|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-311 |
0e+00 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 539.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:COG1125 1 MIEFENVTKRY----PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 241 VGQDRTLKRLLLVSAGDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASG 311
Cdd:COG1125 237 VGADRGLRRLSLLRVEDLMLPEP-PTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-247 |
7.26e-141 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 400.14 E-value: 7.26e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03295 1 IEFENVTKRY--GGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
....*.
gi 446515747 242 GQDRTL 247
Cdd:cd03295 237 GADRLL 242
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-371 |
4.97e-111 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 329.12 E-value: 4.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL----RRNIGYVIQQIGLFPNM 95
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQFALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:TIGR01186 87 TILQNTSLGPELLGWPEQERKEKALELLKLVGLE--EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 176 REVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVGQDRTLKRLllvSA 255
Cdd:TIGR01186 165 RDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVF---DA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 256 GDVTDQQPT--ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVK---RREARNASGICADITHPFRITGKAEDNL 330
Cdd:TIGR01186 242 ERIAQRMNTgpITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDvesIKQARKKAQGLQDVLIDDIYTVDAGTLL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446515747 331 RIVLSRLYESNTSwMPIVDEDGRYNGEISQDYIADYLSSGR 371
Cdd:TIGR01186 322 RETVRKVLKAGIK-VPVVDEDQRLVGIVTRGSLVDALYDSR 361
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-361 |
3.21e-107 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 320.13 E-value: 3.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 5 ENLTKQFVQKK-GQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL----R 79
Cdd:COG4175 26 QGKSKDEILEKtGQTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:COG4175 105 KKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWE--DSYPDELSGGMQQRVGLARALATDP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGS 239
Cdd:COG4175 183 DILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVAD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 240 FV-GQDRTlkRLLlvSAGDVTdQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGICADITH 318
Cdd:COG4175 263 FVeDVDRS--KVL--TAGSVM-RPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVVTADDALEAVKGEKDLEE 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446515747 319 PFR---ITGKAEDNLRIVLSRLYESNTSwMPIVDEDGRYNGEISQD 361
Cdd:COG4175 338 ILLtdvPTVSPDTPLRDLLPLVAESPYP-LAVVDEDGRLLGVISRG 382
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-243 |
8.17e-98 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 294.70 E-value: 8.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntnDMDTVTL-R 79
Cdd:COG3842 5 ALELENVSKRY----GD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR---DVTGLPPeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEG--LADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGS 239
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVAD 234
|
....
gi 446515747 240 FVGQ 243
Cdd:COG3842 235 FIGE 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-246 |
5.69e-90 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 271.82 E-value: 5.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLK-------------------AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGN 62
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 63 ILINGENTNDMDTVTL----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYP 138
Cdd:cd03294 81 VLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEG--WEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 139 KEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250 260
....*....|....*....|....*....
gi 446515747 219 IVQCASPDELLAKPANEFVGSFV-GQDRT 246
Cdd:cd03294 239 LVQVGTPEEILTNPANDYVREFFrGVDRA 267
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-220 |
1.57e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.42 E-value: 1.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdtvtLRR 80
Cdd:COG1116 7 ALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAG--FEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGRIV 220
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIV 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
1.04e-87 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 264.00 E-value: 1.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG--LLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCA 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-242 |
1.32e-87 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 268.86 E-value: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRR 80
Cdd:COG3839 3 SLELENVSKSY-----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233
|
..
gi 446515747 241 VG 242
Cdd:COG3839 234 IG 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-221 |
1.46e-87 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 263.95 E-value: 1.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdtvtLRRN 81
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG--FENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGRIVQ 221
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-242 |
2.43e-83 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 257.77 E-value: 2.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNdMDTVTLRRN 81
Cdd:COG1118 3 IEVRNISKRF----GS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE--GLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
.
gi 446515747 242 G 242
Cdd:COG1118 235 G 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-242 |
5.65e-81 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 247.54 E-value: 5.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvtLRRN 81
Cdd:cd03300 1 IELENVSKFYGGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
.
gi 446515747 242 G 242
Cdd:cd03300 232 G 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-231 |
1.05e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 236.50 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRRN 81
Cdd:COG1131 1 IEVRGLTKRYGDKT-----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAA--DRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-235 |
1.79e-76 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 245.20 E-value: 1.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVT 77
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQ----QigLFPNMTIEENITVVPRMLGW-DKARCKQRAEELMDMVALDARkFLHRYPKEMSGGQQQRIGVI 152
Cdd:COG1123 340 LRRRVQMVFQdpysS--LNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPD-LADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
...
gi 446515747 233 ANE 235
Cdd:COG1123 497 QHP 499
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-243 |
3.26e-75 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 233.00 E-value: 3.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDtvTLRRN 81
Cdd:cd03296 3 IEVRNVSKRFGD-----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENIT----VVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD--WLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFV 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....*.
gi 446515747 238 GSFVGQ 243
Cdd:cd03296 234 YSFLGE 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
4.49e-73 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 226.60 E-value: 4.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL--- 78
Cdd:cd03255 1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDR--LNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEAlKLGDRIAVFRQGRI 219
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
1.57e-72 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 226.01 E-value: 1.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT---VT 77
Cdd:COG1127 5 MIEVRNLTKSFGDRV-----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLG-WDKARCKQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLREHTdLSEAEIRELVLEKLELVGL--PGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPaNEF 236
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPW 236
|
....*
gi 446515747 237 VGSFV 241
Cdd:COG1127 237 VRQFL 241
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
8-241 |
2.63e-72 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 230.43 E-value: 2.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 8 TKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILI-NGENTNDM---DTVTLRR--- 80
Cdd:TIGR03415 26 TREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkDGDGSVDVancDAATLRRlrt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 -NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:TIGR03415 106 hRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLA--QWADRKPGELSGGMQQRVGLARAFATEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGS 239
Cdd:TIGR03415 184 PILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRIIQHGTPEEIVLNPANDYVAD 263
|
..
gi 446515747 240 FV 241
Cdd:TIGR03415 264 FV 265
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
1.14e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 223.38 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:COG1136 4 LLELRNLTKSY-GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 --RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:COG1136 83 lrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDR--LDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGRIV 220
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-235 |
2.59e-71 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 222.95 E-value: 2.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEN--TNDMDTVTL 78
Cdd:COG1126 1 MIEIENLHKSF----GD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENITVVPRM-LGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKA--DAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDPIN-REViqnqfLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:COG1126 154 EPKVMLFDEPTSALDPELvGEV-----LDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
..
gi 446515747 234 NE 235
Cdd:COG1126 229 HE 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-248 |
1.22e-70 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 225.30 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:TIGR03265 5 LSIDNIRKRFGA-----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--KRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSE--RKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFV 235
|
....*..
gi 446515747 242 GQDRTLK 248
Cdd:TIGR03265 236 GEVNWLP 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
1.22e-69 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 216.67 E-value: 1.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMD--TVTLR 79
Cdd:cd03229 1 LELKNVSKRYGQKT-----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITvvprmlgwdkarckqraeelmdmvaldarkflhrYPkeMSGGQQQRIGVIRALAADP 159
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIA----------------------------------LG--LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-247 |
1.01e-68 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 216.20 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvtLRRN 81
Cdd:TIGR00968 1 IEIANISKRFGS-----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA--RDRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:TIGR00968 74 IGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLE--GLGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
....*.
gi 446515747 242 GQDRTL 247
Cdd:TIGR00968 232 GEVNVL 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
5.14e-67 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 210.96 E-value: 5.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE--HLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| CBS_pair_ABC_OpuCA_assoc |
cd04582 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
258-368 |
3.85e-66 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341359 [Multi-domain] Cd Length: 111 Bit Score: 205.31 E-value: 3.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 258 VTDQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGICADITHPFRITGKAEDNLRIVLSRL 337
Cdd:cd04582 1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGDFAHPFKATVPVDENLRVVLSRM 80
|
90 100 110
....*....|....*....|....*....|.
gi 446515747 338 YESNTSWMPIVDEDGRYNGEISQDYIADYLS 368
Cdd:cd04582 81 YEHNTSWLPVVDEDGRYAGEVTQDSIADYLS 111
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-242 |
6.32e-66 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 209.11 E-value: 6.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID--HLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
.
gi 446515747 242 G 242
Cdd:cd03299 231 G 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-240 |
2.08e-64 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 205.04 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVTL 78
Cdd:cd03261 1 IELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENITVVPRMLG-WDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAE--DLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPaNEFV 237
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLV 232
|
...
gi 446515747 238 GSF 240
Cdd:cd03261 233 RQF 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-220 |
1.16e-63 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 203.12 E-value: 1.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -RRNIGYVIQQIG--LFPNMTIEENITVVPRMLG--WDKARCKQRAEELMDMVALDARkFLHRYPKEMSGGQQQRIGVIR 153
Cdd:cd03257 80 rRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEE-VLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-232 |
1.48e-63 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 202.56 E-value: 1.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG1122 1 IELENLSFSYPGGT----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQ----QigLFpNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG1122 77 VGLVFQnpddQ--LF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLE--HLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-232 |
2.48e-63 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 202.43 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT---VT 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGK-VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKA--DAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-243 |
4.48e-63 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 206.34 E-value: 4.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:PRK09452 15 VELRGISKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
..
gi 446515747 242 GQ 243
Cdd:PRK09452 246 GE 247
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-243 |
7.15e-63 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 204.26 E-value: 7.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 37 LLGPSGCGKTTTLKMINRLIAPSSGNILINGENtndmdtVTL----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDK 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGED------VTNvpphLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 113 ARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKK 192
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLE--EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446515747 193 TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVGQ 243
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-235 |
1.42e-62 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 200.85 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTnDMDTVTLRR 80
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE--EFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANE 235
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-243 |
2.47e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 203.39 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT---VT 77
Cdd:COG1135 1 MIELENLSKTFPTKGG-PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKA--DAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFV 237
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
....*.
gi 446515747 238 GSFVGQ 243
Cdd:COG1135 238 RRFLPT 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
1.47e-61 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 196.98 E-value: 1.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTND--MDTVTLR 79
Cdd:cd03262 1 IEIKNLHKSF-----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITVVPR-MLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKA--DAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 159 PPVLLMDEPFGAVDPinrEVIqNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:cd03262 154 PKVMLFDEPTSALDP---ELV-GEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-220 |
2.01e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 196.81 E-value: 2.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKqfVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT--- 77
Cdd:COG2884 1 MIRFENVSK--RYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDK--AKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRkLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-243 |
1.05e-60 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 199.56 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdTVTLRRNIG 83
Cdd:PRK11432 9 LKNITKRFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLL 163
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAG--FEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 164 MDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVGQ 243
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD 239
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
2.87e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 194.89 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:COG3638 2 MLELRNLSKRYPGGT----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -RRNIGYVIQQIGLFPNMTIEENI--------TVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRI 149
Cdd:COG3638 78 lRRRIGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLFPPEDRERALEALERVGLA--DKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-236 |
4.31e-60 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 194.64 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEmCV-LLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLR 79
Cdd:COG1124 1 MLEVRNLSVSY-GQGGRRVPVLKDVSLEVAPGE-SFgLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIG--LFPNMTIEENITVVPRMLGwdKARCKQRAEELMDMVALDARkFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG1124 79 RRVQMVFQDPYasLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPS-FLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEF 236
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-226 |
4.38e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.08 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntndmdTVT--- 77
Cdd:COG4525 3 MLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV------PVTgpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRniGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:COG4525 76 ADR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLAD--FARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGRIVQCASPD 226
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLELD 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
5.42e-60 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 193.55 E-value: 5.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----APSSGNILINGEN--TNDMD 74
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLG-WDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIR 153
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQnqflDMQRKLKK--TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIE----ELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-243 |
4.66e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 195.30 E-value: 4.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntnDMDTVTLR-R 80
Cdd:PRK10851 3 IEIANIKKSFGRTQ-----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENI----TVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIafglTVLPRRERPNAAAIKAKVTQLLEMVQLA--HLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEF 236
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
....*..
gi 446515747 237 VGSFVGQ 243
Cdd:PRK10851 233 VLEFMGE 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
1.15e-58 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 187.99 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRRN 81
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENItvvprmlgwdkarckqraeelmdmvaldarkflhrypkEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-360 |
4.38e-58 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 194.10 E-value: 4.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 5 ENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLR----R 80
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLE--NYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 241 VgqdRTLKRLLLVSAGDVTDQQPT--ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVK----RREARNASGI-C 313
Cdd:PRK10070 265 F---RGVDISQVFSAKDIARRTPNglIRKTPGFGPRSALKLLQDEDREYGYVIERGNKFVGAVSidslKTALTQQQGLdA 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446515747 314 ADITHPFRItgKAEDNLRIVLSRLYESNTSwMPIVDEDGRYNGEISQ 360
Cdd:PRK10070 342 ALIDAPLAV--DAQTPLSELLSHVGQAPCA-VPVVDEDQQYVGIISK 385
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
1.16e-57 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 186.90 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 3 KLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNI 82
Cdd:cd03225 1 ELKNLSFSY---PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQ----QigLFpNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:cd03225 78 GLVFQnpddQ--FF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEG--LRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-232 |
2.84e-57 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 188.04 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT-- 77
Cdd:TIGR04521 1 IKLKNVS--YIYQPGTPFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 -LRRNIGYVIQ----QigLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALDaRKFLHRYPKEMSGGQQQRIGVI 152
Cdd:TIGR04521 79 dLRKKVGLVFQfpehQ--LFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLD-EEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
2.04e-56 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 187.18 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAP---SSGNILINGENTNDMDTVT 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LR----RNIGYVIQ--QIGLFPNMTIEENITVVPRM-LGWDKARCKQRAEELMDMVAL-DARKFLHRYPKEMSGGQQQRI 149
Cdd:COG0444 80 LRkirgREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
....
gi 446515747 230 AKPA 233
Cdd:COG0444 240 ENPR 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-228 |
3.64e-56 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 183.92 E-value: 3.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL--- 78
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENI--------TVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIG 150
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENVlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLL--DKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-235 |
3.77e-56 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 184.42 E-value: 3.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL-----IAPSSGNILINGENTND--MD 74
Cdd:TIGR00972 2 IEIENLNLFYGEKE-----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDkkID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-DKARCKQRAEELMDMVAL-DARK-FLHRYPKEMSGGQQQRIGV 151
Cdd:TIGR00972 77 VVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKdRLHDSALGLSGGQQQRLCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 152 IRALAADPPVLLMDEPFGAVDPINREVIQnqflDMQRKLKK--TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIATGKIE----ELIQELKKkyTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231
|
....*.
gi 446515747 230 AKPANE 235
Cdd:TIGR00972 232 TNPKEK 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
1.91e-55 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 181.55 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNdMDTVTLRRN 81
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL--TDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-244 |
4.54e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 184.62 E-value: 4.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENT---NDMDTVT 77
Cdd:PRK11153 1 MIELKNISKVFPQGGRT-IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKA--DRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP----A 233
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplT 237
|
250
....*....|.
gi 446515747 234 NEFVGSFVGQD 244
Cdd:PRK11153 238 REFIQSTLHLD 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 |
6.03e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 181.06 E-value: 6.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTND--MDTVTL 78
Cdd:PRK09493 1 MIEFKNVSKHF----GP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERA--HHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 158 DPPVLLMDEPFGAVDP-INREViqnqfLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:PRK09493 154 KPKLMLFDEPTSALDPeLRHEV-----LKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*..
gi 446515747 234 NEFVGSF 240
Cdd:PRK09493 229 SQRLQEF 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
1.12e-54 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 180.62 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:COG1120 1 MLEAENLS---VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEEnitVV-----P--RMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIR 153
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRE---LValgryPhlGLFGRPSAEDREAVEEALERTGLEH--LADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-242 |
1.99e-54 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 183.88 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvtLRR 80
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
..
gi 446515747 241 VG 242
Cdd:PRK11607 250 IG 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
3.62e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 186.65 E-value: 3.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPS---SGNILINGENTNDMDTVT 77
Cdd:COG1123 4 LLEVRDLSVRY---PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIG--LFPnMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRAL 155
Cdd:COG1123 81 RGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERR--LDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 156 AADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-228 |
3.91e-54 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 178.33 E-value: 3.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRRN 81
Cdd:cd03265 1 IEVENLVKKYGD-----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVAL-DARkflHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLlEAA---DRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-277 |
1.28e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 179.15 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDtvtlRR 80
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG4152 72 RIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRA--NKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK-PANEFVGS 239
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 446515747 240 FVGQDRTLKRLLLVSAGDVTDQQPTITARPSTPLSEAF 277
Cdd:COG4152 229 ADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELL 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-233 |
3.39e-53 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 179.16 E-value: 3.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKG------QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT 75
Cdd:COG4608 8 LEVRDLKKHFPVRGGlfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 ---VTLRRNIGYVIQ--QIGLFPNMTIEENITVVPRMLG-WDKARCKQRAEELMDMVALDARkFLHRYPKEMSGGQQQRI 149
Cdd:COG4608 88 relRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPE-HADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDpinreV-IQNQ----FLDMQRKLKKTVMLVSHDidealkLG------DRIAVFRQGR 218
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALD-----VsIQAQvlnlLEDLQDELGLTYLFISHD------LSvvrhisDRVAVMYLGK 235
|
250
....*....|....*
gi 446515747 219 IVQCASPDELLAKPA 233
Cdd:COG4608 236 IVEIAPRDELYARPL 250
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-228 |
4.12e-53 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 176.33 E-value: 4.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVT 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENI--------TVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRI 149
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLA--DKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
2.01e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 2.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGqplkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG4619 1 LELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITVVPRMLgwDKARCKQRAEELMDMVALDArKFLHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQLR--ERKFDRERALELLERLGLPP-DILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-231 |
2.75e-52 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 185.04 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG2274 474 IELENVSFRY---PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITVvprmlgWDKARCKQRAEELMDMVALDArkFLHRYPK-------EM----SGGQQQRIG 150
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITL------GDPDATDEEIIEAARLAGLHD--FIEALPMgydtvvgEGgsnlSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDiDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
.
gi 446515747 231 K 231
Cdd:COG2274 699 R 699
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.04e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMdtvtlRR 80
Cdd:COG1121 6 AIELENLT---VSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGL---FPnMTIEEnitVVprMLGWD---------KARCKQRAEELMDMValDARKFLHRYPKEMSGGQQQR 148
Cdd:COG1121 76 RIGYVPQRAEVdwdFP-ITVRD---VV--LMGRYgrrglfrrpSRADREAVDEALERV--GLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCaSPDEL 228
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALY-ELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG-PPEEV 225
|
.
gi 446515747 229 L 229
Cdd:COG1121 226 L 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-221 |
3.57e-51 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 170.17 E-value: 3.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVP---EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING----ENTNDMDTVTLRRNIGYVIQQIGLF 92
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 93 PNMTIEENITVVprMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:cd03297 88 PHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLD--HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446515747 173 PINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-235 |
4.52e-51 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 171.37 E-value: 4.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----APSSGNILINGENTND--MDTVTLRRNIGYVIQQIGLF 92
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDpdVDVVELRRRVGMVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 93 PnMTIEENITVVPRMLGW-DKARCKQRAEELMDMVAL-----DaRkfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:COG1117 105 P-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkD-R--LKKSALGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 167 PFGAVDPINREVIQnqflDMQRKLKK--TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANE 235
Cdd:COG1117 181 PTSALDPISTAKIE----ELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-242 |
1.90e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 173.29 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRNIGYVIQQIGLFPNMTIEENITV 103
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 VPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQF 183
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLA--HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 184 LDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVG 242
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-242 |
2.08e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 172.72 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRR 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELE--PLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
..
gi 446515747 241 VG 242
Cdd:PRK11650 235 IG 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-227 |
2.13e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 170.61 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTND--MDTVT 77
Cdd:PRK13637 3 IKIENLT--HIYMEGTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRAL 155
Cdd:PRK13637 81 IRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 156 AADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDE 227
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
2.36e-50 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 169.45 E-value: 2.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-R 79
Cdd:COG0411 4 LLEVRGLTKRF---GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITV----------VPRMLGWDKAR-----CKQRAEELMDMVALDARkfLHRYPKEMSGG 144
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVaaharlgrglLAALLRLPRARreereARERAEELLERVGLADR--ADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCAS 224
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 446515747 225 PDELLAKPA 233
Cdd:COG0411 237 PAEVRADPR 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-221 |
3.58e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 168.65 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING------ENTNDMDTVTLRRNIGYVIQQIGLFP 93
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 94 NMTIEENITVVP-RMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK11124 96 HLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKP--YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446515747 173 PinreVIQNQFLDMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:PRK11124 174 P----EITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
5.23e-50 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 165.63 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03228 1 IEFKNVSFSY---PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENItvvprmlgwdkarckqraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGR 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
3.82e-49 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 165.69 E-value: 3.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMD-TVTLRR 80
Cdd:cd03219 1 LEVRGLTKRF---GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVV-----PRMLGWDKAR-----CKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIG 150
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAaqartGSGLLLARARreereARERAEELLERVGLADL--ADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 446515747 231 KPA 233
Cdd:cd03219 233 NPR 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-221 |
7.16e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.19 E-value: 7.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE------NTNDMDTVTLRRNIGYVIQQIGLFPN 94
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITVVP-RMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:COG4161 97 LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLT--DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446515747 174 inreVIQNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:COG4161 175 ----EITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-168 |
9.17e-49 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 161.66 E-value: 9.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 102 TVVPRMLGWDKARCKQRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
1.54e-48 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 172.64 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG4987 334 LELEDVSFRY---PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITVVprmlgwdkarcKQRA--EELMDM---VALDarKFLHRYPK-------E----MSGGQ 145
Cdd:COG4987 411 IAVVPQRPHLF-DTTLRENLRLA-----------RPDAtdEELWAAlerVGLG--DWLAALPDgldtwlgEggrrLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDPIN-REVIQnqflDMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGRIVQCA 223
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATeQALLA----DLLEALAgRTVLLITHRL-AGLERMDRILVLEDGRIVEQG 551
|
250
....*....|
gi 446515747 224 SPDELLAKPA 233
Cdd:COG4987 552 THEELLAQNG 561
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-243 |
7.91e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 162.23 E-value: 7.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLKAvdnvNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntnDMDTVTL-R 79
Cdd:COG3840 1 MLRLDDLTYRY---GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPPaE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITvvprmLGWDK-----ARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRA 154
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIG-----LGLRPglkltAEQRAQVEQALERVGLAG--LLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 155 LAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPAN 234
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*....
gi 446515747 235 EFVGSFVGQ 243
Cdd:COG3840 224 PALAAYLGI 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
2.99e-47 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 160.23 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRR 80
Cdd:cd03266 1 MITADALTKRF-RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMvaLDARKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADR--LGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 161 VLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
3.34e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 159.75 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDtvtlRRN 81
Cdd:cd03269 1 LEVENVTKRFGRVT-----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYA--NKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-218 |
4.71e-47 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 159.72 E-value: 4.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVT 77
Cdd:TIGR02673 1 MIEFHNVSKAY----PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFlhRYPKEMSGGQQQRIGVIRALAA 157
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKAD--AFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 158 DPPVLLMDEPFGAVDPINREviqnQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSE----RILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-226 |
2.40e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 159.09 E-value: 2.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvtlRR 80
Cdd:PRK11248 1 MLQISHLYADY---GGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 niGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEG--AEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFR--QGRIVQCASPD 226
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-220 |
2.65e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 157.38 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRN 81
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCkqraEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSA--KKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-231 |
6.60e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.72 E-value: 6.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG1132 340 IEFENVS--FSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITvvprmLGwdkarcKQRA--EELMD-MVALDARKFLHRYPK-----------EMSGGQQQ 147
Cdd:COG1132 416 IGVVPQDTFLF-SGTIRENIR-----YG------RPDAtdEEVEEaAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHD---IDEAlklgDRIAVFRQGRIVQCAS 224
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRlstIRNA----DRILVLDDGRIVEQGT 557
|
....*..
gi 446515747 225 PDELLAK 231
Cdd:COG1132 558 HEELLAR 564
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
2.58e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 153.17 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 3 KLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNI 82
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQqiglfpnmtieenitvvprmlgwdkarckqraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd00267 76 GYVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 163 LMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-233 |
4.31e-45 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 158.73 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE----NTNDMDTVTLRRNIGYVIQQIGLFPNMTIEE 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NITvvprmLGWDKARCKQRAEELMDMVA-LDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PINRE 177
Cdd:COG4148 97 NLL-----YGRKRAPRAERRISFDEVVElLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDlARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 178 VIqnQFLD-MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:COG4148 172 IL--PYLErLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-222 |
7.06e-45 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 152.59 E-value: 7.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 3 KLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNI 82
Cdd:cd03214 1 EVENLSVGYGGRT-----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQiglfpnmtieenitvvprmlgwdkarckqraeelmdMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03214 76 AYVPQA------------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 163 LMDEPFGAVDPINreviQNQFLDMQRKLK----KTVMLVSHDIDEALKLGDRIAVFRQGRIVQC 222
Cdd:cd03214 120 LLDEPTSHLDIAH----QIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
1.88e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.14 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQP-LKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILInGENTNDMDTV--- 76
Cdd:PRK11264 3 AIEVKNLVKKF---HGQTvLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSlsq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 ------TLRRNIGYVIQQIGLFPNMTIEENITVVPRML-GWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRI 149
Cdd:PRK11264 76 qkglirQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPinrEVIqNQFLDMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPD 226
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDP---ELV-GEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250 260
....*....|....*....|.
gi 446515747 227 ELLAKPANE----FVGSFVGQ 243
Cdd:PRK11264 230 ALFADPQQPrtrqFLEKFLLQ 250
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
2.81e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 160.69 E-value: 2.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG4988 337 IELEDVS--FSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPnMTIEENITvvprmLGWDKARcKQRAEELMDMVALDArkFLHRYPKEM-----------SGGQQQRIG 150
Cdd:COG4988 413 IAWVPQNPYLFA-GTIRENLR-----LGRPDAS-DEELEAALEAAGLDE--FVAALPDGLdtplgeggrglSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
.
gi 446515747 231 K 231
Cdd:COG4988 561 K 561
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-222 |
7.56e-44 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 151.19 E-value: 7.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqKKGqplKAVDNVNLNVPEGeMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMdTVTLRRN 81
Cdd:cd03264 1 LQLENLTKRY--GKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA--KKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQC 222
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-233 |
1.58e-43 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 154.50 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTND----MDTVTLRRNIGYVIQQIGLFPNMTIEEN 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ItvvprMLGWDKARCKQRA---EELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PINR 176
Cdd:TIGR02142 96 L-----RYGMKRARPSERRisfERVIELLGIG--HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 177 EVIqnQFLD-MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:TIGR02142 169 EIL--PYLErLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
2.96e-43 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 150.39 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGentNDMDTVTL--- 78
Cdd:cd03218 1 LRAENLSKRYGKRK-----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITKLPMhkr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:cd03218 73 aRLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHIT--HLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNqfldMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQK----IIKILKDRgigVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-230 |
6.66e-43 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 149.12 E-value: 6.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT-LRRNIGYVIQQIGLFPNMTIEE 99
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItvvprMLGWdKARCKQRAEELMDMV-----ALDARkfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPi 174
Cdd:cd03224 95 NL-----LLGA-YARRRAKRKARLERVyelfpRLKER--RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 175 nreVIQNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:cd03224 166 ---KIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
8.71e-43 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 149.12 E-value: 8.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQfVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT---VT 77
Cdd:COG4181 8 IIELRGLTKT-VGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LR-RNIGYVIQQIGLFPNMTIEENItvvprML-----GWDKARckQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGV 151
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALENV-----MLplelaGRRDAR--ARARALLERVGLGHR--LDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGRIVQ 221
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVE 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-232 |
1.73e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 148.25 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENtndmdtVTL-- 78
Cdd:COG1137 3 TLEAENLVKSY---GKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED------ITHlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIR 153
Cdd:COG1137 72 mhkraRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT--HLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQnqflDMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQ----KIIRHLKERgigVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
..
gi 446515747 231 KP 232
Cdd:COG1137 226 NP 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
2.00e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 150.24 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTND--------- 72
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 73 -MDTVT--------------LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALDaRKFLH 135
Cdd:PRK13651 83 vLEKLViqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD-ESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 136 RYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQrKLKKTVMLVSHDIDEALKLGDRIAVFR 215
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 446515747 216 QGRIVQCASPDELLA 230
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-214 |
2.05e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 147.29 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 3 KLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMdtvtlRRNI 82
Cdd:cd03235 1 EVEDLTVSYGGHP-----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGL---FPnMTIEEnitVV-------PRMLGWDKARCKQRAEELMDMValDARKFLHRYPKEMSGGQQQRIGVI 152
Cdd:cd03235 71 GYVPQRRSIdrdFP-ISVRD---VVlmglyghKGLFRRLSKADKAKVDEALERV--GLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINreviQNQFLDMQRKLK---KTVMLVSHDIDEALKLGDRIAVF 214
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKT----QEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
3.29e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 146.47 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRR 80
Cdd:COG4133 2 MLEAENLSCRR---GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARckQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGL--AGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 161 VLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVMLVSHDIDEA-----LKLGDR 210
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
5.01e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 147.75 E-value: 5.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----APSSGNILINGENTNDMDTV 76
Cdd:PRK14247 4 IEIRDLKVSFGQ-----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRRNIGYVIQQIGLFPNMTIEENITVVPRM--LGWDKARCKQRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVI 152
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
....*....
gi 446515747 233 ANEFVGSFV 241
Cdd:PRK14247 237 RHELTEKYV 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
8.00e-42 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 146.46 E-value: 8.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntnDMDTVTLRRNIgyVIQQIGLFPNMTIEENI 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGPDRMV--VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 102 TVVPRMLGWDKARCKQRA--EELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVI 179
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAivEEHIALVGL--TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 446515747 180 QNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-227 |
1.08e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 145.32 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAP---SSGNILINGEntnDMDTV- 76
Cdd:COG4136 1 MLSLENLT---ITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGR---RLTALp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRRNIGYVIQQIGLFPNMTIEENITV-VPRMLGwdKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRAL 155
Cdd:COG4136 73 AEQRRIGILFQDDLLFPHLSVGENLAFaLPPTIG--RAQRRARVEQALEEAGLAG--FADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 156 AADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKlgdriavfrQGRIVQCASPDE 227
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-233 |
1.19e-41 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 146.28 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-RRNIGYVIQQIGLFPNMTIEE 99
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItVVPRMLGWDKARCKQRAEELMDMV-ALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPinreV 178
Cdd:COG0410 98 NL-LLGAYARRDRAEVRADLERVYELFpRL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP----L 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 179 IQNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:COG0410 171 IVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-235 |
1.62e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.88 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLKavdnVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdTVTLRR 80
Cdd:PRK10771 1 MLKLTDITWLY---HHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT--TPPSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITvvprmLGWD---KARCKQRA--EELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRAL 155
Cdd:PRK10771 72 PVSMLFQENNLFSHLTVAQNIG-----LGLNpglKLNAAQREklHAIARQMGIED--LLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 156 AADPPVLLMDEPFGAVDPINReviqNQFLDM------QRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALR----QEMLTLvsqvcqERQL--TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
....*.
gi 446515747 230 AKPANE 235
Cdd:PRK10771 219 SGKASA 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
2.19e-41 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 152.26 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIN-GENTNDMDT--VT 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKpgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LR----RNIGYVIQQIGLFPNMTIEENITV-----VPRMLGwdkarcKQRAEELMDMVALD---ARKFLHRYPKEMSGGQ 145
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLTEaigleLPDELA------RMKAVITLKMVGFDeekAEEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASP 225
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....*
gi 446515747 226 DELLA 230
Cdd:TIGR03269 513 EEIVE 517
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-211 |
2.98e-41 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 144.30 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENT---NDMDTVTLRR 80
Cdd:TIGR03608 1 LKNISKKFGDKV-----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETpplNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 N-IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:TIGR03608 76 EkLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLK--LKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIdEALKLGDRI 211
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
5.86e-41 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 143.70 E-value: 5.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMD---TVTL 78
Cdd:cd03292 1 IEFINVTKTY----PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKH--RALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQNQFLDMQrKLKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-235 |
6.13e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.94 E-value: 6.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkG--QPLKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE---------- 68
Cdd:COG4598 8 ALEVRDLHKSF----GdlEVLKGVS---LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 69 --NTNDMDTVT-LRRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGG 144
Cdd:COG4598 81 elVPADRRQLQrIRTRLGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGLADKR--DAYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 145 QQQRIGVIRALAADPPVLLMDEPFGAVDP-INREViqnqfLDMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPeLVGEV-----LKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
250
....*....|....*
gi 446515747 221 QCASPDELLAKPANE 235
Cdd:COG4598 234 EQGPPAEVFGNPKSE 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-235 |
1.01e-40 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 150.61 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKG------QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIaPSSGNILINGENTNDMDT 75
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 ---VTLRRNIgyviqQI-------GLFPNMTIEENIT---VVPRMlGWDKARCKQRAEELMDMVALDARkFLHRYPKEMS 142
Cdd:COG4172 355 ralRPLRRRM-----QVvfqdpfgSLSPRMTVGQIIAeglRVHGP-GLSAAERRARVAEALEEVGLDPA-ARHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFL----DMQRKLKKTVMLVSHDideaLK----LGDRIAV 213
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALD-----VsVQAQILdllrDLQREHGLAYLFISHD----LAvvraLAHRVMV 498
|
250 260
....*....|....*....|..
gi 446515747 214 FRQGRIVQCASPDELLAKPANE 235
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDAPQHP 520
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-235 |
2.12e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 143.38 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--IAPS---SGNILINGEN--TNDMDTVTLRRNIGYVIQQIGLF 92
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 93 PnMTIEENITVVPRMLGW-DKARCKQRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 170 AVDPINREVIQNQFLDMqrKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANE 235
Cdd:PRK14239 178 ALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-220 |
3.98e-40 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 141.48 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 27 LNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlRRNIGYVIQQIGLFPNMTIEENIT--VV 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGlgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 105 PRMlgwdkarcKQRAEELMDMVALDAR----KFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ 180
Cdd:cd03298 97 PGL--------KLTAEDRQAIEVALARvglaGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446515747 181 NQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-232 |
6.51e-40 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 141.64 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT-VTLRR 80
Cdd:TIGR04406 2 LVAENLIKSYKKRK-----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMhERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENI-TVVPRMLGWDKARCKQRAEELMDmvALDARKFLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLE--EFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDM-QRKLKktVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLkERGIG--VLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
5.09e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 139.45 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGN-ILINGENTNDMDTVTLR 79
Cdd:COG1119 3 LLELRNVT---VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYV---IQQ-------------------IGLFPNMTIEEnitvvprmlgwdkarcKQRAEELMDMVALDARKflHRY 137
Cdd:COG1119 78 KRIGLVspaLQLrfprdetvldvvlsgffdsIGLYREPTDEQ----------------RERARELLELLGLAHLA--DRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 138 PKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREviqnQFLDMQRKL----KKTVMLVSHDIDEALKLGDRIAV 213
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARE----LLLALLDKLaaegAPTLVLVTHHVEEIPPGITHVLL 215
|
250
....*....|....*.
gi 446515747 214 FRQGRIVQCASPDELL 229
Cdd:COG1119 216 LKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-230 |
7.13e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 140.53 E-value: 7.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING----ENTNDMDTVT 77
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 -LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALdARKFLHRYPKEMSGGQQQRIGVIRA 154
Cdd:PRK13645 87 rLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 155 LAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
3.41e-38 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 136.80 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFV--QKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTN-DM---- 73
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvDLaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 74 --DTVTLRRN-IGYVIQqiglFpnmtieenITVVPRM------------LGWDKARCKQRAEELMDMVALDARKFlHRYP 138
Cdd:COG4778 84 prEILALRRRtIGYVSQ----F--------LRVIPRVsaldvvaeplleRGVDREEARARARELLARLNLPERLW-DLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 139 KEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIqnqfLDMQRKLKK--TVML-VSHDIDEALKLGDRIAVFR 215
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV----VELIEEAKArgTAIIgIFHDEEVREAVADRVVDVT 226
|
...
gi 446515747 216 QGR 218
Cdd:COG4778 227 PFS 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-220 |
3.46e-38 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 136.57 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 15 KGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpN 94
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLF-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITvvprmLGwDKARCKQRAEELMDMVALDarKFLHRYPKEM-----------SGGQQQRIGVIRALAADPPVLL 163
Cdd:cd03245 92 GTLRDNIT-----LG-APLADDERILRAAELAGVT--DFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 164 MDEPFGAVDPIN-REVIQNqfldMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGRIV 220
Cdd:cd03245 164 LDEPTSAMDMNSeERLKER----LRQLLGdKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
11-233 |
6.47e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.84 E-value: 6.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 11 FVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILInGE-----NTNDMDTVTLRRNIG 83
Cdd:PRK13634 10 HRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GErvitaGKKNKKLKPLRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQqiglFPNM-----TIEENITVVPRMLGWDKARCKQRAEELMDMVALDArKFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:PRK13634 89 IVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPE-ELLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-231 |
2.25e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 134.97 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEE 99
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItvvprmlgwdkARCKQRAEELMDMVAL---DARKFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMD 165
Cdd:cd03249 96 NI-----------RYGKPDATDEEVEEAAkkaNIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 166 EPFGAVDPINREVIQNQfLDmQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:cd03249 165 EATSALDAESEKLVQEA-LD-RAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-241 |
2.70e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.56 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIA------PSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTI 97
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 98 EENITVVPRMLGW-DKARCKQRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPI 174
Cdd:PRK14246 108 YDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 175 NREVIQNQFLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK14246 188 NSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-219 |
3.61e-37 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 133.69 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPlKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVT 77
Cdd:NF038007 1 MLNMQNAEKCYITKTIKT-KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLsysQKII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRN-IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALA 156
Cdd:NF038007 80 LRRElIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRR--NHKPMQLSGGQQQRVAIARAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDiDEALKLGDRIAVFRQGRI 219
Cdd:NF038007 158 SNPALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-231 |
3.87e-37 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 133.89 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLtkQFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03254 3 IEFENV--NFSYDEKKP--VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITvvprmLGWDKARckqRAEELMDMVALDARKFLHRYPK-----------EMSGGQQQRIG 150
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIR-----LGRPNAT---DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNqflDMQRKLK-KTVMLVSHDIDeALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQE---ALEKLMKgRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
..
gi 446515747 230 AK 231
Cdd:cd03254 226 AK 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
4.02e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVqkkgqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:COG1129 4 LLEMRGISKSFG-----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 N-IGYVIQQIGLFPNMTIEENITV--VPRMLGW-DKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:COG1129 79 AgIAIIHQELNLVPNLSVAENIFLgrEPRRGGLiDWRAMRRRARELLARLGLDID--PDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 157 ADPPVLLMDEPFGAVDPinREViqNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:COG1129 157 RDARVLILDEPTASLTE--REV--ERLFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-241 |
1.25e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 133.43 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----APSSGNILINGEN--TNDMDTVTLRRNIGYVIQQIGLFPN 94
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITVVPRMLGWDKARCK--QRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 171 VDPINREVIQNQFLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
9-232 |
4.59e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 134.06 E-value: 4.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 9 KQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTlRRNIGYVIQQ 88
Cdd:PRK15079 24 KQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE-WRAVRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 89 I------GLFPNMTIEENI-----TVVPRMlgwDKARCKQRAEELMDMVALdARKFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:PRK15079 103 IfqdplaSLNPRMTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGL-LPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 158 DPPVLLMDEPFGAVD-PINREVIqNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK15079 179 EPKLIICDEPVSALDvSIQAQVV-NLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-241 |
5.37e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.01 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTN---DMD----------TVTLRRNIGYVIQQIGL 91
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDgqlkvadknqLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 92 FPNMTIEENITVVP-RMLGWDKARCKQRAEELMDMVALDARKfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:PRK10619 104 WSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERA-QGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 171 VDPinrEVIQNQFLDMQRKLK--KTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK10619 183 LDP---ELVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-231 |
5.79e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.85 E-value: 5.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:TIGR03375 464 IEFRNVSFAY---PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITVvpRMLGWDKARCkQRAEELmdmVALDArkFLHRYPK-----------EMSGGQQQRIG 150
Cdd:TIGR03375 541 IGYVPQDPRLF-YGTLRDNIAL--GAPYADDEEI-LRAAEL---AGVTE--FVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDpINREviqNQFLDMQRKL--KKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMD-NRSE---ERFKDRLKRWlaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
|
...
gi 446515747 229 LAK 231
Cdd:TIGR03375 687 LEA 689
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-220 |
9.01e-36 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 130.53 E-value: 9.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmDTVTLRRNIG 83
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVI-QQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMvaLDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03267 98 VVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSEL--LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 163 LMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-229 |
1.07e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 130.90 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK11231 2 TLRTENLTVGYGTKR-----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQiglfpnMTIEENITV--------VP------RMLGWDKARCkQRAEELMDMVALDARKFlhrypKEMSGGQQ 146
Cdd:PRK11231 77 RLALLPQH------HLTPEGITVrelvaygrSPwlslwgRLSAEDNARV-NQAMEQTRINHLADRRL-----TDLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 147 QRIGVIRALAADPPVLLMDEPFGAVDpINREViqnQFLDMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGRIVQCA 223
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLD-INHQV---ELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
....*.
gi 446515747 224 SPDELL 229
Cdd:PRK11231 221 TPEEVM 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-294 |
1.11e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 132.90 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQP----------------LKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIL 64
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 65 INGENTNDmDTVTLRRNIGYVI---QQigLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMvaLDARKFLHRYPKEM 141
Cdd:COG4586 81 VLGYVPFK-RRKEFARRIGVVFgqrSQ--LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVEL--LDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 142 SGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQnQFL-DMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR-EFLkEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 221 QCASPDELLAKpanefvgsfVGQDRTLK--------RLLLVSAGDVTDQQP---TITARPSTPLSEAFG-IMDDHDIRAI 288
Cdd:COG4586 235 YDGSLEELKER---------FGPYKTIVlelaepvpPLELPRGGEVIEREGnrvRLEVDPRESLAEVLArLLARYPVRDL 305
|
....*.
gi 446515747 289 TVIDND 294
Cdd:COG4586 306 TIEEPP 311
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-231 |
1.65e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 131.44 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING----ENTNDMDT 75
Cdd:PRK13646 3 IRFDNVS--YTYQKGTPYehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 VTLRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALdARKFLHRYPKEMSGGQQQRIGVIR 153
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
2.00e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 135.97 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKkGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPS----SGNILINGENTNDMDTV 76
Cdd:COG4172 6 LLSVEDLSVAFGQG-GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRR----NIGYVIQQ--IGLFPNMTIEENITVVPRM-LGWDKARCKQRAEELMDMVAL-DARKFLHRYPKEMSGGQQQR 148
Cdd:COG4172 85 ELRRirgnRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDPERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFL----DMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCA 223
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALD-----VtVQAQILdllkDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250
....*....|
gi 446515747 224 SPDELLAKPA 233
Cdd:COG4172 240 PTAELFAAPQ 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-241 |
2.70e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 130.29 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--IAPS---SGNILINGENTND--MDTVTLRRNIGYVIQQIGLFP 93
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 94 NmTIEENITVVPRMLGWdKARCKQRAEELMDMVAL--DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK14243 105 K-SIYDNIAYGARINGY-KGDMDELVERSLRQAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 172 DPINREVIQnqflDMQRKLKK--TVMLVSHDIDEALKLGDRIAVF---------RQGRIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK14243 183 DPISTLRIE----ELMHELKEqyTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDY 258
|
.
gi 446515747 241 V 241
Cdd:PRK14243 259 V 259
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-231 |
2.99e-35 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 129.27 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNM 95
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITVVPRMLGWDKARCKQRAEELMDmvaldarkFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLM 164
Cdd:cd03251 91 TVAENIAYGRPGATREEVEEAARAANAHE--------FIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 165 DEPFGAVDPINREVIQNQfldMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:cd03251 163 DEATSALDTESERLVQAA---LERLMKnRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
3.15e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.85 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:COG4559 1 MLEAENLS---VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGL-FPnMTIEEnitVVpRM----LGWDKARCKQRAEELMDMVALDArkFLHR-YPkEMSGGQQQRIGVIRA 154
Cdd:COG4559 76 RRAVLPQHSSLaFP-FTVEE---VV-ALgrapHGSSAAQDRQIVREALALVGLAH--LAGRsYQ-TLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 155 LA-------ADPPVLLMDEPFGAVDPINreviQNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCAS 224
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAH----QHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
....*
gi 446515747 225 PDELL 229
Cdd:COG4559 224 PEEVL 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-221 |
5.69e-35 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 128.06 E-value: 5.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 26 NLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTndMDTVTLRRNIGYVIQQIGLFPNMTIEENITvvp 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHLTVRQNIG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 106 rmLGWD-----KARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ 180
Cdd:TIGR01277 93 --LGLHpglklNAEQQEKVVDAAQQVGIA--DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446515747 181 NQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-231 |
6.18e-35 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 128.37 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03252 1 ITFEHVR--FRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITVVprmlgwDKARCKQRAEELMDMValDARKFLHRYPK-----------EMSGGQQQRIG 150
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLA--GAHDFISELPEgydtivgeqgaGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNqflDMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMR---NMHDICAgRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
..
gi 446515747 230 AK 231
Cdd:cd03252 225 AE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-221 |
6.53e-35 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 129.15 E-value: 6.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 15 KGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT---LRRNIGYVIQQ-IG 90
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 91 LF-PNMTIEENITVVPR-MLGWDKARCKQRAEELMDMVALDArKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:TIGR02769 100 AVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRS-EDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446515747 169 GAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-232 |
1.41e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.79 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE----NTNDMDT 75
Cdd:PRK13641 3 IKFENVD--YIYSPGTPMekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 VTLRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALDaRKFLHRYPKEMSGGQQQRIGVIR 153
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.12e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqFVQKKGQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13632 7 MIKVENVS--FSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQ-----IGLfpnmTIE-------ENITVVPRMLgwdkarcKQRAEELMDMVALDarKFLHRYPKEMSGGQQQR 148
Cdd:PRK13632 84 KIGIIFQNpdnqfIGA----TVEddiafglENKKVPPKKM-------KDIIDDLAKKVGME--DYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALkLGDRIAVFRQGRIVQCASPDEL 228
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
.
gi 446515747 229 L 229
Cdd:PRK13632 230 L 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
9.34e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.39 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:PRK13647 5 IEVEDLH--FRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQ----QIglFpNMTIEENITVVPRMLGWDKARCKQRAEELMDMValDARKFLHRYPKEMSGGQQQRIGVIRALAA 157
Cdd:PRK13647 81 VGLVFQdpddQV--F-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAV--RMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPdELLAKPA 233
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-227 |
1.83e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE-----NTNDmdt 75
Cdd:COG3845 5 ALELRGITKRF----G-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirSPRD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 vTLRRNIGYVIQQIGLFPNMTIEENItvvprMLGW--------DKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQ 147
Cdd:COG3845 77 -AIALGIGMVHQHFMLVPNLTVAENI-----VLGLeptkggrlDRKAARARIRELSERYGLDVD--PDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 148 RIGVIRALAADPPVLLMDEPFGAVDPinREViqNQFLDMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGRIVQCAS 224
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTP--QEA--DELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
...
gi 446515747 225 PDE 227
Cdd:COG3845 225 TAE 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
1.89e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 122.71 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03246 1 LEVENVS--FRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENItvvprmlgwdkarckqraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMqRKLKKTVMLVSHDIdEALKLGDRIAVFRQGRI 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-220 |
2.84e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.14 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTkqFVQKKGQplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDtvtLRRNIG 83
Cdd:cd03226 2 IENIS--FSYKKGT--EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQQIG--LFPNmTIEENITVVPRmlgwDKARCKQRAEELMDMVALDARKFLHryPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03226 75 YVMQDVDyqLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERH--PLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
6.31e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 123.66 E-value: 6.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL 78
Cdd:COG1101 1 MLELKNLSKTF--NPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQ--QIGLFPNMTIEENITVV-----PRMLGWdkARCKQRAEELMDMVA---------LDAR-KFLhrypkem 141
Cdd:COG1101 79 AKYIGRVFQdpMMGTAPSMTIEENLALAyrrgkRRGLRR--GLTKKRRELFRELLAtlglglenrLDTKvGLL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 142 SGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIqnqfLDMQRKL----KKTVMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALV----LELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
...
gi 446515747 218 RIV 220
Cdd:COG1101 226 RII 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-231 |
7.17e-33 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 123.11 E-value: 7.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03253 1 IEFENVTFAYDPGR----PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITvvprmLGWDKArckqrAEELMDMVALDAR--KFLHRYPK-----------EMSGGQQQR 148
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIR-----YGRPDA-----TDEEVIEAAKAAQihDKIMRFPDgydtivgerglKLSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDEL 228
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
...
gi 446515747 229 LAK 231
Cdd:cd03253 223 LAK 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
8.53e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.53 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTlRRN 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKA--DAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-230 |
8.76e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 123.08 E-value: 8.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 5 ENLTKQFvqkKGQplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntnDMDTVTL----RR 80
Cdd:PRK10895 7 KNLAKAY---KGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE---DISLLPLharaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRML-GWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLR--DSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 160 PVLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-231 |
1.52e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.27 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQ-KKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV-TL 78
Cdd:PRK13633 4 MIKCKNVSYKYESnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQiglfPNMTI-----EENITVVPRMLGWDKARCKQRAEELMDMVAL-DARKFLhryPKEMSGGQQQRIGVI 152
Cdd:PRK13633 84 RNKAGMVFQN----PDNQIvativEEDVAFGPENLGIPPEEIRERVDESLKKVGMyEYRRHA---PHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
1.54e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 119.84 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE-----NTNDMdtv 76
Cdd:cd03216 1 LELRGITKRF----G-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfaSPRDA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 tLRRNIGYVIQqiglfpnmtieenitvvprmlgwdkarckqraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALA 156
Cdd:cd03216 73 -RRAGIAMVYQ-----------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 157 ADPPVLLMDEPFGAVDPinREViqNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03216 99 RNARLLILDEPTAALTP--AEV--ERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
2.68e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 122.43 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqpLKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLI----APSS-----GNIlINGENTN 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGShiellGRT-VQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 72 DMDTVTLRRNIGYVIQQIGLFPNMTIEENITV-----VP---RMLGWDKARCKQRAEELMDMVALdaRKFLHRYPKEMSG 143
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgsTPfwrTCFSWFTREQKQRALQALTRVGM--VHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-228 |
3.61e-32 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 120.71 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-RRNIGYVIQQIGLFPNMTIEE 99
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItvvprMLGWD--KARCKQRAEELMDMV-ALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPinr 176
Cdd:TIGR03410 95 NL-----LTGLAalPRRSRKIPDEIYELFpVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP--- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 177 EVIQnqflDMQRKLKK-------TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:TIGR03410 165 SIIK----DIGRVIRRlraeggmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
3.77e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.34 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:COG4604 1 MIEIKNVSKRYGGKV-----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEEnitVV-----PRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRAL 155
Cdd:COG4604 76 RLAILRQENHINSRLTVRE---LVafgrfPYSKGRLTAEDREIIDEAIAYLDLED--LADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 156 AADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-234 |
7.73e-32 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 127.17 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPlKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:TIGR01846 456 ITFENIR--FRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENItvvprmlgwdkARCKQRA--EELMDMVAL-DARKFLHRYPK-----------EMSGGQQQ 147
Cdd:TIGR01846 533 MGVVLQENVLF-SRSIRDNI-----------ALCNPGApfEHVIHAAKLaGAHDFISELPQgyntevgekgaNLSGGQRQ 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIDeALKLGDRIAVFRQGRIVQCASPDE 227
Cdd:TIGR01846 601 RIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEE 677
|
....*..
gi 446515747 228 LLAKPAN 234
Cdd:TIGR01846 678 LLALQGL 684
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-231 |
7.80e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 126.61 E-value: 7.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEEN 100
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLF-NRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ITVvprmlgwdkARCKQRAEELMD-MVALDARKFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:PRK13657 429 IRV---------GRPDATDEEMRAaAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 169 GAVDpINREVIQNQFLDMQRKlKKTVMLVSH---DIDEAlklgDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13657 500 SALD-VETEAKVKAALDELMK-GRTTFIIAHrlsTVRNA----DRILVFDNGRVVESGSFDELVAR 559
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-231 |
9.33e-32 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 125.97 E-value: 9.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQP--ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITVvprmlgwdkARCKQRAEELMDM-VALDARKFLHRYP-----------KEMSGGQQQRI 149
Cdd:TIGR02204 416 MALVPQDPVLFAA-SVMENIRY---------GRPDATDEEVEAAaRAAHAHEFISALPegydtylgergVTLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQnQFLD--MQrklKKTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDE 227
Cdd:TIGR02204 486 AIARAILKDAPILLLDEATSALDAESEQLVQ-QALEtlMK---GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAE 560
|
....
gi 446515747 228 LLAK 231
Cdd:TIGR02204 561 LIAK 564
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-230 |
1.62e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:PRK13635 6 IRVEHISFRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQ----QiglFPNMTIEENITV------VPR--MLgwdkarckQRAEELMDMVALDArkFLHRYPKEMSGGQQQRI 149
Cdd:PRK13635 83 VGMVFQnpdnQ---FVGATVQDDVAFglenigVPReeMV--------ERVDQALRQVGMED--FLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 150 GVIRALAADPPVLLMDEPFGAVDPINREviqnQFLDMQRKLKK----TVMLVSHDIDEALKlGDRIAVFRQGRIVQCASP 225
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRR----EVLETVRQLKEqkgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
....*
gi 446515747 226 DELLA 230
Cdd:PRK13635 225 EEIFK 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-232 |
4.09e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.10 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL---RRNIGYVIQQIGLFPNMTIEE 99
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NI-------TVVPRMLgwdkarckQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK11831 104 NVayplrehTQLPAPL--------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 173 PINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-225 |
6.79e-31 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 124.74 E-value: 6.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFvQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENT-NDMDTVtlRRNI 82
Cdd:TIGR01257 931 VKNLVKIF-EPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAV--RQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGLFPNMTIEENITVVPRMLG--WDKARCKQraEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGrsWEEAQLEM--EAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 161 VLLMDEPFGAVDPINREVIQNqfLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASP 225
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWD--LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-213 |
1.01e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 122.78 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NITVvpRMLGWDKARCKQRAE--ELMDMVAlDARKFLH----RYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:TIGR02857 415 NIRL--ARPDASDAEIREALEraGLDEFVA-ALPQGLDtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446515747 174 INreviQNQFLDMQRKLK--KTVMLVSHDiDEALKLGDRIAV 213
Cdd:TIGR02857 492 ET----EAEVLEALRALAqgRTVLLVTHR-LALAALADRIVV 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
1.03e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.10 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK09536 3 MIDVSDLS---VEFGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITV-----VPRMLGWDKArcKQRA-EELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRA 154
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEMgrtphRSRFDTWTET--DRAAvERAMERTGVAQ--FADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 155 LAADPPVLLMDEPFGAVDpINREViqnQFLDMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD-INHQV---RTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 446515747 232 P 232
Cdd:PRK09536 230 D 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.91e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILI----NGENTNDMDTV 76
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 T------------LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArKFLHRYPKEMS 142
Cdd:PRK13631 101 TnpyskkiknfkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD-SYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDmQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQC 222
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|.
gi 446515747 223 ASPDELLAKPA 233
Cdd:PRK13631 258 GTPYEIFTDQH 268
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-222 |
1.93e-30 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 116.09 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFV--QKKGQPLK---------------AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIL 64
Cdd:cd03220 1 IELENVSKSYPtyKGGSSSLKklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 65 INGentndmdTVTLRRNIGYviqqiGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGG 144
Cdd:cd03220 81 VRG-------RVSSLLGLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELG--DFIDLPVKTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQC 222
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-231 |
2.68e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.86 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNM 95
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF-SA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITvvprmLGWDKArckqRAEELMDMVA-------LDARKFLHRYPKE----MSGGQQQRIGVIRALAADPPVLLM 164
Cdd:PRK11160 429 TLRDNLL-----LAAPNA----SDEALIEVLQqvgleklLEDDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 165 DEPFGAVDP-INREVIQNQFLDMQrklKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK11160 500 DEPTEGLDAeTERQILELLAEHAQ---NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-249 |
2.93e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.12 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSG-----NILINGENT-NDMDTVTLR 79
Cdd:PRK14271 26 NLTLGFAGKT-----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPnMTIEENI-------TVVPRMLGWDKARCKQRAEELMDMValdaRKFLHRYPKEMSGGQQQRIGVI 152
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVlagvrahKLVPRKEFRGVAQARLTEVGLWDAV----KDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
250 260
....*....|....*....|.
gi 446515747 233 AN----EFVGSFVGQDRTLKR 249
Cdd:PRK14271 254 KHaetaRYVAGLSGDVKDAKR 274
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-229 |
4.79e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13548 2 MLEARNLS---VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGL-FPnMTIEEnitVVpRMLGWDKARCKQRAEELMD--MVALDARKFLHRYPKEMSGGQQQRIGVIRALA- 156
Cdd:PRK13548 77 RRAVLPQHSSLsFP-FTVEE---VV-AMGRAPHGLSRAEDDALVAaaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 157 -----ADPPVLLMDEPFGAVDPINreviQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDE 227
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 446515747 228 LL 229
Cdd:PRK13548 228 VL 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
5.05e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.44 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13652 3 LIETRDLCYSYSGSK----EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQ----QIGlfpNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK13652 79 FVGLVFQnpddQIF---SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLE--ELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
5.35e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.90 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSS-----GNILINGENTND--MD 74
Cdd:PRK14258 8 IKVNNLSFYYDTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-------DKARCKQRAEELMDMValdaRKFLHRYPKEMSGGQQQ 147
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrpkleidDIVESALKDADLWDEI----KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVF-----RQGRIVQC 222
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEF 237
|
250 260
....*....|....*....|....
gi 446515747 223 ASPDELLAKPAN----EFVGSFVG 242
Cdd:PRK14258 238 GLTKKIFNSPHDsrtrEYVLSRLG 261
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-238 |
8.53e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.85 E-value: 8.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT-LR 79
Cdd:PRK13644 1 MIRLENVSYSY--PDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGL-FPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:PRK13644 77 KLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE--KYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEaLKLGDRIAVFRQGRIVQCASPDELLAKPANEFVG 238
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-230 |
1.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13642 4 ILEVENLV--FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQI-GLFPNMTIEENITVVPRMLGWDKARCKQRAEELMdmVALDARKFLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEAL--LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDELLA 230
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-229 |
1.33e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.60 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNI----LINGENTNDMDTV 76
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKQRAEELMDMVALdARKFLHRYPKEMSGGQQQRIGVIRA 154
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL-ADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 155 LAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
1.58e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.77 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKkgQPLKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdtvtLRRNIG 83
Cdd:PRK11247 15 LNAVSKRYGER--TVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQQIGLFPNMTIEENITvvprmLGWdKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPVLL 163
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVG-----LGL-KGQWRDAALQALAAVGLADRA--NEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 164 MDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-231 |
1.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY--TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQI-GLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADP 159
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQD--FKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 160 PVLLMDEPFGAVDPINR-EVIQNqFLDMQRKLKKTVMLVSHDIDEaLKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKT-IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-229 |
2.53e-29 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 114.11 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 17 QPLkavdnvNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMT 96
Cdd:PRK10575 28 HPL------SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEEnITVVPR-----MLGWDKARCKQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK10575 102 VRE-LVAIGRypwhgALGRFGAADREKVEEAISLVGL--KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 172 DpINREV-----IQNqfLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK10575 179 D-IAHQVdvlalVHR--LSQERGL--TVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-220 |
4.67e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 115.36 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMD-TVTL---RRNIGYVIQQIGLFPNMTIEE 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkGICLppeKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NIT--VVPRMlgwdkarckqrAEELMDMVA-LDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PIN 175
Cdd:PRK11144 96 NLRygMAKSM-----------VAQFDKIVAlLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446515747 176 REVIqnQFLDmqrKLKKTV---ML-VSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:PRK11144 165 RELL--PYLE---RLAREInipILyVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-220 |
4.89e-29 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 110.87 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvTLRRN 81
Cdd:cd03247 1 LSINNVSFSY---PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENItvvprmlgwdkarckqraeelmdmvaldARKFlhrypkemSGGQQQRIGVIRALAADPPV 161
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNL----------------------------GRRF--------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGRIV 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKII 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
8.31e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 110.60 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN-IGYVI---QQIGLFPNM 95
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITVvPRMLgwdkarckqraeelmdmvaldarkflhrypkemSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:cd03215 94 SVAENIAL-SSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446515747 176 REVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-221 |
1.64e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKG------QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENtndMD 74
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR---ID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 75 TVT------LRRNIGYVIQQ--IGLFPNMTIEENIT---VVPRMLGWDKARckQRAEELMDMVALDARKFLhRYPKEMSG 143
Cdd:PRK10261 390 TLSpgklqaLRRDIQFIFQDpyASLDPRQTVGDSIMeplRVHGLLPGKAAA--ARVAWLLERVGLLPEHAW-RYPHEFSG 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-221 |
2.44e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.68 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQFvqKKGQPLKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT---LR-R 80
Cdd:PRK11629 10 NLCKRY--QEGSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVvPRMLGWDK-ARCKQRAEELMDMVALDARKFlHRyPKEMSGGQQQRIGVIRALAADP 159
Cdd:PRK11629 88 KLGFIYQFHHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLAAVGLEHRAN-HR-PSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 160 PVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGRIVQ 221
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
2.80e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.35 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM---DTVT 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVAL-DARKflhRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLlDKAK---NFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRkLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
3.34e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 111.32 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQF----VQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV 76
Cdd:PRK10419 3 LLNVSGLSHHYahggLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 ---TLRRNIGYVIQQ-IGLF-PNMTIEENITVVPR-MLGWDKARCKQRAEELMDMVALDArKFLHRYPKEMSGGQQQRIG 150
Cdd:PRK10419 83 qrkAFRRDIQMVFQDsISAVnPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDD-SVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 151 VIRALAADPPVLLMDEpfgAVDPINReVIQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:PRK10419 162 LARALAVEPKLLILDE---AVSNLDL-VLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-232 |
7.65e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.59 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQFVQKKG-----QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT--- 77
Cdd:PRK11308 10 DLKKHYPVKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQ--IGLFPNMTI----EENITVVPRMlgwDKARCKQRAEELMDMVALDArKFLHRYPKEMSGGQQQRIGV 151
Cdd:PRK11308 90 LRQKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSL---SAAERREKALAMMAKVGLRP-EHYDRYPHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
.
gi 446515747 232 P 232
Cdd:PRK11308 246 P 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
1.53e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFV--QKKGQPLK---------------AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNI 63
Cdd:COG1134 4 MIEVENVSKSYRlyHEPSRSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 64 LINGEntndmdtvtlrrnIGYVIQ-QIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLH----RYp 138
Cdd:COG1134 84 EVNGR-------------VSALLElGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELG--DFIDqpvkTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 139 kemSGGQQQRIGVIRALAADPPVLLMDEPFGAVDpinrEVIQNQFLD-MQRKLK--KTVMLVSHDIDEALKLGDRIAVFR 215
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGD----AAFQKKCLArIRELREsgRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|....*.
gi 446515747 216 QGRIVQCASPDELLAK 231
Cdd:COG1134 221 KGRLVMDGDPEEVIAA 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-231 |
1.57e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 113.69 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqfVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG4618 331 LSVENLT---VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITvvpRMLGWDKARCKQ--RAEELMDMVAldarkflhRYPK-----------EMSGGQQQR 148
Cdd:COG4618 408 IGYLPQDVELFDG-TIAENIA---RFGDADPEKVVAaaKLAGVHEMIL--------RLPDgydtrigeggaRLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINrEVIQNQFLDMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEG-EAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
...
gi 446515747 229 LAK 231
Cdd:COG4618 554 LAR 556
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
2.34e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE--NTNDMDTVTLRRNIGYVIQQIG--LFPNmT 96
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVGIVFQNPDdqLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEG--FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 177 EVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
2.77e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.67 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:PRK10535 4 LLELKDIRRSY-PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 --RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR--VEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNqFLDMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGRIV 220
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-200 |
3.96e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 112.45 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEEN 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ITVvprmlgwdkARCKQRAEELMDMValdARKFLHRYPKEM---------------SGGQQQRIGVIRALAADPPVLLMD 165
Cdd:TIGR02868 429 LRL---------ARPDATDEELWAAL---ERVGLADWLRALpdgldtvlgeggarlSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 446515747 166 EPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHD 200
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-230 |
5.66e-27 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 112.53 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItvvprMLGwdkARCKQRAEELMDMVAL-----DARKFLHRYPKEM-------SGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:TIGR01193 567 NL-----LLG---AKENVSQDEIWAACEIaeikdDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 168 FGAVDPINREVIQNQFLDMQrklKKTVMLVSHDIDEAlKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
1.06e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.50 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV-TLR 79
Cdd:PRK11614 5 MLSFDKVSAHYGK-----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITvvprMLGW--DKARCKQRAEELMDMVA-LDARKflHRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLA----MGGFfaERDQFQERIKWVYELFPrLHERR--IQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 157 ADPPVLLMDEPFGAVDPInreVIQnQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPI---IIQ-QIFDTIEQLREqgmTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-211 |
1.26e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.02 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGQpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDT---VT 77
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LR-RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARkfLHRYPKEMSGGQQQRIGVIRALA 156
Cdd:PRK10584 85 LRaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKR--LDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 157 ADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRI 211
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-231 |
2.56e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 110.98 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQF---VqkkgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE--NTNDMDTv 76
Cdd:NF033858 267 IEARGLTMRFgdfT--------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 tlRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIgvirALA 156
Cdd:NF033858 338 --RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLAD--VADALPDSLPLGIRQRL----SLA 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 157 A----DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGRIVQCASPDELLAK 231
Cdd:NF033858 410 VavihKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAALVAA 487
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
3.79e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTlRRN 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA-----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVAL----DARKflhrypKEMSGGQQQRIGVIRALAA 157
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLeskaDARV------SDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 158 DPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-205 |
9.58e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 9.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingentndmdTVTLRRNIGYVIQQIGL---F 92
Cdd:NF040873 4 GRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 93 PnMTIEENITV--VPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:NF040873 71 P-LTVRDLVAMgrWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 446515747 171 VDPINREVIqNQFLDMQRKLKKTVMLVSHDIDEAL 205
Cdd:NF040873 150 LDAESRERI-IALLAEEHARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-228 |
1.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPL--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING-ENTND---MDT 75
Cdd:PRK13649 3 INLQNVS--YTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtLITSTsknKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 76 VTLRRNIGYVIQqiglFPNM-----TIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFlHRYPKEMSGGQQQRIG 150
Cdd:PRK13649 81 KQIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLF-EKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREviqnQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDE 227
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRK----ELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
.
gi 446515747 228 L 228
Cdd:PRK13649 232 I 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-231 |
1.53e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENI 101
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 102 TVVPRMLGWDKARCKQRAEELMDMVAldarkflhRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:TIGR01842 413 ARFGENADPEKIIEAAKLAGVHELIL--------RLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 171 VDPINREVIQNQFLDMQRKlKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-231 |
2.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE--NTNDMDTVTLRRNIGYVIQQIG--LFpNMT 96
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPDnqLF-SAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEENITVVPRMLGWDKARCKQRAEELMDMVALDARKflHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 177 EVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-231 |
2.79e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.41 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:PRK11176 342 IEFRNVTFTY-PGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITVvprmlgwdkARCKQRAEELMDMVALDAR--KFLHRYPK-----------EMSGGQQQR 148
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAY---------ARTEQYSREQIEEAARMAYamDFINKMDNgldtvigengvLLSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSH---DIDEAlklgDRIAVFRQGRIVQCASP 225
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHrlsTIEKA----DEILVVEDGEIVERGTH 562
|
....*.
gi 446515747 226 DELLAK 231
Cdd:PRK11176 563 AELLAQ 568
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
3.86e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 101.01 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGentndmdtvtlrrN 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENITvvprmlgWDKARCKQRAEELMDMVALDarKFLHRYPK-------E----MSGGQQQRIG 150
Cdd:cd03250 68 IAYVSQEPWIQ-NGTIRENIL-------FGKPFDEERYEKVIKACALE--PDLEILPDgdlteigEkginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDP-INREVIQNQFLDMqRKLKKTVMLVSHDIdEALKLGDRIAVFRQGR 218
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGL-LLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
7.72e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMD-TVTLR 79
Cdd:PRK09700 5 YISMAGIGKSF-----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITV----VPRMLG---WDKARCKQRAEELMDMVALdaRKFLHRYPKEMSGGQQQRIGVI 152
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIgrhlTKKVCGvniIDWREMRVRAAMMLLRVGL--KVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVdpINREV-----IQNQFldmqRKLKKTVMLVSHDIDEALKLGDRIAVFRQG-----RIVQC 222
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL--TNKEVdylflIMNQL----RKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSD 231
|
....*..
gi 446515747 223 ASPDELL 229
Cdd:PRK09700 232 VSNDDIV 238
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-254 |
9.09e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 101.70 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQfvqkKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTT----LKMINRLIAPSSGNILINGEntnDMDTVT 77
Cdd:PRK10418 5 IELRNIALQ----AAQPL--VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGK---PVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LR-RNIGYVIQ--QIGLFPNMTIEENITVVPRMLGwdKARCKQRAEELMDMVAL-DARKFLHRYPKEMSGGQQQRIGVIR 153
Cdd:PRK10418 76 LRgRKIATIMQnpRSAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 154 ALAADPPVLLMDEPFGAVDPinreVIQNQFLDMQRKLKKT----VMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDV----VAQARILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250 260
....*....|....*....|....*
gi 446515747 230 AKPANEFVGSFVGQDRTLKRLLLVS 254
Cdd:PRK10418 230 NAPKHAVTRSLVSAHLALYGMELAS 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-231 |
9.26e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--IAPSSGNILIN------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 67 ---GE-----------------NTNDMDTVTLRRNIGYVIQQ-IGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDM 125
Cdd:TIGR03269 76 skvGEpcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 126 VALDARkfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEAL 205
Cdd:TIGR03269 156 VQLSHR--ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*.
gi 446515747 206 KLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
1.88e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKG------QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIApSSGNILING---ENTN 71
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGqplHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 72 DMDTVTLRRNIGYVIQ--QIGLFPNMT----IEENITVVPRMLgwDKARCKQRAEELMDMVALDARKfLHRYPKEMSGGQ 145
Cdd:PRK15134 354 RRQLLPVRHRIQVVFQdpNSSLNPRLNvlqiIEEGLRVHQPTL--SAAQREQQVIAVMEEVGLDPET-RHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDpinrEVIQNQFLDMQRKLKKTVML----VSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSLQQKHQLaylfISHDLHVVRALCHQVIVLRQGEVVE 506
|
250
....*....|....*
gi 446515747 222 CASPDELLAKPANEF 236
Cdd:PRK15134 507 QGDCERVFAAPQQEY 521
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-232 |
2.01e-24 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 102.19 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG-WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 ---RRNIGYVIQQIGLFPNMTIE--ENI--TVVPRMLGWD-KARC-------KQRAEELMDMVAL-DARKFLHRYPKEMS 142
Cdd:PRK15093 81 rerRKLVGHNVSMIFQEPQSCLDpsERVgrQLMQNIPGWTyKGRWwqrfgwrKRRAIELLHRVGIkDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQC 222
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 446515747 223 ASPDELLAKP 232
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-222 |
6.20e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.50 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVqKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI---APSSGNILINGEntnDMDTVTLRR 80
Cdd:cd03234 6 WWDVGLKAK-NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDA--RKFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 159 PPVLLMDEPFGAVDPInrevIQNQFLDMQRKL---KKTVMLVSHDI-DEALKLGDRIAVFRQGRIVQC 222
Cdd:cd03234 162 PKVLILDEPTSGLDSF----TALNLVSTLSQLarrNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYS 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
9.06e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.48 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKkGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIaPS------SGNILINGENTNDMD 74
Cdd:PRK15134 5 LLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 75 TVTLRR----NIGYVIQQ--IGLFPNMTIEENITVV---PRMLGWDKARckqrAEEL--MDMVAL-DARKFLHRYPKEMS 142
Cdd:PRK15134 83 EQTLRGvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVlslHRGMRREAAR----GEILncLDRVGIrQAAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPinreVIQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250
....*....|....*...
gi 446515747 219 IVQCASPDELLAKPANEF 236
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPY 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-228 |
1.28e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 3 KLENLTkqfvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN- 81
Cdd:COG3845 259 EVENLS----VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVI---QQIGLFPNMTIEENITV----VPRMLGW---DKARCKQRAEELMDmvaldarKFLHRYP------KEMSGGQ 145
Cdd:COG3845 335 VAYIPedrLGRGLVPDMSVAENLILgryrRPPFSRGgflDRKAIRAFAEELIE-------EFDVRTPgpdtpaRSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 146 QQRIGVIRALAADPPVLLMDEP-----FGAVdpinrEVIQNQFLDMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPtrgldVGAI-----EFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
....*...
gi 446515747 221 QCASPDEL 228
Cdd:COG3845 482 GEVPAAEA 489
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-228 |
1.39e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTtlkMINRLI--APSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFP 93
Cdd:PRK11174 362 GKTL--AGPLNFTLPAGQRIALVGPSGAGKTS---LLNALLgfLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 94 NmTIEENITvvprmLGWDKARckqrAEELMDMVAL-DARKFLHRYPK-----------EMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK11174 437 G-TLRDNVL-----LGNPDAS----DEQLQQALENaWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFLDMQRklKKTVMLVSHDIDEaLKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
2.56e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.75 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDM-DTVTLR 79
Cdd:PRK11300 5 LLSVSGLMMRF-----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIGYVIQQIGLFPNMTIEENITVVP-RML------GWDKARCKQRAE-ELMDMVA--LDA---RKFLHRYPKEMSGGQQ 146
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLVAQhQQLktglfsGLLKTPAFRRAEsEALDRAAtwLERvglLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 147 QRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPD 226
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
....*.
gi 446515747 227 ELLAKP 232
Cdd:PRK11300 240 EIRNNP 245
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
16-232 |
2.75e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 101.56 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNm 95
Cdd:TIGR03796 491 EPPL--IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEG- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITVvprmlgWDKA-------RCKQRAEeLMDMVAldARKFLHRYP-----KEMSGGQQQRIGVIRALAADPPVLL 163
Cdd:TIGR03796 568 TVRDNLTL------WDPTipdadlvRACKDAA-IHDVIT--SRPGGYDAElaeggANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 164 MDEPFGAVDPINREVIqnqfLDMQRKLKKTVMLVSH------DIDEalklgdrIAVFRQGRIVQCASPDELLAKP 232
Cdd:TIGR03796 639 LDEATSALDPETEKII----DDNLRRRGCTCIIVAHrlstirDCDE-------IIVLERGKVVQRGTHEELWAVG 702
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-232 |
3.26e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 97.30 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:PRK11701 6 LLSVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 --RRNI-----GYVIQQI--GLFPNMTIEENITVVPRMLGWDK-ARCKQRAEELMDMVALDARKfLHRYPKEMSGGQQQR 148
Cdd:PRK11701 81 aeRRRLlrtewGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAAR-IDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFLDMQRKLKKT----VMLVSHDIDEALKLGDRIAVFRQGRIVQCA 223
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLD-----VsVQARLLDLLRGLVRElglaVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
....*....
gi 446515747 224 SPDELLAKP 232
Cdd:PRK11701 235 LTDQVLDDP 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-273 |
8.81e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 8.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNI-----LINGENT----- 70
Cdd:PRK10261 12 VLAVENLNIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 71 NDMDTVTLRR----NIGYVIQQ--IGLFPNMTIEENITVVPRM-LGWDKARCKQRAEELMDMVAL-DARKFLHRYPKEMS 142
Cdd:PRK10261 91 SEQSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPinreVIQNQFLD----MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQlikvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 219 IVQCASPDELLAKPANEF----------VGSFVGQDRTlKRLLLVSAGDVTDQQPTI---TARPSTPL 273
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYtrallaavpqLGAMKGLDYP-RRFPLISLEHPAKQEPPIeqdTVVDGEPI 313
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-229 |
1.03e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTIEENIT 102
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 103 --VVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDpINREVIQ 180
Cdd:PRK10253 104 rgRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-ISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446515747 181 NQFL-DMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK10253 183 LELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-203 |
1.30e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 NItVVPRMLGWDKARCKQRAEELMDMvALDaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVI 179
Cdd:PRK10247 100 NL-IFPWQIRNQQPDPAIFLDDLERF-ALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|....
gi 446515747 180 QNQFLDMQRKLKKTVMLVSHDIDE 203
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-228 |
2.75e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGE-----NTNDMdtvtLRRNIGYVI---QQIGL 91
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirSPRDA----IRAGIAYVPedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 92 FPNMTIEENIT--VVPRM--LGW-DKARCKQRAEELMDMVALdarkflhRYP------KEMSGGQQQRIgVI-RALAADP 159
Cdd:COG1129 342 VLDLSIRENITlaSLDRLsrGGLlDRRRERALAEEYIKRLRI-------KTPspeqpvGNLSGGNQQKV-VLaKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 160 PVLLMDEPFGAVDpIN--REVIQnqFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:COG1129 414 KVLILDEPTRGID-VGakAEIYR--LIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-220 |
3.42e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.00 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 5 ENLTKQFVQKKGQPLKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLIAPS-SGNILINGENtndMDTVTLRRN 81
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRP---LDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNMTIEENITVVprmlgwdkARCKQraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFA--------AKLRG-----------------------LSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 162 LLMDEPFGAVDPINreviQNQFLDMQRKLK---KTVMLVSHDI-DEALKLGDRIAVFRQGRIV 220
Cdd:cd03213 133 LFLDEPTSGLDSSS----ALQVMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-232 |
3.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGN---ILINGENTNDMDTVTLRRNIGYVIQQI-GLFPNMT 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEENITV------VPR--MLgwdkaRCKQRAEELMDMValdarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:PRK13640 102 VGDDVAFglenraVPRpeMI-----KIVRDVLADVGML-----DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 169 GAVDPINREviqnQFLDMQRKLKK----TVMLVSHDIDEAlKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK13640 172 SMLDPAGKE----QILKLIRKLKKknnlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-235 |
1.86e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKG----QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV 76
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRRNIGYVIQ--QIGLFPNMTIEEnITVVPRMLGWD---KARcKQRAEELMDMVALdARKFLHRYPKEMSGGQQQRIGV 151
Cdd:PRK15112 84 YRSQRIRMIFQdpSTSLNPRQRISQ-ILDFPLRLNTDlepEQR-EKQIIETLRQVGL-LPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
....
gi 446515747 232 PANE 235
Cdd:PRK15112 241 PLHE 244
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-232 |
1.98e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEENITv 103
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF-SGSVRENIA- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 vprmLGWDKArckQRAEELMDMVALDARKFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:TIGR00958 577 ----YGLTDT---PDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 173 pinreVIQNQFLDMQRKLK-KTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:TIGR00958 650 -----AECEQLLQESRSRAsRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-231 |
2.46e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 95.66 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEENIt 102
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF-NDTIAYNI- 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 103 vvprmlGWDKARCKQRA-EELMDMVALDArkFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:COG5265 453 ------AYGRPDASEEEvEAAARAAQIHD--FIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 171 VDPINREVIQNQFLDMQRklKKTVMLVSH---DIDEAlklgDRIAVFRQGRIVQCASPDELLAK 231
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAHrlsTIVDA----DEILVLEAGRIVERGTHAELLAQ 582
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-232 |
2.76e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.43 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPssgNILINGE--NTNDMDTVTL----- 78
Cdd:COG4170 8 NLTIEIDTPQG-RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHVTADrfRWNGIDLLKLsprer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 ----RRNIGYVIQ--QIGLFPNMTI----EENI---TVVPRMLGWDKARcKQRAEELMDMVAL-DARKFLHRYPKEMSGG 144
Cdd:COG4170 84 rkiiGREIAMIFQepSSCLDPSAKIgdqlIEAIpswTFKGKWWQRFKWR-KKRAIELLHRVGIkDHKDIMNSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINreviQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFRLLARLNQlqgtSILLISHDLESISQWADTITVLYCGQTV 238
|
250
....*....|..
gi 446515747 221 QCASPDELLAKP 232
Cdd:COG4170 239 ESGPTEQILKSP 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-244 |
3.73e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.59 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV-TLRRNIGYVIQQIGLFPNMTIE 98
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 99 ENITV--VPRMLGW-DKARCKQRAEELMDMVALD---ARKFlhrypKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK11288 98 ENLYLgqLPHKGGIvNRRLLNYEAREQLEHLGVDidpDTPL-----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 173 piNREvIQNQF--LDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVqcASPDELLAKPANEFVGSFVGQD 244
Cdd:PRK11288 173 --ARE-IEQLFrvIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV--ATFDDMAQVDRDQLVQAMVGRE 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-231 |
6.21e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 37 LLGPSGCGKTTTLKMINRLIAPSSGNILINGE--NTNDMDTVTLRRNIGYVIQQiglfPNMTI-----EENITVVPRMLG 109
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD----PEQQIfytdiDSDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 110 WDKARCKQRAEELMDMValDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINReviqNQFLDMQRK 189
Cdd:PRK13638 108 VPEAEITRRVDEALTLV--DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR----TQMIAIIRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446515747 190 L---KKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:PRK13638 182 IvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-232 |
1.37e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 89.89 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTL-- 78
Cdd:TIGR02323 3 LLQVSGLSKSY-----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 -------RRNIGYVIQQI--GLFPNMTIEENITVVPRMLGWDK-ARCKQRAEELMDMVALDARKfLHRYPKEMSGGQQQR 148
Cdd:TIGR02323 78 aerrrlmRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDPTR-IDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPinreVIQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGRIVQCAS 224
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRdlglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
....*...
gi 446515747 225 PDELLAKP 232
Cdd:TIGR02323 233 TDQVLDDP 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-231 |
4.43e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.11 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKminrLIA----PSSGNILINGentNDMDTVTLRRN----IGYVIQQIG-- 90
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLS----LIAgarkIQQGRVEVLG---GDMADARHRRAvcprIAYMPQGLGkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 91 LFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:NF033858 89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 171 VDPINReviqNQFLDMQRKLKK-----TVMLVSHDIDEALKLgDRIAVFRQGRIVQCASPDELLAK 231
Cdd:NF033858 167 VDPLSR----RQFWELIDRIRAerpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-200 |
6.97e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFvqkKGQPLkaVDNVNLNVPEGEmCV-LLGPSGCGKTTTLKMINRLIAPSSGNILINGENTndmdtvtlrrnI 82
Cdd:COG0488 1 LENLSKSF---GGRPL--LDDVSLSINPGD-RIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-----------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGLFPNMTIEENI-TVVPRMlgWDKARCKQRAEELMDMVALDARKF---------------------------- 133
Cdd:COG0488 64 GYLPQEPPLDDDLTVLDTVlDGDAEL--RALEAELEELEAKLAEPDEDLERLaelqeefealggweaearaeeilsglgf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 134 ----LHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPfgavdpinreviQNqFLDMQ---------RKLKKTVMLVSHD 200
Cdd:COG0488 142 peedLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP------------TN-HLDLEsiewleeflKNYPGTVLVVSHD 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-173 |
2.50e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.10 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMdTVTLRRNIGYVIQQIGLFPNMTIEENITV 103
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLPGLKPELSALENLHF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 VPRMLGWDKARCkqraEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:TIGR01189 97 WAAIHGGAQRTI----EDALAAVGLTG--FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-219 |
3.58e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.22 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENItv 103
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDNI-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 vprmlgwdkARCKQRAEELMDMVALD---ARKFLHRYPKE-----------MSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:cd03248 109 ---------AYGLQSCSFECVKEAAQkahAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446515747 170 AVDPINREVIQNQFLDMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGRI 219
Cdd:cd03248 180 ALDAESEQQVQQALYDWPE--RRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
4.16e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKGqPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI----APSSGNILINGENTNDMDTV 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESA-PFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 77 TLRRNIGYVIQQIGLFPNMTIEENITVVPRML-------GWDKARCKQRAEELMDMVAL-DARKFLHRYPKEMSGGQQQR 148
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMeaikvhqGGNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....
gi 446515747 229 LAKP 232
Cdd:PRK11022 242 FRAP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
6.16e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQP-LKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMdTVTLR 79
Cdd:PRK15439 11 LLCARSISKQY---SGVEvLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 80 RNIG-YVI-QQIGLFPNMTIEENITV-VPRMLGwDKARCKQRAEELMDMVALDARKFLhrypkeMSGGQQQRIGVIRALA 156
Cdd:PRK15439 84 HQLGiYLVpQEPLLFPNLSVKENILFgLPKRQA-SMQKMKQLLAALGCQLDLDSSAGS------LEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 157 ADPPVLLMDEPFGAVDPINREviqNQFLDMQRKLKKTVMLV--SHDIDEALKLGDRIAVFRQGRIV 220
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETE---RLFSRIRELLAQGVGIVfiSHKLPEIRQLADRISVMRDGTIA 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-220 |
1.10e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILInGENTndmdtvtlrr 80
Cdd:COG0488 315 VLELEGLSKSY---GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQ-QIGLFPNMTIEENItvvprmlgWDKARcKQRAEELMDMVAldarKFL------HRYPKEMSGGQQQRIGVIR 153
Cdd:COG0488 379 KIGYFDQhQEELDPDKTVLDEL--------RDGAP-GGTEQEVRGYLG----RFLfsgddaFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 154 ALAADPPVLLMDEPFGAVDPINREVIqNQFLDmqrKLKKTVMLVSHD---IDealKLGDRIAVFRQGRIV 220
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEAL-EEALD---DFPGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-217 |
3.02e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 82.76 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 16 GQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSG-----NILINGENTNDMDTVTlRRNIGYVIQQIG 90
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRN-RYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 91 LFpNMTIEENITvvprmlgWDKARCKQRAEELMDMVALDARKFLHRYPKE---------MSGGQQQRIGVIRALAADPPV 161
Cdd:cd03290 90 LL-NATVEENIT-------FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQteigerginLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 162 LLMDEPFGAVD-PINREVIQNQFLDMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:cd03290 162 VFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-222 |
3.05e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.99 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEN--TNDMDtvtL 78
Cdd:TIGR01257 1937 ILRLNELTKVY---SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNISD---V 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSL--YADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIvQC 222
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF-QC 2150
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
262-363 |
5.65e-18 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 78.83 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 262 QPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGI--------CADITHPFRITGKAEDNLRIV 333
Cdd:cd02205 2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEgglaldtpVAEVMTPDVITVSPDTDLEEA 81
|
90 100 110
....*....|....*....|....*....|
gi 446515747 334 LSRLYESNTSWMPIVDEDGRYNGEISQDYI 363
Cdd:cd02205 82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-199 |
7.00e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.15 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 17 QPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTnDMDTVTLRRNIGYVIQQIGLFPNMT 96
Cdd:PRK13540 14 QPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEENItvvprmlgWDKARCKQRAEELMDMVALDARKFLHRYP-KEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:PRK13540 91 LRENC--------LYDIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 446515747 176 REVIQNQfLDMQRKLKKTVMLVSH 199
Cdd:PRK13540 163 LLTIITK-IQEHRAKGGAVLLTSH 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-230 |
7.74e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 59 SSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFpNMTIEENITVVPRMLGWD--KARCKQRA-EELMDMVALDARKFLH 135
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREdvKRACKFAAiDEFIESLPNKYDTNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 136 RYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIdEALKLGDRIAVF- 214
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFn 1432
|
170 180
....*....|....*....|
gi 446515747 215 ---RQGRIVQC-ASPDELLA 230
Cdd:PTZ00265 1433 npdRTGSFVQAhGTHEELLS 1452
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-221 |
8.22e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEN-TNDMDTVTLRRNIGYVIQ---QIGLFPNM 95
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLDAVKKGMAYITEsrrDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 96 TIEENITVVP--RMLGW-------DKARCKQRAEELMDMVALDARKfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PRK09700 357 SIAQNMAISRslKDGGYkgamglfHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 167 PFGAVDPINREVIQNqfldMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGRIVQ 221
Cdd:PRK09700 436 PTRGIDVGAKAEIYK----VMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-225 |
1.06e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 81.00 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqKKGQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03244 3 IEFKNVSLRY--RPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITvvPrmLG-------WD---KARCKQRAEELMDmvALDARkfLHRYPKEMSGGQQQRIGV 151
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLD--P--FGeysdeelWQaleRVGLKEFVESLPG--GLDTV--VEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 152 IRALAADPPVLLMDEPFGAVDPIN----REVIQNQFLDmqrklkKTVMLVSHDIDEALKLgDRIAVFRQGRIVQCASP 225
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETdaliQKTIREAFKD------CTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK13648 7 IIVFKNVSFQY---QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NIGYVIQQ---------------IGLFPNMTIEENI-TVVPRMLgwdkarckqraeELMDMvaLDARKFlhrYPKEMSGG 144
Cdd:PRK13648 84 HIGIVFQNpdnqfvgsivkydvaFGLENHAVPYDEMhRRVSEAL------------KQVDM--LERADY---EPNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREviqnQFLDMQRKLKK----TVMLVSHDIDEALKlGDRIAVFRQGRIV 220
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQ----NLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVY 221
|
250
....*....|.
gi 446515747 221 QCASPDELLAK 231
Cdd:PRK13648 222 KEGTPTEIFDH 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.15e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntndmdtvtLRr 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR-----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 nIGYVIQQIGLFPNM--TIEENITVVPRMlgwdkarckQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAAD 158
Cdd:PRK09544 69 -IGYVPQKLYLDTTLplTVNRFLRLRPGT---------KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 159 PPVLLMDEPFGAVDpINREVIQNQFLD-MQRKLKKTVMLVSHDI-------DEALKLGDRI 211
Cdd:PRK09544 139 PQLLVLDEPTQGVD-VNGQVALYDLIDqLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
2.08e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.26 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingentndmdTVTLRRN 81
Cdd:cd03221 1 IELENLSKTY---GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQqiglfpnmtieenitvvprmlgwdkarckqraeelmdmvaldarkflhrypkeMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03221 65 IGYFEQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 162 LLMDEPFGAVDPINREVIQNQFldmqRKLKKTVMLVSHD---IDealKLGDRIAVFRQGR 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDryfLD---QVATKIIELEDGK 144
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-216 |
3.45e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDtvtLRRNIGYVIQQIGLFPNMTIEENITV 103
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 VPRMLGWDKArckqRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQf 183
Cdd:PRK13539 97 WAAFLGGEEL----DIAAALEAVGLAP--LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL- 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 446515747 184 ldMQRKLKK--TVMLVSH---DIDEALKLgdRIAVFRQ 216
Cdd:PRK13539 170 --IRAHLAQggIVIAATHiplGLPGAREL--DLGPFAA 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
4.28e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlIAPS---SGNILINGE-----NTND 72
Cdd:PRK13549 5 LLEMKNITKTF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEelqasNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 73 mdtvTLRRNIGYVIQQIGLFPNMTIEENI------TVVPRMlgwDKARCKQRAEELMDMVALD---ARKFlhrypKEMSG 143
Cdd:PRK13549 79 ----TERAGIAIIHQELALVKELSVLENIflgneiTPGGIM---DYDAMYLRAQKLLAQLKLDinpATPV-----GNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIqnqfLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVL----LDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-172 |
1.04e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEnTNDMDTVTLRRNIGYVIQQIGLFPNMTIEENITVv 104
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 105 prmlgWDKARCKQRAEELMDMVALDArkFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:cd03231 97 -----WHADHSDEQVEEALARVGLNG--FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.65e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlIAPS---SGNILINGE-----NTND 72
Cdd:TIGR02633 1 LLEMKGIVKTF-----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSplkasNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 73 mdtvTLRRNIGYVIQQIGLFPNMTIEENITV-------VPRMlgwDKARCKQRAEELMDMVALDARKfLHRYPKEMSGGQ 145
Cdd:TIGR02633 75 ----TERAGIVIIHQELTLVPELSVAENIFLgneitlpGGRM---AYNAMYLRAKNLLRELQLDADN-VTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMlVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVY-ISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-201 |
2.49e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDmdtvTLRRN-IGYVIQQIGL---FPNMT 96
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAYVPQSEEVdwsFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 ieENITVVPRM--LGW---DKARCKQRAEELMDMValDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK15056 98 --EDVVMMGRYghMGWlrrAKKRDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|...
gi 446515747 172 DpINREViqnQFLDMQRKLK---KTVMLVSHDI 201
Cdd:PRK15056 174 D-VKTEA---RIISLLRELRdegKTMLVSTHNL 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-236 |
3.36e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 77.45 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 31 EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIngentnDMDTVTlrrnigYVIQQIGLFPNMTIEENITVVPRMLGW 110
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------ELDTVS------YKPQYIKADYEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 111 DkarcKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIqNQFLDm 186
Cdd:cd03237 92 H----PYFKTEIAKPLQIE--QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVI-RRFAE- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446515747 187 qrKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQC-ASPDELLAKPANEF 236
Cdd:cd03237 164 --NNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGvANPPQSLRSGMNRF 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-233 |
4.82e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.23 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPS---SGNILINGENTNDMDTVTLRR----NIGYVIQQ--IGL 91
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 92 FPNMTIEENITVVpRML--GWDKARCKQRAEELMDMVAL-DARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:PRK09473 111 NPYMRVGEQLMEV-LMLhkGMSKAEAFEESVRMLDAVKMpEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 169 GAVDPinreVIQNQFLDMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPA 233
Cdd:PRK09473 190 TALDV----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-232 |
4.86e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEEN 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ITvvprmLGWDKARcKQRAEELMDM--VALDARKFLHRYPKE-------MSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK10789 409 IA-----LGRPDAT-QQEIEHVARLasVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 172 D-PINREVIQNqfLDMQRKlKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:PRK10789 483 DgRTEHQILHN--LRQWGE-GRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-229 |
5.71e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 31 EGEMCVLLGPSGCGKTTTLKMINRLIAPS---SGNILINGENtndMDTVTLRRNIGYVIQQIGLFPNMTIEENITV---- 103
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMP---IDAKEMRAISAYVQQDDLFIPTLTVREHLMFqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 -VPRMLGWDKARckQRAEELMDMVAL-DARKFLHRYP---KEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN-RE 177
Cdd:TIGR00955 127 rMPRRVTKKEKR--ERVDEVLQALGLrKCANTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMaYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446515747 178 VIQnQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:TIGR00955 205 VVQ-VLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
1.29e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.08 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQkkgqpLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTlKMINRLIAPSSGNILINGEnTNDMDTVTLRRN 81
Cdd:NF000106 14 VEVRGLVKHFGE-----VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*-TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IG-YVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPP 160
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLT--EAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 161 VLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAK 231
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-229 |
2.08e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 32 GEMCVLLGPSGCGKTTTLKMINRLIaPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTIEENITvvprMLGWD 111
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLT----LHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 112 KARCKQRA---EELMDMVALDarKFLHRYPKEMSGGQQQRI---GVI----RALAADPPVLLMDEPFGAVDpINREVIQN 181
Cdd:PRK03695 97 KTRTEAVAsalNEVAEALGLD--DKLGRSVNQLSGGEWQRVrlaAVVlqvwPDINPAGQLLLLDEPMNSLD-VAQQAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446515747 182 QFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-219 |
2.52e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 12 VQKKGQPLKAVD--------NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVT-LRRNI 82
Cdd:PRK15439 261 QQAAGAPVLTVEdltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVI---QQIGLFPNMTIEENIT--VVPRMLGWdkarcKQRAEElmdmvaldaRKFLHRYPKEM--------------SG 143
Cdd:PRK15439 341 VYLPedrQSSGLYLDAPLAWNVCalTHNRRGFW-----IKPARE---------NAVLERYRRALnikfnhaeqaartlSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPINReviqNQFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK15439 407 GNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR----NDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-199 |
5.49e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.19 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIngentndmdtvTLRRN 81
Cdd:cd03223 1 IELENLS--LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQiGLFPNMTIEENITvvprmlgwdkarckqraeelmdmvaldarkflhrYP--KEMSGGQQQRIGVIRALAADP 159
Cdd:cd03223 66 LLFLPQR-PYLPLGTLREQLI----------------------------------YPwdDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446515747 160 PVLLMDEPFGAVDPinrEViQNQFLDMQRKLKKTVMLVSH 199
Cdd:cd03223 111 KFVFLDEATSALDE---ES-EDRLYQLLKELGITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-230 |
5.94e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.99 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpnmtieenitvvPRMLGWDKARCKQRAEELMDM------VALDARKFLHRypkEMSGGQQQRIGVIRAL 155
Cdd:COG4615 408 FSAVFSDFHLF------------DRLLGLDGEADPARARELLERleldhkVSVEDGRFSTT---DLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 156 AADPPVLLMDEpFGA-VDPINREVIQNQFLDMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:COG4615 473 LEDRPILVFDE-WAAdQDPEFRRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAALAA 546
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-233 |
6.38e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLIAPS-------SGNILINGENTNDMDTVTLRRNIGYVIQQ----- 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 89 ---------IGLFPNMTIEENITVVPRMLGWdkarckqRAEELMDMVALDARKFlhrypKEMSGGQQQRIGVIRALA--- 156
Cdd:PRK13547 97 afsareivlLGRYPHARRAGALTHRDGEIAW-------QALALAGATALVGRDV-----TTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 157 ------ADPPVLLMDEPFGAVDPINreviQNQFLDMQRKLKKT----VMLVSHDIDEALKLGDRIAVFRQGRIVQCASPD 226
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAH----QHRLLDTVRRLARDwnlgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....*..
gi 446515747 227 ELLaKPA 233
Cdd:PRK13547 241 DVL-TPA 246
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-220 |
6.57e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 72.68 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 11 FVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPS---SGNILINGeNTNDMDTVTLRRNIGYVIQ 87
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG-IPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 88 QIGLFPNMTIEENITVVPRMLGwdkarckqraeelmdmvaldarkflHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446515747 168 FGAVDPINREVIQNQFLDMQRKLKKTVML-VSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-221 |
9.53e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlIAPS---SGNILINGE-----NTNDMDtvt 77
Cdd:NF040905 6 GITKTF-----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEvcrfkDIRDSE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 lrrNIGYVI--QQIGLFPNMTIEENItvvprMLG----------WDKARckQRAEELMDMVALDARkflhryP----KEM 141
Cdd:NF040905 77 ---ALGIVIihQELALIPYLSIAENI-----FLGnerakrgvidWNETN--RRARELLAKVGLDES------PdtlvTDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 142 SGGQQQRIGVIRALAADPPVLLMDEPFGAvdpINREVIQNqFLDMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAA---LNEEDSAA-LLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGR 216
|
...
gi 446515747 219 IVQ 221
Cdd:NF040905 217 TIE 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-223 |
1.21e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFvqkkgqP-LKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTN-DMDTVTL 78
Cdd:PRK10762 4 LLQLKGIDKAF------PgVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 79 RRNIGYVIQQIGLFPNMTIEENI----TVVPRMLGWDKARCKQRAEELmdMVALDARKFLHRYPKEMSGGQQQRIGVIRA 154
Cdd:PRK10762 78 EAGIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 155 LAADPPVLLMDEPFGAVDPINRE----VIqnqfldmqRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGR-IVQCA 223
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETEslfrVI--------RELKSQgrgIVYISHRLKEIFEICDDVTVFRDGQfIAERE 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-199 |
3.62e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTkqfVQK-KGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMIN--------RLIAPSSGNIL------- 64
Cdd:COG4178 362 ALALEDLT---LRTpDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLflpqrpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 65 -INGentndmdtvTLRRNIGYviqqiglfPNmtIEENITvvprmlgwdkarcKQRAEELMDMVALDArkFLHRY------ 137
Cdd:COG4178 437 lPLG---------TLREALLY--------PA--TAEAFS-------------DAELREALEAVGLGH--LAERLdeeadw 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515747 138 PKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINreviQNQFLDM-QRKLKK-TVMLVSH 199
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALYQLlREELPGtTVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-199 |
3.93e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIN-GENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENIT 102
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 103 VVPRML-------------GWD-----------KARCKQRAEELM---------------------DMVALDARKFLHRY 137
Cdd:PTZ00265 482 YSLYSLkdlealsnyynedGNDsqenknkrnscRAKCAGDLNDMSnttdsneliemrknyqtikdsEVVDVSKKVLIHDF 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 138 ---------------PKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSH 199
Cdd:PTZ00265 562 vsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-240 |
5.89e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.39 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQF---------------VQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIN 66
Cdd:PRK13546 5 VNIKNVTKEYriyrtnkermkdaliPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 67 GEntndmdtvtlrrnIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQ 146
Cdd:PRK13546 85 GE-------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELG--EFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 147 QRIGVIRALAADPPVLLMDEPFGAVDpinrEVIQNQFLDMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGRIVQCA 223
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGD----QTFAQKCLDKIYEFKeqnKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
250
....*....|....*..
gi 446515747 224 SPDELLAKpANEFVGSF 240
Cdd:PRK13546 226 ELDDVLPK-YEAFLNDF 241
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-225 |
6.43e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.13 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLK---NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITVVPRmlgwdkarckQRAEELMDMVALdarkflhrypKE----MSGGQQQRIGVIRALAA 157
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDE----------YSDEEIYGALRV----------SEgglnLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 158 DPPVLLMDEPFGAVDPIN----REVIQNQFLDmqrklkKTVMLVSHDIDEALKLgDRIAVFRQGRIVQCASP 225
Cdd:cd03369 143 RPRVLVLDEATASIDYATdaliQKTIREEFTN------STILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-234 |
6.85e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIaPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 102 TV-VPRMLgwDKARCKQRAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRAL-----AADPP--VLLMDEPFGAVDp 173
Cdd:COG4138 91 ALhQPAGA--SSEAVEQLLAQLAEALGLE--DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 174 inreVIQNQFLDmqRKLKK------TVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLaKPAN 234
Cdd:COG4138 166 ----VAQQAALD--RLLRElcqqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-205 |
1.19e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI--APSSGNIlingentndmdtvtlrrnigyVIQQIGLFPNMTIEEN 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------------------DVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ItvvprmlgwDKARCKQRAEELMDMVAL-DARKFLHRYpKEMSGGQQQRIGVIRALAADPPVLLMDEpFGAV-DPINREV 178
Cdd:COG2401 106 I---------GRKGDFKDAVELLNAVGLsDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDE-FCSHlDRQTAKR 174
|
170 180
....*....|....*....|....*....
gi 446515747 179 IQNQFLDMQRKLKKTVMLVSH--DIDEAL 205
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHhyDVIDDL 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-231 |
2.15e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.90 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPlKAVDNVNLNVPEGEMCVLLGPSGCGKTTtlkMINRLIApssgnilingentnDMDT----VT 77
Cdd:TIGR00957 637 ITVHNAT--FTWARDLP-PTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLA--------------EMDKveghVH 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 78 LRRNIGYVIQQiGLFPNMTIEENItvvprMLGwdKARCKQRAEELMDMVALDA---------RKFLHRYPKEMSGGQQQR 148
Cdd:TIGR00957 697 MKGSVAYVPQQ-AWIQNDSLRENI-----LFG--KALNEKYYQQVLEACALLPdleilpsgdRTEIGEKGVNLSGGQKQR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDP-INREVIQNQFLDMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDE 227
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQE 847
|
....
gi 446515747 228 LLAK 231
Cdd:TIGR00957 848 LLQR 851
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-172 |
2.21e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTvTLRRNIGYVIQQIGLFPNMTIEENIT 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 103 VVPRMLGwdkarcKQRAEELMDmvALDA---RKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK13538 97 FYQRLHG------PGDDEALWE--ALAQvglAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-219 |
2.33e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNdmdTVT----LRRNIGYVIQQI---GLFPN 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV---TRSpqdgLANGIVYISEDRkrdGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITVVP-RMLGWDKARCKQRAEELM--DMVALdarkFLHRYP------KEMSGGQQQRIGVIRALAADPPVLLMD 165
Cdd:PRK10762 345 MSVKENMSLTAlRYFSRAGGSLKHADEQQAvsDFIRL----FNIKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 166 EPFGAVD-PINREVIQ--NQFldmqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK10762 421 EPTRGVDvGAKKEIYQliNQF----KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-167 |
6.59e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.88 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 5 ENLTKQfVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLIAPS-SGNILINGENTNDmdtvTLRRNI 82
Cdd:cd03232 7 KNLNYT-VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLDK----NFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGLFPNMTIEENITvvprmlgwdkarckqraeelmdmvaldarkfLHRYPKEMSGGQQQR--IGVirALAADPP 160
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALR-------------------------------FSALLRGLSVEQRKRltIGV--ELAAKPS 128
|
....*..
gi 446515747 161 VLLMDEP 167
Cdd:cd03232 129 ILFLDEP 135
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-217 |
9.12e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.96 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntndmdtvtlrrnIGYVIQQIGLFPNmTIEENITV 103
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 vprMLGWDKARCKQ--RAEELMDMVALDARK---FLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:cd03291 121 ---GVSYDEYRYKSvvKACQLEEDITKFPEKdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446515747 179 IqnqFLDMQRKL--KKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:cd03291 198 I---FESCVCKLmaNKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-203 |
9.85e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQ---------------FVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIN 66
Cdd:PRK13545 5 VKFEHVTKKykmynkpfdklkdlfFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 67 GENTndmdtvtlrrnigYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMValDARKFLHRYPKEMSGGQQ 146
Cdd:PRK13545 85 GSAA-------------LIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFA--DIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 147 QRIGVIRALAADPPVLLMDEPFGAVDpinrEVIQNQFLDMQRKLK---KTVMLVSHDIDE 203
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGD----QTFTKKCLDKMNEFKeqgKTIFFISHSLSQ 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-219 |
1.81e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.46 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNMTIEEN 100
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 101 ITVVPRMLGWDKARCKqraeeLMDMVALDARKFLHrypKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ 180
Cdd:PRK10522 418 KPANPALVEKWLERLK-----MAHKLELEDGRISN---LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190
....*....|....*....|....*....|....*....
gi 446515747 181 NQFLDMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGRI 219
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-229 |
4.01e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.47 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI--NRLIAPSSGNILINGENTNDMdTVTLRrnigyviQQIGLFpnmtiee 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEER-------ARLGIF------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 100 nitvvprmLGWdkarckQRAEElMDMVALdaRKFLhRYPKE-MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:cd03217 81 --------LAF------QYPPE-IPGVKN--ADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446515747 179 IQNQFLDMqRKLKKTVMLVSH--DIDEALKlGDRIAVFRQGRIVqCASPDELL 229
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIV-KSGDKELA 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-220 |
5.38e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFvqkkgQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTV-TLRRNI 82
Cdd:PRK10982 1 MSNISKSF-----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGLFPNMTIEENITV--VPRMlGW--DKARCKQRAEELMDMVALDARkflhryPKE----MSGGQQQRIGVIRA 154
Cdd:PRK10982 76 SMVHQELNLVLQRSVMDNMWLgrYPTK-GMfvDQDKMYRDTKAIFDELDIDID------PRAkvatLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 155 LAADPPVLLMDEPFGAVDpiNREViqNQFLDMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLT--EKEV--NHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-221 |
1.13e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKminrLIA------PSSGNILINGENTNDMDtVTLR--RNIGYVIQQIGLFPN 94
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAK----VLMghpkyeVTSGSILLDGEDILELS-PDERarAGIFLAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEE------NITVVPRMlgwDKARCKQRAEELMDMVALDArKFLHRYPKE-MSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:COG0396 92 VSVSNflrtalNARRGEEL---SAREFLKLLKEKMKELGLDE-DFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 168 --------FGAVdpinREVIqNQFldmqRKLKKTVMLVSH-----DIDEAlklgDRIAVFRQGRIVQ 221
Cdd:COG0396 168 dsgldidaLRIV----AEGV-NKL----RSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVK 221
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
265-367 |
1.27e-11 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 61.81 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNA--SGICADITHPFR------------ITGKAEDNL 330
Cdd:COG3448 13 VTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRAllPDRLDELEERLLdlpvedvmtrpvVTVTPDTPL 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 446515747 331 RIVLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYL 367
Cdd:COG3448 93 EEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-217 |
2.61e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.32 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntndmdtvtlrrnIGYVIQQIGLFPNmTIEENITV 103
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 vprMLGWDKARCKQ--RAEELMDMVALDARK---FLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:TIGR01271 510 ---GLSYDEYRYTSviKACQLEEDIALFPEKdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446515747 179 IqnqFLDMQRKL--KKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:TIGR01271 587 I---FESCLCKLmsNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-231 |
3.22e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTkqFVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:PRK10790 341 IDIDNVS--FAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYViQQIGLFPNMTIEENITvvprmLGWDKArcKQRAEELMDMVALD--ARKF---LHRYPKE----MSGGQQQRIGVI 152
Cdd:PRK10790 417 VAMV-QQDPVVLADTFLANVT-----LGRDIS--EEQVWQALETVQLAelARSLpdgLYTPLGEqgnnLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQnQFLDMQRKlKKTVMLVSH---DIDEAlklgDRIAVFRQGRIVQCASPDELL 229
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQ-QALAAVRE-HTTLVVIAHrlsTIVEA----DTILVLHRGQAVEQGTHQQLL 562
|
..
gi 446515747 230 AK 231
Cdd:PRK10790 563 AA 564
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-173 |
5.95e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVtlrRNIGYVIQQIGLFPNMTIEENITVV 104
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 105 PRMLGWdkaRCKQRAEELMDMVAL-DARKFLHRypkEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:PRK13543 107 CGLHGR---RAKQMPGSALAIVGLaGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-220 |
6.98e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 17 QPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIngentndmdtvtlRRNIGYVIQQIGLFpNMT 96
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 97 IEENItvvprmLGWDkarcKQRAEELMDMVAL-----DARKFLHRYPKE-------MSGGQQQRIGVIRALAADPPVLLM 164
Cdd:PTZ00243 737 VRGNI------LFFD----EEDAARLADAVRVsqleaDLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 165 DEPFGAVDP-INREVIQNQFLDmqRKLKKTVMLVSHDIdEALKLGDRIAVFRQGRIV 220
Cdd:PTZ00243 807 DDPLSALDAhVGERVVEECFLG--ALAGKTRVLATHQV-HVVPRADYVVALGDGRVE 860
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-235 |
1.07e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGEntndmdTVTLRRNIGYVIQQI----------GLFPN 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK------PIDIRSPRDAIRAGImlcpedrkaeGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITVVPR----MLGW--DKARCKQRAEELMDMVALdarKFLHRYPKEM--SGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PRK11288 346 HSVADNINISARrhhlRAGCliNNRWEAENADRFIRSLNI---KTPSREQLIMnlSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 167 PFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRIVqcaspDELLAKPANE 235
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQATE 485
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-230 |
1.56e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLK-MINRLIAPSSGNILINGentndmdtvtlrrNIGYVIQQIGLFpNMTIEENIt 102
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQVSWIF-NATVRDNI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 103 vvprMLG--WDKArckqRAEELMDMVALdaRKFLHRYPK-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:PLN03130 700 ----LFGspFDPE----RYERAIDVTAL--QHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 170 AVDP-INREVIQNQFLDMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDELLA 230
Cdd:PLN03130 770 ALDAhVGRQVFDKCIKDELR--GKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
253-367 |
1.61e-10 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 58.34 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 253 VSAGDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGIC---------ADI-THPFrI 322
Cdd:COG0517 1 MKVKDIMTTDV-VTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEgkdlldtpvSEVmTRPP-V 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446515747 323 TGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYL 367
Cdd:COG0517 79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-228 |
2.01e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTtlkminrLIAPSSGNiLINGENTndmdTVTLRRN 81
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKP--TLSDINLEIPVGSLVAIVGGTGEGKTS-------LISAMLGE-LSHAETS----SVVIRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFpNMTIEENItvvprMLGWDKArcKQRAEELMDMVAL--DARKFLHRYPKEM-------SGGQQQRIGVI 152
Cdd:PLN03232 681 VAYVPQVSWIF-NATVRENI-----LFGSDFE--SERYWRAIDVTALqhDLDLLPGRDLTEIgergvniSGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446515747 153 RALAADPPVLLMDEPFGAVDP-INREVIQNQfldMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGRIVQCASPDEL 228
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAhVAHQVFDSC---MKDELKgKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-236 |
2.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 29 VPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENITVVPRML 108
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 109 GWDKARCKQRAeELMDMV-----ALDARKFlhRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQf 183
Cdd:PLN03232 1338 DADLWEALERA-HIKDVIdrnpfGLDAEVS--EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT- 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446515747 184 ldMQRKLKKTVMLV-SHDIDEALKLgDRIAVFRQGRIVQCASPDELLAKPANEF 236
Cdd:PLN03232 1414 --IREEFKSCTMLViAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| CBS_pair_arch |
cd09836 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
263-368 |
4.35e-10 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 56.76 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 263 PTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARN--ASGICAD------ITHPFrITGKAEDNLRIVL 334
Cdd:cd09836 4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRavAEGIDLDtpveeiMTKNL-VTVSPDESIYEAA 82
|
90 100 110
....*....|....*....|....*....|....
gi 446515747 335 SRLYESNTSWMPIVDEDGRYNGEISQDYIADYLS 368
Cdd:cd09836 83 ELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-199 |
4.59e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 39 GPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLrrniGYVIQQIGLFPNMTIEENITVVPRMlgWDKARCKQR 118
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLKLEMTVFENLKFWSEI--YNSAETLYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 119 AEELMDMvaldaRKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNqFLDMQRKLKKTVMLVS 198
Cdd:PRK13541 107 AIHYFKL-----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVLLSS 180
|
.
gi 446515747 199 H 199
Cdd:PRK13541 181 H 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-219 |
1.29e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLIAPSSGNILINGENTNDMDTV-TLRRNIGYVIQ---QIGLFPN 94
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAqAIRAGIAMVPEdrkRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 95 MTIEENITVVPRMLGWDKARCKQRAEE---LMDMVALDARKFLHRYP-KEMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRIDAAAELqiiGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446515747 171 VD-PINREVIQNQFLDMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:TIGR02633 434 VDvGAKYEIYKLINQLAQEGV--AIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-204 |
1.40e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILI-------NGENTNDmdtvtLRRNIGYVIQQI------ 89
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTlfgrrrgSGETIWD-----IKKHIGYVSSSLhldyrv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 90 ----------GLFPNMTIEENITvvprmlgwDKARckQRAEELMDMVALDARkfLHRYP-KEMSGGQQQRIGVIRALAAD 158
Cdd:PRK10938 352 stsvrnvilsGFFDSIGIYQAVS--------DRQQ--KLAQQWLDILGIDKR--TADAPfHSLSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446515747 159 PPVLLMDEPFGAVDPINREVIQnQFLDMQRKLKKTVML-VSHDIDEA 204
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVR-RFVDVLISEGETQLLfVSHHAEDA 465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-216 |
1.55e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 32 GEMCVLLGPSGCGKTTTLKMINRLIAPSSGN-ILINGENTNDMDTVTLRRNIGyviqqiglfpnmtieenitvvprmlgw 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 111 dkarckqraeelmdmvaldarkflHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ-----NQFLD 185
Cdd:smart00382 55 ------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLL 110
|
170 180 190
....*....|....*....|....*....|.
gi 446515747 186 MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQ 216
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-238 |
2.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 37 LLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENITVVPRMLGWDKARCK 116
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDADLWESL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 117 QRAEeLMDMV-----ALDARkfLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQfldMQRKLK 191
Cdd:PLN03130 1349 ERAH-LKDVIrrnslGLDAE--VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT---IREEFK 1422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446515747 192 KTVMLV-SHDIDEALKLgDRIAVFRQGRIVQCASPDELLAKPANEFVG 238
Cdd:PLN03130 1423 SCTMLIiAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-214 |
2.56e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 31 EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILIngentndmdtvTLRrnIGYVIQQIGLFPNMTIEENITVVPRMLG- 109
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELK--ISYKPQYIKPDYDGTVEDLLRSITDDLGs 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 110 -WDKarckqraEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIQNqfl 184
Cdd:PRK13409 431 sYYK-------SEIIKPLQLE--RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRR--- 498
|
170 180 190
....*....|....*....|....*....|...
gi 446515747 185 dMQRKLKKTVMLVSHDI---DealKLGDRIAVF 214
Cdd:PRK13409 499 -IAEEREATALVVDHDIymiD---YISDRLMVF 527
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-218 |
4.15e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 32 GEMCVLLGPSGCGKTTTLKMINRLIAPSS--GNILINGENTNDMdtvTLRRnIGYVIQQIGLFPNMTIEENITVV----- 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ---ILKR-TGFVTQDDILYPHLTVRETLVFCsllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 105 PRMLG-WDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQF 183
Cdd:PLN03211 170 PKSLTkQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190
....*....|....*....|....*....|....*
gi 446515747 184 LDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGR 218
Cdd:PLN03211 250 GSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-245 |
5.39e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.46 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLK---HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENI----TVVPRMLgWDKARCKQraeeLMDMV-----ALDArkFLHRYPKEMSGGQQQRIGVI 152
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLdpecKCTDDRL-WEALEIAQ----LKNMVkslpgGLDA--VVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIQNqfLDMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGRIVQCASPDELLAKP 232
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQK--VVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
250
....*....|...
gi 446515747 233 ANEFvGSFVGQDR 245
Cdd:cd03288 246 DGVF-ASLVRTDK 257
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-229 |
5.46e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKKGQPLKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIApSSGNILINGENTNDMDTVTLRRN 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLE---NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 IGYVIQQIGLFPNmTIEENITVVPRmlgWDKARCKQRAEElmdmVALdaRKFLHRYPKEM-----------SGGQQQRIG 150
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGK---WSDEEIWKVAEE----VGL--KSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 151 VIRALAADPPVLLMDEPFGAVDPINREVIqnqfldmQRKLKK-----TVMLVSHDIdEALKLGDRIAVFRQGRIVQCASP 225
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVI-------RKTLKQafadcTVILSEHRI-EAMLECQRFLVIEENKVRQYDSI 220
|
....
gi 446515747 226 DELL 229
Cdd:cd03289 221 QKLL 224
|
|
| CBS_pair_bact_arch |
cd17775 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
262-367 |
6.88e-09 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 53.31 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 262 QPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRR--------EARNASGICA-DITHPFRITGKAEDNLRI 332
Cdd:cd17775 3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRdivvevvaKGLDPKDVTVgDIMSADLITAREDDGLFE 82
|
90 100 110
....*....|....*....|....*....|....*
gi 446515747 333 VLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYL 367
Cdd:cd17775 83 ALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-214 |
7.96e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 31 EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingentndmdTVTLRrnIGYVIQQIGLFPNMTIEENI-TVVPRMLG 109
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--ISYKPQYISPDYDGTVEEFLrSANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 110 --WDKarckqraEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIQNqf 183
Cdd:COG1245 432 ssYYK-------TEIIKPLGLE--KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRR-- 500
|
170 180 190
....*....|....*....|....*....|....
gi 446515747 184 ldMQRKLKKTVMLVSHDI---DealKLGDRIAVF 214
Cdd:COG1245 501 --FAENRGKTAMVVDHDIyliD---YISDRLMVF 529
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-206 |
9.31e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKKGQPLKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLiAPSSGNILINGENTNDMDTVTLRRNIG 83
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQ---DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQQIGLFPNmTIEENITVVPRmlgWDKARCKQRAEElmdmVALdaRKFLHRYPKEM-----------SGGQQQRIGVI 152
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEE----VGL--KSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446515747 153 RALAADPPVLLMDEPFGAVDPINREVIqnqfldmQRKLKK-----TVMLVSHDIDEALK 206
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQII-------RKTLKQsfsncTVILSEHRVEALLE 1417
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-219 |
1.15e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-----NRliapSSGNILING-----ENTNDmdtvTLRRNIGYVIQ-- 87
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGkpvkiRNPQQ----AIAQGIAMVPEdr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 88 -QIGLFPNMTIEENIT--VVPRMLGW---DKARCKQRAEELMDMVALDARKFLHRYpKEMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK13549 348 kRDGIVPVMGVGKNITlaALDRFTGGsriDDAAELKTILESIQRLKVKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515747 162 LLMDEPFGAVD-----PINRevIQNQFLDMQrklkKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK13549 427 LILDEPTRGIDvgakyEIYK--LINQLVQQG----VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
241-367 |
1.36e-08 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 54.50 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 241 VGQDRTLKRLLLVSAGDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDnDGKPLGFVKRREARNASGIC------- 313
Cdd:COG2524 74 VVAEKELGLVLKMKVKDIMTKDV-ITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGrdlldap 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 314 -ADITHPFRITGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYL 367
Cdd:COG2524 152 vSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-231 |
1.56e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRRNIGYVIQQIGLFPNmTIEENITV 103
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 104 VPRMLGWDKARCKQRAEeLMDMVALDARKFLHRYPK---EMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ 180
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAH-LKTFVSALPDKLDHECAEggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 181 ----NQFLDMqrklkkTVMLVSHDIDEALKLgDRIAVFRQGRIVQCASPDELLAK 231
Cdd:TIGR00957 1462 stirTQFEDC------TVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-231 |
2.00e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 24 NVNLNVPEGEMCVLLGPSGCGKTTTLKminrLIA--PS----SGNILINGENTNDMDTvTLRRNIG------YVIQqigl 91
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSK----VIAghPAykilEGDILFKGESILDLEP-EERAHLGiflafqYPIE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 92 FPNMTIEENItvvprMLGWDKARCKQRAEEL------------MDMVALDArKFLHRYPKE-MSGGQQQRIGVIRALAAD 158
Cdd:CHL00131 96 IPGVSNADFL-----RLAYNSKRKFQGLPELdplefleiinekLKLVGMDP-SFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 159 PPVLLMDEPFGAVDpINREVIQNQFLDMQRKLKKTVMLVSH--DIDEALKlGDRIAVFRQGRIVQCASPDelLAK 231
Cdd:CHL00131 170 SELAILDETDSGLD-IDALKIIAEGINKLMTSENSIILITHyqRLLDYIK-PDYVHVMQNGKIIKTGDAE--LAK 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-200 |
2.42e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFvqkKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINgENTndmdtvtlrrNIG 83
Cdd:PRK15064 322 VENLTKGF---DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENA----------NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 84 YVIQ--------QIGLFPNM----TIEENITVVPRMLGwdkaRckqraeelMDMVALDARKFlhryPKEMSGGQQQRIGV 151
Cdd:PRK15064 386 YYAQdhaydfenDLTLFDWMsqwrQEGDDEQAVRGTLG----R--------LLFSQDDIKKS----VKVLSGGEKGRMLF 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446515747 152 IRALAADPPVLLMDEPFGAVDpinREVIQ--NQFLDmqrKLKKTVMLVSHD 200
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMD---MESIEslNMALE---KYEGTLIFVSHD 494
|
|
| CBS_pair_inorgPPase |
cd04597 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ... |
265-359 |
3.87e-08 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.
Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 50.81 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRRE-ARNASGIcadITHPFRITGKAEDNLRIVLSRLYESNTS 343
Cdd:cd04597 8 EPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDiARTVDYI---MTKDNLIVFKEDDYLDEVKEIMLNTNFR 84
|
90
....*....|....*.
gi 446515747 344 WMPIVDEDGRYNGEIS 359
Cdd:cd04597 85 NYPVVDENNKFLGTIS 100
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
265-369 |
4.76e-08 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 50.98 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARN---ASGIC------ADITHPFRITGKAEDNLRIVLS 335
Cdd:COG2905 10 VTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRrvlAEGLDpldtpvSEVMTRPPITVSPDDSLAEALE 89
|
90 100 110
....*....|....*....|....*....|....
gi 446515747 336 RLYESNTSWMPIVDeDGRYNGEISQDYIADYLSS 369
Cdd:COG2905 90 LMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSE 122
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-167 |
5.46e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFVQKkgqPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINgentndmDTVTLrrn 81
Cdd:TIGR03719 323 IEAENLTKAFGDK---LL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------ETVKL--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 82 iGYVIQQ-IGLFPNMTIEENITVVPRMLGWDKARCKQRAeelmdMVAL------DARKFLhrypKEMSGGQQQRIGVIRA 154
Cdd:TIGR03719 388 -AYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRfnfkgsDQQKKV----GQLSGGERNRVHLAKT 457
|
170
....*....|...
gi 446515747 155 LAADPPVLLMDEP 167
Cdd:TIGR03719 458 LKSGGNVLLLDEP 470
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
263-304 |
9.22e-08 |
|
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.
Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 48.28 E-value: 9.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446515747 263 PTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRR 304
Cdd:smart00116 1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRR 42
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
255-309 |
3.28e-07 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 46.82 E-value: 3.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 255 AGDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNA 309
Cdd:pfam00571 1 VKDIMTKDV-VTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-240 |
5.38e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.49 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 29 VPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingentnDMDTVTlrrnIGYVIQQIGLfpnmtieenitvvprml 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--------EWDGIT----PVYKPQYIDL----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 109 gwdkarckqraeelmdmvaldarkflhrypkemSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQR 188
Cdd:cd03222 73 ---------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446515747 189 KLKKTVMLVSHDIDEALKLGDRIAVFR-QGRIVQCASPDELLAKPANEFVGSF 240
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVFEgEPGVYGIASQPKGTREGINRFLRGY 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-219 |
6.09e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKqfvqkKGQPlkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDTVTLRR 80
Cdd:PRK10982 250 ILEVRNLTS-----LRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 81 NiGYVI-----QQIGLFPNMTIEEN--ITVVPRMLG----WDKARCKQRAEELMDmvALDARKFLHRYP-KEMSGGQQQR 148
Cdd:PRK10982 323 H-GFALvteerRSTGIYAYLDIGFNslISNIRNYKNkvglLDNSRMKSDTQWVID--SMRVKTPGHRTQiGSLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGRI 219
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-220 |
8.73e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTtLKM------INRLIapsSGNILINGEntnDMDTVTLRRNIG----YVIQ-- 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsvfgrsYGRNI---SGTVFKDGK---EVDVSTVSDAIDaglaYVTEdr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 88 -QIGLFPNMTIEENITVvPRMLGWDKARCKQRAEELMdmVALDARKFLH-RYPK------EMSGGQQQRIGVIRALAADP 159
Cdd:NF040905 347 kGYGLNLIDDIKRNITL-ANLGKVSRRGVIDENEEIK--VAEEYRKKMNiKTPSvfqkvgNLSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 160 PVLLMDEPFGAVDP---------INREVIQNqfldmqrklkKTVMLVSHDIDEALKLGDRIAVFRQGRIV 220
Cdd:NF040905 424 DVLILDEPTRGIDVgakyeiytiINELAAEG----------KGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
244-301 |
1.72e-06 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 46.78 E-value: 1.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 244 DRTLKRLLLVSAGDVTDQ-------QPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:COG0517 50 DRDLRRALAAEGKDLLDTpvsevmtRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGII 114
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-201 |
1.76e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 26 NLNVP-EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingENTNDMDTVtLRRNIGYVIQQiglFPNMTIEENITVV 104
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY----DEEPSWDEV-LKRFRGTELQD---YFKKLANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 105 ---------PRMLgwdKARCKQ---RAEE--LMDMVA--LDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:COG1245 164 hkpqyvdliPKVF---KGTVRElleKVDErgKLDELAekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*..
gi 446515747 169 GAVDPINR----EVIQnqflDMQRKlKKTVMLVSHDI 201
Cdd:COG1245 241 SYLDIYQRlnvaRLIR----ELAEE-GKYVLVVEHDL 272
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
256-301 |
2.55e-06 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 49.44 E-value: 2.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446515747 256 GDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:PRK14869 71 RDLEIDKP-VTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLV 115
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
244-305 |
3.22e-06 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 46.01 E-value: 3.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515747 244 DRTLKRLLLVSAGDVTdQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRRE 305
Cdd:COG3448 64 DELEERLLDLPVEDVM-TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTD 124
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-200 |
4.87e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 4 LENLTKQFVQKKgqplkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLK-MINRLiAPSSGNIlingentndmdTVTLRRNI 82
Cdd:PRK11147 322 MENVNYQIDGKQ-----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRI-----------HCGTKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQ-QIGLFPNMTIEEN-------ITV--VPR-MLGWdkarckqraeeLMDmvaldarkFLH-----RYP-KEMSGGQ 145
Cdd:PRK11147 385 AYFDQhRAELDPEKTVMDNlaegkqeVMVngRPRhVLGY-----------LQD--------FLFhpkraMTPvKALSGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQrklkKTVMLVSHD 200
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ----GTVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-101 |
7.83e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 2 IKLENLTKQFvqkkGQPLkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILInGEntndmdTVTLrrn 81
Cdd:PRK11819 325 IEAENLSKSF----GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE------TVKL--- 389
|
90 100
....*....|....*....|.
gi 446515747 82 iGYVIQQ-IGLFPNMTIEENI 101
Cdd:PRK11819 390 -AYVDQSrDALDPNKTVWEEI 409
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-200 |
8.04e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLTKQFVQKkgqPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILING------------- 67
Cdd:PRK15064 1 MLSTANITMQFGAK---PL--FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPnerlgklrqdqfa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 68 -ENTNDMDTVTLRRNIGYVIQQ----IGLFPNMTIEENITV------VPRMLGWDkarCKQRAEELMDMVALDARkfLHR 136
Cdd:PRK15064 76 fEEFTVLDTVIMGHTELWEVKQerdrIYALPEMSEEDGMKVadlevkFAEMDGYT---AEARAGELLLGVGIPEE--QHY 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515747 137 YP-KEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDpINreVIqnQFL-DMQRKLKKTVMLVSHD 200
Cdd:PRK15064 151 GLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-IN--TI--RWLeDVLNERNSTMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-172 |
1.26e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 6 NLTKQfVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLkmiNRLIAPSSGNILINGE---NTNDMDTvTLRRNI 82
Cdd:TIGR00956 764 NLTYE-VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDrlvNGRPLDS-SFQRSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 83 GYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQR---AEELMDMVAL----DArkfLHRYPKE-MSGGQQQR--IGVi 152
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMesyaDA---VVGVPGEgLNVEQRKRltIGV- 914
|
170 180
....*....|....*....|.
gi 446515747 153 rALAADPPVLL-MDEPFGAVD 172
Cdd:TIGR00956 915 -ELVAKPKLLLfLDEPTSGLD 934
|
|
| CBS_pair_ABC_OpuCA_assoc |
cd04583 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
265-353 |
1.38e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 43.66 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVK----RREARNASGIcADITHPFRITGKAEDNLRIVLSRLYES 340
Cdd:cd04583 5 VTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDiediNRNYRKAKKV-GEIMERDVFTVKEDSLLRDTVDRILKR 83
|
90
....*....|...
gi 446515747 341 NTSWMPIVDEDGR 353
Cdd:cd04583 84 GLKYVPVVDEQGR 96
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-200 |
1.42e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 18 PLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGentndmDTVTLR------RNIG-----YV- 85
Cdd:PRK11147 17 PL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ------DLIVARlqqdppRNVEgtvydFVa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 86 --IQQIG-----------LFPNMTIEENITVVPRML-------GWdkaRCKQRAEELMDMVALDARKFLhrypKEMSGGQ 145
Cdd:PRK11147 89 egIEEQAeylkryhdishLVETDPSEKNLNELAKLQeqldhhnLW---QLENRINEVLAQLGLDPDAAL----SSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446515747 146 QQRIGVIRALAADPPVLLMDEPFGAVDPinrEVIQ--NQFLdmqRKLKKTVMLVSHD 200
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDI---ETIEwlEGFL---KTFQGSIIFISHD 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-173 |
2.27e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.28 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 1 MIKLENLtkQFVQKKGQPLkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMIN--------RLIAPSSGNILINGENTNd 72
Cdd:TIGR00954 451 GIKFENI--PLVTPNGDVL--IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQRPY- 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 73 MDTVTLRRNIGYviqqiglfPnMTIEENItvvprmlgwDKARCKQRAEELMDMVALDarKFLHR---------YPKEMSG 143
Cdd:TIGR00954 526 MTLGTLRDQIIY--------P-DSSEDMK---------RRGLSDKDLEQILDNVQLT--HILEReggwsavqdWMDVLSG 585
|
170 180 190
....*....|....*....|....*....|
gi 446515747 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
265-301 |
3.23e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 43.19 E-value: 3.23e-05
10 20 30
....*....|....*....|....*....|....*..
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:cd04586 6 VTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIV 42
|
|
| CBS_pair_plant_CBSX |
cd17789 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ... |
201-303 |
3.44e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 43.23 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 201 IDEALKL--GDRIAVF----RQGRIVQCASPDELLAKPA----NEFVGSFVGQDRT------LKRLLLVSAG----DVTD 260
Cdd:cd17789 14 VDEALELlvENRITGLpvidEDWRLVGVVSDYDLLALDSisgrSQTDNNFPPADSTwktfneVQKLLSKTNGkvvgDVMT 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446515747 261 QQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKR 303
Cdd:cd17789 94 PSP-LVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITR 135
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
245-361 |
4.10e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 42.98 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 245 RTLKRLLLVsaGDVTDQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASG---ICADITHPFr 321
Cdd:COG4109 10 DTFKEILLV--EDIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDdtpIEDVMTKNP- 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446515747 322 ITGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEIS-QD 361
Cdd:COG4109 87 ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISrQD 127
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
265-353 |
4.15e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 42.40 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASgicaDITHPFR---------ITGKAEDNLRIVLS 335
Cdd:cd04601 5 VTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFET----DLSTPVSevmtpderlVTAPEGITLEEAKE 80
|
90
....*....|....*...
gi 446515747 336 RLYESNTSWMPIVDEDGR 353
Cdd:cd04601 81 ILHKHKIEKLPIVDDNGE 98
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
245-304 |
9.66e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 42.03 E-value: 9.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 245 RTLKRLLLVSAGDVTdQQPTITARPSTPLSEAFGIMDDHDIRAITVIDnDGKPLGFVKRR 304
Cdd:cd04586 75 EEYVKAHGRTVGDVM-TRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRA 132
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
248-306 |
1.04e-04 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 41.82 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515747 248 KRLL-LVSAGDVTDQQPT-----------ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREA 306
Cdd:COG4109 58 GRLVgIVTSKDILGKDDDtpiedvmtknpITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-201 |
1.16e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 26 NLNVP-EGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNIlingENTNDMDTVtLRRNIGYVIQQigLFPNMtIEENITVV 104
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY----EEEPSWDEV-LKRFRGTELQN--YFKKL-YNGEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 105 ---------PRMLgwdKARCKQ---------RAEELMDMVALDarKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PRK13409 164 hkpqyvdliPKVF---KGKVREllkkvdergKLDEVVERLGLE--NILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446515747 167 P---------FGAVDPInREVIQNqfldmqrklkKTVMLVSHDI 201
Cdd:PRK13409 239 PtsyldirqrLNVARLI-RELAEG----------KYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-245 |
1.58e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 32 GEMCVLLGPSGCGKTTTLKMINRLIAPS----SGNILINGENTNDMDTvTLRRNIGYVIQQIGLFPNMTIEENI------ 101
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKK-HYRGDVVYNAETDVHFPHLTVGETLdfaarc 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 102 -TVVPRMLGWDK-ARCKQRAEELMDMVALDA---RKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:TIGR00956 166 kTPQNRPDGVSReEYAKHIADVYMATYGLSHtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATA 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 177 EVIQNQFLDMQRKLKKTV-MLVSHDIDEALKLGDRIAVFRQGRIVQCASPDEllAKPANEFVGsFVGQDR 245
Cdd:TIGR00956 246 LEFIRALKTSANILDTTPlVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADK--AKQYFEKMG-FKCPDR 312
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
111-213 |
1.72e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 111 DKARCKQRAEELMDMVALDaRKFlhrypKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINReviqNQFLDMQRKL 190
Cdd:PRK10938 112 DPARCEQLAQQFGITALLD-RRF-----KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR----QQLAELLASL 181
|
90 100
....*....|....*....|....*.
gi 446515747 191 KK---TVMLVSHDIDEALKLGDRIAV 213
Cdd:PRK10938 182 HQsgiTLVLVLNRFDEIPDFVQFAGV 207
|
|
| CBS_pair_HPP_assoc |
cd04600 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
265-364 |
2.03e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 41.01 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLG------FVKRREA----------------RNASGIC-ADI-THPF 320
Cdd:cd04600 6 VTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGivtladLLKHADLdpprglrgrlrrtlglRRDRPETvGDImTRPV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446515747 321 RiTGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEISQ-DYIA 364
Cdd:cd04600 86 V-TVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQsDLIA 129
|
|
| CBS_pair_AcuB_like |
cd04584 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
265-310 |
2.86e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 40.48 E-value: 2.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDnDGKPLGFVKRREARNAS 310
Cdd:cd04584 11 VTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRAS 55
|
|
| CBS_pair_arch_MET2_assoc |
cd04605 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
265-301 |
3.98e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 39.53 E-value: 3.98e-04
10 20 30
....*....|....*....|....*....|....*..
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:cd04605 72 ITARPDEPIELAARKMEKHNISALPVVDDDRRVIGII 108
|
|
| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc |
cd17771 |
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ... |
265-307 |
7.21e-04 |
|
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 38.84 E-value: 7.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREAR 307
Cdd:cd17771 7 VTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLL 49
|
|
| CBS_pair_voltage-gated_CLC_archaea |
cd04594 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
265-363 |
1.07e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 38.09 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASG------ICADITHpFRITGKAEDNLRIvLSRly 338
Cdd:cd04594 5 IKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENKSPgkvgkyVVRGSPY-VTPTSSLEEAWEI-MMR-- 80
|
90 100
....*....|....*....|....*
gi 446515747 339 eSNTSWMPIVDEdGRYNGEISQDYI 363
Cdd:cd04594 81 -NKSRWVAVVEK-GKFLGIITLDDL 103
|
|
| CBS_pair_ABC_Gly_Pro_assoc |
cd09831 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
260-360 |
1.23e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341402 [Multi-domain] Cd Length: 116 Bit Score: 38.31 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 260 DQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV-----KRREARNASGIcADITHPFRITGKAEDNLRIVL 334
Cdd:cd09831 5 KTQVTVIEKTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVsvdslRAALKENAQSL-EDAFLTDVETVPADTSLSDIL 83
|
90 100
....*....|....*....|....*.
gi 446515747 335 SRLYESNTSwMPIVDEDGRYNGEISQ 360
Cdd:cd09831 84 GLVASAPCP-LPVVDEDGRYLGVISK 108
|
|
| CBS_pair_SIS_assoc |
cd04604 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
245-301 |
2.00e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341378 [Multi-domain] Cd Length: 124 Bit Score: 37.75 E-value: 2.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 245 RTLKR---LLLVSAGDVTDQQPtITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:cd04604 59 RALEKgldILNLPAKDVMTRNP-KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGIL 117
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
265-358 |
2.41e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 39.68 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDnDGKPLGFVKRREARNASGICADI----THPFRITGKAEDNLRIVLSRLYES 340
Cdd:pfam00478 91 VTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDLRFETDLSQPVsevmTKENLVTAPEGTTLEEAKEILHKH 169
|
90
....*....|....*...
gi 446515747 341 NTSWMPIVDEDGRYNGEI 358
Cdd:pfam00478 170 KIEKLPVVDDNGRLVGLI 187
|
|
| CBS_pair_bac |
cd04629 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
265-301 |
2.53e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 37.42 E-value: 2.53e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:cd04629 6 VTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFL 42
|
|
| CBS_pair_arch1_repeat1 |
cd17780 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
269-365 |
3.44e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341416 [Multi-domain] Cd Length: 106 Bit Score: 36.94 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 269 PSTPLSEAFGIMDDHDIRAItVIDNDGKPLGFVKRREA-----RNASGICADITHPFRITgkAEDNLRIVLSRLYESNTS 343
Cdd:cd17780 9 ADTRLGKVRGLFEDENPKGV-VVTDDGEYEGVVTERQLlqshvEDDAKVGALVRAAPKVD--RTEDVREVARLLVEGGTK 85
|
90 100
....*....|....*....|..
gi 446515747 344 WMPIVdEDGRYNGEISQDYIAD 365
Cdd:cd17780 86 VAPVF-EGGSLWGVVTADAILE 106
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
260-301 |
3.47e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 37.13 E-value: 3.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446515747 260 DQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV 301
Cdd:cd04608 8 DLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMV 49
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-247 |
3.53e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 134 LHRYPKEMSGGQQQRIGVIRALAAD-PPVL-LMDEP-FGAVDPINREVIQNqfLDMQRKLKKTVMLVSHDiDEALKLGDR 210
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPsIGLHQRDNRRLINT--LKRLRDLGNTLIVVEHD-EDTIRAADY 558
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446515747 211 I------AVFRQGRIVQCASPDELLAKPaNEFVGSFVGQDRTL 247
Cdd:TIGR00630 559 VidigpgAGEHGGEVVASGTPEEILANP-DSLTGQYLSGRKKI 600
|
|
| CBS_pair_HRP1_like |
cd04622 |
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
266-364 |
3.71e-03 |
|
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 37.01 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 266 TARPSTPLSEAFGIMDDHDIRAITVIDNDgKPLGFVKRR--------EARNASGI-CADITHPFRITGKAEDNLRIVLSR 336
Cdd:cd04622 7 TVSPDTTLREAARLMRDLDIGALPVCEGD-RLVGMVTDRdivvravaEGKDPNTTtVREVMTGDVVTCSPDDDVEEAARL 85
|
90 100
....*....|....*....|....*...
gi 446515747 337 LYESNTSWMPIVDEDGRYNGEISQDYIA 364
Cdd:cd04622 86 MAEHQVRRLPVVDDDGRLVGIVSLGDLA 113
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
135-199 |
3.80e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446515747 135 HRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLdmqrKLKKTVMLVSH 199
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| CBS_pair_archHTH_assoc |
cd04588 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ... |
265-303 |
4.30e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 36.74 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKR 303
Cdd:cd04588 67 ITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITR 105
|
|
| AdhP |
COG1064 |
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
197-292 |
7.40e-03 |
|
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];
Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 38.17 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515747 197 VSHDIDEALKLgdriaVFRQGRIVQCASPDELLAKPAN-------EFVGSFVGQDRTLKRLL-LVSAGDVTdqqPTITAR 268
Cdd:COG1064 237 APATVNAALAL-----LRRGGRLVLVGLPGGPIPLPPFdlilkerSIRGSLIGTRADLQEMLdLAAEGKIK---PEVETI 308
|
90 100
....*....|....*....|....
gi 446515747 269 PSTPLSEAFGIMDDHDIRAITVID 292
Cdd:COG1064 309 PLEEANEALERLRAGKVRGRAVLD 332
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
265-310 |
9.77e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 37.75 E-value: 9.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446515747 265 ITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFV------KRREARNAS 310
Cdd:pfam00478 151 VTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLItikdieKAKEYPNAA 202
|
|
| |
