312
Cdd:cd06352 228 ifielfkdgfgGNSTDGWERNDGRDEDAKQAYesllvisLSRPSNPEYDNFSKEVKARakeppfycYDASEEEVSPYAaa 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2294035498 313 -YDATRVLAAAMEKADSVDPAVY-----LPVLRAISYSGVTGQIAFDKEGNlKSPTFTVYKVVDGKWQPQTVL 379
Cdd:cd06352 308 lYDAVYLYALALNETLAEGGNYRngtaiAQRMWNRTFQGITGPVTIDSNGD-RDPDYALLDLDPSTGKFVVVL 379
|
|
| PBP1_NHase |
cd06358 |
type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively ... |
33-348 |
1.20e-06 |
|
type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides; This group includes the type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides, which are subsequently converted by amidases to yield free carboxylic acids and ammonia. NHases from bacteria and fungi have been purified and characterized. In Rhodococcus sp., the nitrile hydratase operon consists of six genes encoding NHase regulator 2, NHase regulator 1, amidase, NHase alpha subunit, NHase beta subunit, and NHase activator. The operon produces a constitutive hydratase that has a broad substrate spectrum: aliphatic and aromatic nitriles, mononitriles and dinitriles, hydroxynitriles and amino-nitriles, and a constitutive amidase of equally low substrate specificity. NHases are metalloenzymes containing either cobalt or iron, and therefore can be classified into two subgroups: ferric NHases and cobalt NHases.
Pssm-ID: 380581 [Multi-domain] Cd Length: 333 Bit Score: 49.90 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 33 IGLAGPLTGPSARIGKDLENGAQLAIDDINKQHpTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVghwnTGT 112
Cdd:cd06358 2 IGLLIPLSGPAGLWGPSCEACAELAAAEINAAG-GILGREV--ELVLIDAGGPPAEVAAAARRLVDDGAVDAI----VGM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 113 SIPAARVyhdagiaQVAPVATGHA---YTKQ---GFDTSFRVMGHDDDGGQF--AGQYAVQTLKAKRIAVIDDRTAFGQG 184
Cdd:cd06358 75 HTSAVRQ-------ALANAVGGRVpyvYTPLyegGERTPGVYAIGETPEEQLrpALRWLADERRVRRWFLVGNDYVWPRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 185 LADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNAD--LIFFGGVDS-------QAAPLARRIKQMGIS---AT 252
Cdd:cd06358 148 SHAAARRYIARLGGEVVGERFVPLGEDDFERVLARIRASRPDavLISLVGQDAvdfnrafAAAGLAGRILRLSPAideNV 227
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 253 LMGAGG------FVSQTFLQLAQKEGNgvvalepglpveqmpggkafeQAYQSRYHTHIELHAP----FA---YDATRVL 319
Cdd:cd06358 228 LLAIGAdatenlYSASGYFASLRTAAN---------------------LAFLERYHAAFGDRAPplnaLGescYEGVHFL 286
|
330 340
....*....|....*....|....*....
gi 2294035498 320 AAAMEKADSVDPAVYLPVLRAISYSGVTG 348
Cdd:cd06358 287 AALARRAGSLDVRALAAAAEGLTYESPRG 315
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|
| PBP1_GPCR_family_C-like |
cd06350 |
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ... |
57-249 |
5.19e-06 |
|
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (m; Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins.
Pssm-ID: 380573 Cd Length: 350 Bit Score: 48.06 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 57 AIDDINK-----QHPTIGG----------KAVTFKLQSEDDQSDPRTAVAVAQRLVDSGVAGVVGHWNTGTSIPAARVYH 121
Cdd:cd06350 36 AIEEINNdssllPNVTLGYdirdtcssssVALESSLEFLLDNGIKLLANSNGQNIGPPNIVAVIGAASSSVSIAVANLLG 115
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 122 DAGIAQVAPVATG-HAYTKQGFDTSFRVMGHDDdggqfagQYA------VQTLKAKRIAVIDDRTAFGQGLADEFIKSLK 194
Cdd:cd06350 116 LFKIPQISYASTSpELSDKIRYPYFLRTVPSDT-------LQAkaiadlLKHFNWNYVSTVYSDDDYGRSGIEAFEREAK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2294035498 195 AQGIDIVDRQYVD--DKTVDFSAVLTAIRSK-NADLIFFGGVDSQAAPLARRIKQMGI 249
Cdd:cd06350 189 ERGICIAQTIVIPenSTEDEIKRIIDKLKSSpNAKVVVLFLTESDARELLKEAKRRNL 246
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| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
75-300 |
4.86e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 44.66 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 75 FKLQSEDDQSDPRTAVAVAQRLVDSGVAG-VVGHWNTGTSIPAARVYHDAGIaqvaPVATGHAYTKQGFDTSFrVMGHDD 153
Cdd:cd06319 30 YEFVTYDQKNSANEQVTNANDLIAQGVDGiIISPTNSSAAPTVLDLANEAKI----PVVIADIGTGGGDYVSY-IISDNY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 154 DGGQFAGQYAVQTLKAK-----RIAVID---DRTaFGQGLADEFIKSLKAQGIDIVDRQYVDDKTVD--FSAVlTAIRSK 223
Cdd:cd06319 105 DGGYQAGEYLAEALKENgwgggSVGIIAipqSRV-NGQARTAGFEDALEEAGVEEVALRQTPNSTVEetYSAA-QDLLAA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294035498 224 NADLI-FFGGVDSQAAPLARRIKQMGISATLMGAGGFVSQTFLQL-AQKEGNGVVALEpglPVEQmpGGKAFEQAYQSR 300
Cdd:cd06319 183 NPDIKgIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLiKDGKLDGTVAQQ---PFGM--GARAVELAIQAL 256
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|
| PBP1_SBP-like |
cd06327 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
32-263 |
5.13e-05 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in gram-negative, gram-positive bacteria, and archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380550 [Multi-domain] Cd Length: 336 Bit Score: 44.87 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 32 TIGLAGPLTGP-SARIGKDLENGAQLAIDDINkqhPTIGGKAVtfKLQSEDDQSDPRTAVAVAQRLVDS-GVAGVVGHWN 109
Cdd:cd06327 1 RIGVLTDLSGVyADLSGPGSVEAAKMAVEDFG---GKVLGRPI--EVVSADHQNKPDVASAIAREWYDRdGVDAIVDVPN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 110 TGTSIPAARVYHDAGI-----AQVAPVATGHAYTKQGFDTSFrvmghddDGGQFA---GQYAVQTLKaKRIAVIDDRTAF 181
Cdd:cd06327 76 SAVALAVQKLAKEKKKiaivtGAGSSDLTGKACSPYGVHWAY-------DTYALArgtVKALVKQGG-KSWFFITADYAF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 182 GQGLADEFIKSLKAQGIDIVDRQYVDDKTVDFSAVLTAIRSKNADLIFF--GGVDsqaapLARRIKQM---GISATLMG- 255
Cdd:cd06327 148 GHSLEADATAAVKAAGGKVVGSVRHPLGTTDFSSFLLQAQASGADVIALanAGAD-----LVNAVKQArefGLTDGGQKl 222
|
....*...
gi 2294035498 256 AGGFVSQT 263
Cdd:cd06327 223 AALLLFIT 230
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
70-257 |
7.53e-03 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 37.93 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 70 GKAVTFKLQSEDDQSDPRTAVAVAQRLVDSGVAG-VVGHWNTGTSIPAARVYHDAGIaqvaPVATGHAYTKQGFDTSFRV 148
Cdd:cd01536 25 AKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAiIIAPVDSEALVPAVKKANAAGI----PVVAVDTDIDGGGDVVAFV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294035498 149 MGHDDDGGQFAGQYAVQTLKAK-RIAVI---------DDRTafgQGladeFIKSLKA-QGIDIVDRQYVD-DKTVDFSAV 216
Cdd:cd01536 101 GTDNYEAGKLAGEYLAEALGGKgKVAILegppgsstaIDRT---KG----FKEALKKyPDIEIVAEQPANwDRAKALTVT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2294035498 217 LTAIRS-KNADLIFFGGvDSQAAPLARRIKQMGISATLMGAG 257
Cdd:cd01536 174 ENLLQAnPDIDAVFAAN-DDMALGAAEALKAAGRTGDIKIVG 214
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