|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-306 |
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: 513.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGnR 240
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG-A 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 241 GRTWyegkSVADVLPLDESVQLEGQALSLHASLQEALVRVRDEEV--VPV-EENGQYIGALTSRHIVNY 306
Cdd:COG1125 240 DRGL----RRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGVdwLLVvDEDGRPLGWLTLEDLLRA 304
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
1.89e-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: 398.98 E-value: 1.89e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-290 |
7.68e-115 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 335.53 E-value: 7.68e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyniNEL---RWD 77
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEG--LADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 238 GNrgRTWYEGKSVADVlplDESVQLEGQALSLHASL-----QEALVRVRDEEVVPVEE 290
Cdd:COG3842 237 GE--ANLLPGTVLGDE---GGGVRTGGRTLEVPADAglaagGPVTVAIRPEDIRLSPE 289
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-292 |
5.76e-106 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 313.16 E-value: 5.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyniNEL----Rw 76
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLppkdR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEF 236
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 237 IGNRGRTWYEGKSVADvlpldeSVQLEGQALSLHASL-----QEALVRVRDEEVVPVEENG 292
Cdd:COG3839 234 IGSPPMNLLPGTVEGG------GVRLGGVRLPLPAALaaaagGEVTLGIRPEHLRLADEGD 288
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-299 |
1.29e-101 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 303.18 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL----RWDIGYVLQQIALFPHMTIAENIA 98
Cdd:COG4175 48 FDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 99 VVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKD 178
Cdd:COG4175 128 FGLEIQGVPKAERRERAREALELVGLAG--WEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 179 IVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFignrgrtwyegksVADVLPLD- 257
Cdd:COG4175 206 LLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADF-------------VEDVDRSKv 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1263193398 258 ---ESVQLEGQAL-SLHASLQEALVRVRDEEV---VPVEENGQYIGALT 299
Cdd:COG4175 273 ltaGSVMRPPEAVvSEKDGPRVALRRMREEGIsslYVVDRDRRLLGVVT 321
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-238 |
2.54e-100 |
|
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: 299.07 E-value: 2.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRW----DIGYVLQQIALFP 89
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREvrrkKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEE--YEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 170 LSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-238 |
1.94e-95 |
|
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: 281.82 E-value: 1.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRwdIGYV 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-237 |
5.21e-95 |
|
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: 282.22 E-value: 5.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 15 TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL----RWDIGYVLQQIALFPH 90
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPL 170
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEG--WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 171 SREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
7.99e-95 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 281.21 E-value: 7.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSY---EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyniNELRWD 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAG--FEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEG-----KVVQLDTP----EGIIHNP 228
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPrprdRELRTSP 239
|
....*.
gi 1263193398 229 knEFVE 234
Cdd:COG1116 240 --EFAA 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-217 |
2.25e-94 |
|
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: 278.25 E-value: 2.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqyNINELRWDIGYV 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG--LLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
6.24e-92 |
|
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: 272.42 E-value: 6.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNInelrwDI 78
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEdisLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG--FENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKE--GKVVQ 217
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-290 |
1.01e-90 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 273.95 E-value: 1.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqYNIN----ELRwd 77
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNlpprERR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG--LADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 238 GNrgrtwyegKSVADVLPLDESVQLEGQALSLHASLQE--ALVRVRDEEVVPVEE 290
Cdd:COG1118 235 GC--------VNVLRGRVIGGQLEADGLTLPVAEPLPDgpAVAGVRPHDIEVSRE 281
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
3.51e-80 |
|
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: 243.35 E-value: 3.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYedGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN---INELRW 76
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQQIALFPHMTIAENIAVvP--EMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAF-PlrEHTDLSEAEIRELVLEKLELVGLPG--AADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPkNEFVE 234
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVR 238
|
...
gi 1263193398 235 EFI 237
Cdd:COG1127 239 QFL 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-238 |
6.03e-79 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 244.86 E-value: 6.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI-----QQYNINElrw 76
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaENRHVNT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 digyVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK09452 91 ----VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEE--FAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEF 236
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244
|
..
gi 1263193398 237 IG 238
Cdd:PRK09452 245 IG 246
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
2.13e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 238.42 E-value: 2.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYV 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD--AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIH 226
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
4.84e-78 |
|
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: 237.62 E-value: 4.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQ----QiaLFpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG1122 81 FQnpddQ--LF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEH--LADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
8.81e-78 |
|
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: 245.97 E-value: 8.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYE----DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRW 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 ---DIGYVLQ--QIALFPHMTIAENIAVVPE-MRQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRA 150
Cdd:COG1123 340 lrrRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPPD-LADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
.
gi 1263193398 231 E 231
Cdd:COG1123 499 P 499
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-239 |
2.44e-77 |
|
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: 236.08 E-value: 2.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELrwDIGYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIA----VVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLDW--LADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
..
gi 1263193398 238 GN 239
Cdd:cd03296 238 GE 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
1.74e-76 |
|
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: 232.92 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElRwDIGYV 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-R-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEH--LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLD 219
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-238 |
1.21e-75 |
|
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: 235.70 E-value: 1.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqyNINELRWDIGYV 81
Cdd:TIGR03265 5 LSIDNIRKRFGA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT--RLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLdPDIyRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGL-PGS-ERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-238 |
3.04e-75 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 230.65 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI--QQYNINELRWDI 78
Cdd:COG1126 1 MIEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGLdPDiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGL-AD-KADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDP-LSREQLQkDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEF 236
Cdd:COG1126 158 MLFDEPTSALDPeLVGEVLD-VMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
..
gi 1263193398 237 IG 238
Cdd:COG1126 236 LS 237
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-238 |
5.86e-73 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 225.06 E-value: 5.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINelRWDIGYV 81
Cdd:TIGR00968 1 IEIANISKRFGS-FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEG--LGDRYPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-238 |
6.53e-72 |
|
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: 222.21 E-value: 6.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqyNINELRWDIGYVLQQIALFPHMTIAENI 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQK 177
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMLGIDHLL--NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 178 DIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:cd03299 171 ELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
2.20e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 220.30 E-value: 2.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDG---TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL--- 74
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 -RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAA 153
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGD--RLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMqEALSLGDRICIMKEGKVV 216
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
3.23e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 223.80 E-value: 3.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDG---TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL--- 74
Cdd:COG1135 1 MIELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSD--KADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPlsreQLQKDIVQLQKKIQK----TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:COG1135 159 PKVLLCDEATSALDP----ETTRSILDLLKDINRelglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
....*...
gi 1263193398 231 EFVEEFIG 238
Cdd:COG1135 235 ELTRRFLP 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-236 |
1.38e-70 |
|
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: 218.53 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYedGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---RWD 77
Cdd:cd03261 1 IELRGLTKSF--GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVvP--EMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAF-PlrEHTRLSEEEIREIVLEKLEAVGLRGA--EDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPkNEFVEE 235
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQ 234
|
.
gi 1263193398 236 F 236
Cdd:cd03261 235 F 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
3.97e-70 |
|
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: 215.51 E-value: 3.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNIN--ELRWDIG 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVL 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
4.27e-70 |
|
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: 216.56 E-value: 4.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 3 QFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQ----QIAlfpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:cd03225 81 FQnpddQFF---GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEG--LRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
1.30e-69 |
|
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: 216.29 E-value: 1.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDG---TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL--- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDK--ADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 155 PKIVLMDEPFSALDPLSREQlqkdIVQLQKKIQK----TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:cd03258 159 PKVLLCDEATSALDPETTQS----ILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-238 |
5.66e-69 |
|
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: 217.75 E-value: 5.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 33 LIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWdIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIK 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 113 ARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVF 192
Cdd:TIGR01187 79 PRVLEALRLVQLEE--FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1263193398 193 VTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIG 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
5.97e-69 |
|
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: 214.35 E-value: 5.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGtKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE-----TTEGSILIDGKDI--QQYNINEL 74
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPhMTIAENIAVVPEMRQ-WSKKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAA 153
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGI 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-237 |
1.51e-68 |
|
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: 213.57 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWDIGY 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE--FLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLqKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-238 |
2.74e-68 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 216.87 E-value: 2.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRwdIGYV 81
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIA----VVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAfgltVLPRRERPNAAAIKAKVTQLLEMVQLAH--LADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
.
gi 1263193398 238 G 238
Cdd:PRK10851 238 G 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
2.74e-68 |
|
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: 212.35 E-value: 2.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDG---TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---- 74
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL--NHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEAlSLGDRICIMKEGKV 215
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-280 |
1.13e-67 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 214.66 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL--- 74
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSD--KADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPlsreQLQKDIVQLQKKIQK----TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:PRK11153 159 PKVLLCDEATSALDP----ATTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1263193398 231 EFVEEFIGnrgrtwyegksvaDVLPLDESVQLEGQALSLHASLQEALVRV 280
Cdd:PRK11153 235 PLTREFIQ-------------STLHLDLPEDYLARLQAEPTTGSGPLLRL 271
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-238 |
2.38e-67 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 214.17 E-value: 2.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTkaVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNInELRwDIGY 80
Cdd:NF040840 1 MIRIENLSKDWKEFK--LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPP-EKR-GIAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:NF040840 77 VYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISH--LLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:NF040840 155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
2.17e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 207.60 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE---LRWD 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSD--KAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDP-LSREqlqkdIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGKVVQlDTPEG 223
Cdd:COG2884 159 LLADEPTGNLDPeTSWE-----IMELLEEINRrgtTVLIATHDLELVDRMPKRVLELEDGRLVR-DEARG 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
3.57e-66 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 207.99 E-value: 3.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN---INELRWD 77
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAV--VPEM-------RQWSKKDiKARVDDLLHMVGLDPDIYRdrMPDELSGGQKQRVGVV 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgrLGRTstwrsllGLFPPED-RERALEALERVGLADKAYQ--RADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVqLDTP 221
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV-FDGP 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
8.19e-65 |
|
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: 203.51 E-value: 8.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDG---TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRW- 76
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 --DIGYVLQ--QIALFPHMTIAENIAvvpEM-----RQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGV 147
Cdd:cd03257 81 rkEIQMVFQdpMSSLNPRMTIGEQIA---EPlrihgKLSKKEARKEAVLLLLVGVGLPEEVL-NRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-292 |
1.31e-64 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 207.39 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyniNEL----Rw 76
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELepadR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEP--LLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEF 236
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 237 IGNRGRTWYEGKSVAD--VLPLDESVQLEGQALSLHASLQEALVRVRDEEVVPVEENG 292
Cdd:PRK11650 235 IGSPAMNLLDGRVSADgaAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEG 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-304 |
2.20e-64 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 206.49 E-value: 2.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELrwDIGYVLQQI 85
Cdd:PRK11432 11 NITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAG--FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 166 ALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGNrgrtwy 245
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD------ 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 246 egksvADVLPL---DESVQLEGQALSLHASLQ------EALVRVRDEEVVpVEENGQYIGALTSRHIV 304
Cdd:PRK11432 240 -----ANIFPAtlsGDYVDIYGYRLPRPAAFAfnlpdgECTVGVRPEAIT-LSEQGEESQRCTIKHVA 301
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-239 |
9.30e-64 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 205.84 E-value: 9.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQynINELRWDIGY 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGN 239
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
3.22e-63 |
|
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: 198.91 E-value: 3.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI--QQYNINELRWDIG 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLAD--KADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 159 LMDEPFSALDP-LSREQLQKdIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:cd03262 158 LFDEPTSALDPeLVGEVLDV-MKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-224 |
1.06e-62 |
|
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: 199.99 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI---QQYNINEL 74
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQqialFPHM-----TIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYL-ERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGI 224
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
1.17e-62 |
|
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: 198.56 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---RWDI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAV--VPEM-------RQWSKKDiKARVDDLLHMVGLDPDIYRdrMPDELSGGQKQRVGVVR 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSgrLGRRstwrslfGLFPKEE-KQRALAALERVGLLDKAYQ--RADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-254 |
1.36e-62 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 203.73 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRW----DIGYVLQQIALFPHMT 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSR 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLEN--YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 173 EQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVeefignrgRTWYEGKSVAD 252
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV--------RTFFRGVDISQ 272
|
..
gi 1263193398 253 VL 254
Cdd:PRK10070 273 VF 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
4.32e-62 |
|
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: 205.14 E-value: 4.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE---TTEGSILIDGKDIQQYNINELRW 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQ--QIALFPhMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:COG1123 84 RIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLER--RLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
1.26e-61 |
|
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: 196.18 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSY---EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWD 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQI--ALFPHMTIAENIAvvpE-MRQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILA---EpLRIHGLPDREERIAELLEQVGLPPS-FLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPLsreqLQKDIVQLQKKIQK----TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:COG1124 157 PELLLLDEPTSALDVS----VQAEILNLLKDLREerglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 1263193398 231 EFVEEFIG 238
Cdd:COG1124 233 PYTRELLA 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-225 |
2.49e-61 |
|
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: 195.65 E-value: 2.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAV-----VPEMRQWSKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALgryphLGLFGRPSAED-REAVEEALERTGLEH--LADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-221 |
5.56e-61 |
|
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: 193.49 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqQYNINELRWDIGY 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD--KANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 161 DEPFSALDPLSREQLQkDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:cd03263 158 DEPTSGLDPASRRAIW-DLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-237 |
1.26e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 193.93 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNInelrwD 77
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQdvsLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLAD--FARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGkvvqldtPEGIIHNPKNEFVEEFI 237
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG-------PGRIVERLELDFSRRFL 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-242 |
6.32e-60 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 192.17 E-value: 6.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIET-----TEGSILIDGKDI--QQYNINEL 74
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPhMTIAENIAVVPEMRQW-SKKDIKARVDDLLHMVGLdPDIYRDRMPD---ELSGGQKQRVGVVRA 150
Cdd:COG1117 91 RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL-WDEVKDRLKKsalGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
250
....*....|..
gi 1263193398 231 EFVEEFIgnRGR 242
Cdd:COG1117 247 KRTEDYI--TGR 256
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-237 |
6.34e-60 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 191.46 E-value: 6.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ--QYNINELRWDI 78
Cdd:PRK09493 1 MIEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLdpdiyRDRM---PDELSGGQKQRVGVVRALAAN 154
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGL-----AERAhhyPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVE 234
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
...
gi 1263193398 235 EFI 237
Cdd:PRK09493 234 EFL 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
7.27e-60 |
|
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: 189.15 E-value: 7.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYV 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03230 79 PEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
5.34e-59 |
|
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: 191.81 E-value: 5.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSY--EDGT-KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE---TTEGSILIDGKDIQQYN---I 71
Cdd:COG0444 1 LLEVRNLKVYFptRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 72 NELRW-DIGYVLQ--QIALFPHMTIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVG 146
Cdd:COG0444 81 RKIRGrEIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 147 VVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIH 226
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 1263193398 227 NPK 229
Cdd:COG0444 241 NPR 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-238 |
5.46e-59 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 193.32 E-value: 5.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 7 VSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyNINEL---RWDIGYVLQ 83
Cdd:PRK11000 9 VTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVppaERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 84 QIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEP 163
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLL--DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 164 FSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-224 |
1.19e-58 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 189.18 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKD-IQQYNINELRWDIG 79
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQ----QialFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:TIGR04520 81 MVFQnpdnQ---FVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMED--FRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALsLGDRICIMKEGKVVQLDTPEGI 224
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREI 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
2.46e-58 |
|
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: 198.90 E-value: 2.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:COG2274 474 IELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVvpemrqwSKKDI-KARVDDLLHMVGLDPDIyrDRMPD-----------ELSGGQKQRVGVV 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENITL-------GDPDAtDEEIIEAARLAGLHDFI--EALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMqEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHE 694
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
7.47e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.02 E-value: 7.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPhMTIAENIAVVPEMRQwsKKDIKARVDDLLHMVGLDPDIyRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDI-LDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
1.47e-57 |
|
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: 182.97 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMqEALSLGDRICIMKEGK 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKG--KTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-222 |
2.04e-57 |
|
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: 185.19 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN---INELRWD 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAV--------VPEM-RQWSKKDiKARVDDLLHMVGLDpDIYRDRMpDELSGGQKQRVGVV 148
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHgrlgykptWRSLlGRFSEED-KERALSALERVGLA-DKAYQRA-DQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-217 |
2.44e-57 |
|
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: 184.04 E-value: 2.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIK---KGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI----QQYNINELRWDIGYVLQQIALF 88
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVpeMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:cd03297 88 PHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLDH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 169 PLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-222 |
3.30e-57 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 193.84 E-value: 3.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENIAvvpemrqWSKKDI-KARVDDLLHMVGLDPDIyrDRMPD-----------ELSGGQKQRVGVVR 149
Cdd:COG1132 420 PQDTFLF-SGTIRENIR-------YGRPDAtDEEVEEAAKAAQAHEFI--EALPDgydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDM---QEAlslgDRICIMKEGKVVQLDTPE 222
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLstiRNA----DRILVLDDGRIVEQGTHE 559
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-229 |
2.66e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 182.62 E-value: 2.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRW---DIGYVLQ--QIALFPH 90
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQdpYASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDp 169
Cdd:COG4608 112 MTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRPE-HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 170 LSreqLQKDIV----QLQKKIQKTIVFVTHDmqeaLS----LGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG4608 190 VS---IQAQVLnlleDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-229 |
4.18e-55 |
|
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: 179.17 E-value: 4.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIGYVLQQ 84
Cdd:cd03219 5 GLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAVVPEMRQ----------WSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:cd03219 84 PRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLAD--LADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLqKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
4.58e-55 |
|
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: 178.21 E-value: 4.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE---LRWD 77
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKA--DAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPlsreQLQKDIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:TIGR02673 159 LLADEPTGNLDP----DLSERILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
1.40e-54 |
|
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: 178.31 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIG 79
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQ---------------WSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQR 144
Cdd:COG0411 83 RTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLAD--RADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 145 VGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGI 224
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
....*
gi 1263193398 225 IHNPK 229
Cdd:COG0411 241 RADPR 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.13e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.66 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQynineLRWDIGY 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIAL---FPhMTIAEniaVV-----PEMRQW---SKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVR 149
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRD---VVlmgryGRRGLFrrpSRAD-REAVDEALERVGLED--LADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGkVVQLDTPE 222
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
5.46e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 173.68 E-value: 5.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIG 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKrARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVL 159
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITH--LRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQkkiQKTI-VFVT-HDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
6.51e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 175.30 E-value: 6.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINelrwDIGY 80
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGD--RANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
9.05e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 174.02 E-value: 9.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQ----QialFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:PRK13632 87 IIFQnpdnQ---FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMED--YLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALsLGDRICIMKEGKVVQLDTPEGIIHNpknefvEE 235
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN------KE 234
|
..
gi 1263193398 236 FI 237
Cdd:PRK13632 235 IL 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
2.28e-52 |
|
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: 171.31 E-value: 2.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINelrwDIGYV 81
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSE--YANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 162 EPFSALDPLSREqLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03269 154 EPFSGLDPVNVE-LLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
8.45e-52 |
|
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: 179.18 E-value: 8.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENIAVvpemrqwSKKDI-KARVDDLLHMVGLDPDIyrDRMPD-------E----LSGGQKQRVGVVR 149
Cdd:COG4988 417 PQNPYLF-AGTIRENLRL-------GRPDAsDEELEAALEAAGLDEFV--AALPDgldtplgEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMqEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHE 556
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-221 |
1.01e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 172.15 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI--QQYNINELR 75
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 76 WDIGYVLQ--QIALFPHmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAA 153
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
4.56e-51 |
|
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: 177.27 E-value: 4.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:COG4987 334 LELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVV-P-----EMRQwskkdikarvddLLHMVGLDPDIyrDRMPD-------E----LSGGQKQ 143
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLArPdatdeELWA------------ALERVGLGDWL--AALPDgldtwlgEggrrLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 144 RVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEG 223
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555
|
....*
gi 1263193398 224 IIHNP 228
Cdd:COG4987 556 LLAQN 560
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-229 |
5.00e-51 |
|
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: 168.49 E-value: 5.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQ 84
Cdd:cd03218 5 NLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 165 SALDPLSREQLQKDIVQL-QKKIQktiVFVT-HDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
9.05e-51 |
|
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: 166.07 E-value: 9.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 5 NHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQ 84
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFphmtiaeniavvpemrqwskkdikarvdDLLHMvgldpdiyRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:cd03214 82 LELL----------------------------GLAHL--------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 165 SALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
9.56e-51 |
|
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: 167.20 E-value: 9.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN---INELRWDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKH--RALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDP-LSREqlqkdIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:cd03292 159 IADEPTGNLDPdTTWE-----IMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
2.20e-50 |
|
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: 164.34 E-value: 2.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 3 QFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVL 82
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 83 QqialfphmtiaeniavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVLMDE 162
Cdd:cd00267 80 Q-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 163 PFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 |
1.98e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 164.16 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDslhLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElRwDIGY 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIA--VVPEMRqWSKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGlgLRPGLK-LTAEQ-RAQVEQALERVGLAG--LLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
8.30e-49 |
|
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: 162.64 E-value: 8.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELrwdigYVLQQIALFPHMTIAENI 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 --AVVPEMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQL 175
Cdd:TIGR01184 76 alAVDRVLPDLSKSERRAIVEEHIALVGLTEA--ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1263193398 176 QKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEG 213
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-231 |
1.26e-48 |
|
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: 169.87 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETtEGSILIDGKDIQQYNINE---LRWDIgyvlqQI------- 85
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrpLRRRM-----QVvfqdpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIAvvpE-----MRQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:COG4172 374 SLSPRMTVGQIIA---EglrvhGPGLSAAERRARVAEALEEVGLDPA-ARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 161 DEPFSALDpLSreqLQKDIVQLQKKIQK----TIVFVTHDMQ--EALSlgDRICIMKEGKVVQLDTPEGIIHNPKNE 231
Cdd:COG4172 450 DEPTSALD-VS---VQAQILDLLRDLQRehglAYLFISHDLAvvRALA--HRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-222 |
1.88e-48 |
|
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: 161.38 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNInELRWDIGYV 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLE--AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-217 |
2.33e-48 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 162.22 E-value: 2.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK---AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNInelrwDI 78
Cdd:NF040729 2 LKIQNISKTFINNKKeneVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-----DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:NF040729 77 GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTG--KENLYPHQISGGMKQRTAVIRALACKPEVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIM--KEGKVVQ 217
Cdd:NF040729 155 LMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-228 |
2.42e-48 |
|
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: 165.27 E-value: 2.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 32 VLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ--QYNIN---ELRwDIGYVLQQIALFPHMTIAENIAVVpeMRQW 106
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsARGIFlppHRR-RIGYVFQEARLFPHLSVRGNLLYG--RKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 107 SKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKI 186
Cdd:COG4148 106 PRAERRISFDEVVELLGIGHLL--DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1263193398 187 QKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:COG4148 184 DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
4.27e-48 |
|
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: 158.19 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHMTIAENI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYR--DRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-302 |
1.53e-47 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 161.79 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 9 KSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYVLQQIALF 88
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGE--AADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 169 PLSREQLqKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIihnpKNEFVEEFIGNRGRTWYEGK 248
Cdd:TIGR01188 157 PRTRRAI-WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL----KRRLGKDTLESRPRDIQSLK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 249 SVADVLP--LDESVQlegQALSLHASLQEALVRVRD-EEVVP-----VEENGQYIGALTSRH 302
Cdd:TIGR01188 232 VEVSMLIaeLGETGL---GLLAVTVDSDRIKILVPDgDETVPeiveaAIRNGIRIRSISTER 290
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
6.97e-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: 157.14 E-value: 6.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTK---AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWD 77
Cdd:cd03266 1 MITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEE--LLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 158 VLMDEPFSALDPLSREQLqKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03266 158 LLLDEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-217 |
5.25e-46 |
|
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: 155.78 E-value: 5.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYED--GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPhMTIAENI------AVVPEMRQWSKkdiKARVDDLLhmVGLdPDIYRDRMPD---ELSGGQKQRVGVVRA 150
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIrygkpdATDEEVEEAAK---KANIHDFI--MSL-PDGYDTLVGErgsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDM---QEAlslgDRICIMKEGKVVQ 217
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLstiRNA----DLIAVLQNGQVVE 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
5.54e-46 |
|
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: 154.66 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGeFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYV 81
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGD--RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-240 |
9.08e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 155.70 E-value: 9.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 11 YEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE-----TTEGSILIDGKDIQQYNIN--ELRWDIGYVLQ 83
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 84 QIALFPhMTIAENiaVVPEMRQWSKKDiKARVDDLLHMVGLDPDIY---RDRMPDE---LSGGQKQRVGVVRALAANPKI 157
Cdd:PRK14239 94 QPNPFP-MSIYEN--VVYGLRLKGIKD-KQVLDEAVEKSLKGASIWdevKDRLHDSalgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
...
gi 1263193398 238 GNR 240
Cdd:PRK14239 248 SGK 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-216 |
9.96e-46 |
|
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: 154.28 E-value: 9.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSY-EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03245 3 IEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAvvpeMRQWSKKDikARVDDLLHMVGLDPDIYR-----DRMPDE----LSGGQKQRVGVVRAL 151
Cdd:cd03245 83 VPQDVTLF-YGTLRDNIT----LGAPLADD--ERILRAAELAGVTDFVNKhpnglDLQIGErgrgLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIVQLqkKIQKTIVFVTHDMQeALSLGDRICIMKEGKVV 216
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-216 |
1.75e-45 |
|
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: 163.88 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSY-EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:TIGR03375 464 IEFRNVSFAYpGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVvpEMRQWSKKDI--KARVDDLLHMVGLDPDIYrDRMPDE----LSGGQKQRVGVVRALAAN 154
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIAL--GAPYADDEEIlrAAELAGVTEFVRRHPDGL-DMQIGErgrsLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKdivQLQKKIQ-KTIVFVTHDMQeALSLGDRICIMKEGKVV 216
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKD---RLKRWLAgKTLVLVTHRTS-LLDLVDRIIVMDNGRIV 678
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-217 |
8.44e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.93 E-value: 8.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElrwdiGY 80
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEG--AEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMK--EGKVVQ 217
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-217 |
1.52e-44 |
|
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: 151.61 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAvvpemrqWSKKDI-KARVDDLLHMVGLDPDIyrDRMPD-----------ELSGGQKQRVGVV 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIA-------YGRPGAtREEVEEAARAANAHEFI--MELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHdmqeALSL---GDRICIMKEGKVVQ 217
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH----RLSTienADRIVVLEDGKIVE 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-207 |
3.64e-44 |
|
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: 149.99 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 3 QFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQynineLRWDIGYVL 82
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 83 QQIAL---FPhMTIAENIAV--VPEMR--QWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMglYGHKGlfRRLSKADKAKVDEALERVGLSE--LADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRI 207
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
4.83e-44 |
|
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: 148.52 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMqEALSLGDRICIMKEGKV 215
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
20-216 |
5.47e-44 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 149.78 E-value: 5.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 20 SLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI---QQYNINELRWDIGYVLQQIALFPHMTIAEN 96
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaSKKQLVQLRRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 97 IAVVPEM-RQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDplsrEQL 175
Cdd:TIGR02982 103 VQMALELqPNLSYQEARERARAMLEAVGLGDHL--NYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALD----SKS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1263193398 176 QKDIVQLQKKIQK----TIVFVTHDmQEALSLGDRICIMKEGKVV 216
Cdd:TIGR02982 177 GRDVVELMQKLAKeqgcTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 |
5.70e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINrLIETTE------GSILIDGK---DIQQYNI 71
Cdd:PRK11264 3 AIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEagtirvGDITIDTArslSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 72 NELRWDIGYVLQQIALFPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRA 150
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPvIVKGEPKEEATARARELLAKVGLAGK--ETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKN 230
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
250
....*....|...
gi 1263193398 231 E----FVEEFIGN 239
Cdd:PRK11264 238 PrtrqFLEKFLLQ 250
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-222 |
7.91e-44 |
|
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: 150.07 E-value: 7.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENI------AVVPEMRQWSKkdiKARVDDLLhmVGLdPDIYrDRMPDE----LSGGQKQRVGVVRAL 151
Cdd:cd03253 81 PQDTVLF-NDTIGYNIrygrpdATDEEVIEAAK---AAQIHDKI--MRF-PDGY-DTIVGErglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTPE 222
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-222 |
8.56e-44 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 149.17 E-value: 8.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMK-MINRLIE--TTEGSILIDGKDIQQYNINELRwdIGYVLQQIALFPHMTIA 94
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 95 ENIAV-VPemRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSRE 173
Cdd:COG4136 95 ENLAFaLP--PTIGRAQRRARVEQALEEAGLAG--FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 174 QLQKDIVQLQKKIQKTIVFVTHDMQEALSlgdricimkEGKVVQLDTPE 222
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQ 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-229 |
1.97e-43 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 151.78 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---RWDIGYVLQQ--IALFPH 90
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIA-----VVPEMrqwSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:PRK15079 115 MTIGEIIAeplrtYHPKL---SRQEVKDRVKAMMLKVGLLPNLI-NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 166 ALDPlsreQLQKDIVQLQKKIQK----TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:PRK15079 191 ALDV----SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-234 |
7.11e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.85 E-value: 7.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINrLIET-TEGSILIDG------KDIQQYNINEL 74
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLETpDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAA 153
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTD--KADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKK-IqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEF 232
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTgI--TQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQTEAF 236
|
..
gi 1263193398 233 VE 234
Cdd:COG4161 237 AH 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-240 |
8.42e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 147.75 E-value: 8.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 15 TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE-----TTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFP 89
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIAVVPEMRQW--SKKDIKARVDDLLHMVGLDPDIyRDRM---PDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:PRK14247 96 NLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEV-KDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 165 SALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGNR 240
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTGR 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
1.27e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 148.31 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTK-----AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ-QYNINEL 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQ----QIAlfphMTIAE-NIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVR 149
Cdd:PRK13633 84 RNKAGMVFQnpdnQIV----ATIVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYE--YRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTPEGI 224
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-240 |
3.32e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 146.35 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 11 YEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGK------DIQQYNINELRWDIGYVLQQ 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAV-VPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRM---PDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:PRK14246 99 PNPFPHLSIYDNIAYpLKSHGIKEKREIKKIVEECLRKVGLWKEVY-DRLnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGNR 240
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIGR 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
3.42e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.09 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIG 79
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQW---SKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDP--DTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 |
4.02e-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: 144.54 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGY 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVpeMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFW--AALYGLRADREAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1263193398 161 DEPFSALDPLSREQLQkDIVQLQKKIQKTIVFVTHD 196
Cdd:COG4133 156 DEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-227 |
1.27e-41 |
|
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: 143.73 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQIALF 88
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVPEMRqwSKKDIKARVDDLLHMVgldPDIY--RDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:cd03224 88 PELTVEENLLLGAYAR--RRAKRKARLERVYELF---PRLKerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 167 LDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHN 227
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-237 |
1.39e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 144.60 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDslhLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE-----TTEGSILIDGKDIQQYNIN--ELRWDIGYVLQQIALF 88
Cdd:PRK14267 21 KGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVPEMRQW--SKKDIKARVDDLLHMVGLDPDIyRDRM---PDELSGGQKQRVGVVRALAANPKIVLMDEP 163
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEV-KDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 164 FSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-228 |
1.65e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 145.13 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN-INELRWDIG 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIAL-FPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEK--YRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEaLSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-222 |
3.48e-41 |
|
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: 142.75 E-value: 3.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHmTIAENIAVvpeMRQWSKKDikaRVDDLLHMVGLDPDIYR-----DRMPDE----LSGGQKQRVGVVRALA 152
Cdd:cd03254 83 LQDTFLFSG-TIMENIRL---GRPNATDE---EVIEAAKEAGAHDFIMKlpngyDTVLGEnggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 153 ANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDM---QEAlslgDRICIMKEGKVVQLDTPE 222
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLstiKNA----DKILVLDDGKIIEEGTHD 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-228 |
8.23e-41 |
|
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: 145.25 E-value: 8.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 33 LIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ------QYNINELRwdIGYVLQQIALFPHMTIAENIavVPEMRQW 106
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPEKRR--IGYVFQEARLFPHLSVRGNL--RYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 107 SKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKI 186
Cdd:TIGR02142 104 RPSERRISFERVIELLGIGHLL--GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1263193398 187 QKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.99e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 142.85 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ----QYNINE 73
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 74 LRWDIGYVLQqialFPHM-----TIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyRDRMPDELSGGQKQRVGVV 148
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEEL-LARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
2.85e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.18 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTK--AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDI 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQI-ALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQD--FKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEaLSLGDRICIMKEGKVVQLDTPE 222
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPR 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-217 |
2.95e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 140.92 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDG------KDIQQYNINELR 75
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 76 WDIGYVLQQIALFPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKP--YADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQK-KIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAEtGI--TQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-240 |
3.40e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 141.46 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINR---LIET--TEGSILIDGKDIQQYNIN--ELRWDIGYVLQQIALFP 89
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HmTIAENIAVVPEMRQWsKKDIKARVDDLLHMVGLdPDIYRDRMPDE---LSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:PRK14243 105 K-SIYDNIAYGARINGY-KGDMDELVERSLRQAAL-WDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 167 LDPLSREQLQKDIVQLqkKIQKTIVFVTHDMQEALSLGDRICIM---------KEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK14243 182 LDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
...
gi 1263193398 238 GNR 240
Cdd:PRK14243 260 SGR 262
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
6.61e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 141.09 E-value: 6.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLI---ETTEGSILIDGKDIQQYNINELRWD 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQI-ALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVG-LDpdiYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmLD---YIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEAlSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
9.66e-40 |
|
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: 139.83 E-value: 9.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEG-SILIDGKDIQQYNINELRWDIG 79
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YV---LQQiaLFPHMTIAENI------AVVPEMRQWSKKDIkARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRA 150
Cdd:COG1119 82 LVspaLQL--RFPRDETVLDVvlsgffDSIGLYREPTDEQR-ERARELLELLGLAH--LADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
3.09e-39 |
|
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: 136.98 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYedGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE----LRWDIGY 80
Cdd:TIGR03608 3 NISKKF--GDKVIlDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDpdIYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLN--LKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMqEALSLGDRI 207
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-217 |
4.05e-39 |
|
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: 144.51 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHmTIAENI 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AVVPEMRqwSKKDIKA----RVDDL-LHMvgldPDIYrDRMPDE----LSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:COG4618 427 ARFGDAD--PEKVVAAaklaGVHEMiLRL----PDGY-DTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 169 PLSREQLQKDIVQLqKKIQKTIVFVTHDMQeALSLGDRICIMKEGKVVQ 217
Cdd:COG4618 500 DEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
6.24e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK-AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQ----QialFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK13635 86 VFQnpdnQ---FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMED--FLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTPEGI 224
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-238 |
6.39e-39 |
|
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: 137.04 E-value: 6.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIG 79
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQwSKKDIKARVDDLLHMVgldPDIY--RDRMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELF---PRLKerRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPknEFVEEFI 237
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EVREAYL 234
|
.
gi 1263193398 238 G 238
Cdd:COG0410 235 G 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
1.13e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 137.14 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGy 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQ---IAL------------FPHmtiaeniavvpemrqwSK----KDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQ 141
Cdd:COG4604 79 ILRQenhINSrltvrelvafgrFPY----------------SKgrltAEDREIIDEAIAYLDLED--LADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 142 KQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
....
gi 1263193398 222 EGII 225
Cdd:COG4604 221 EEII 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
1.68e-38 |
|
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: 135.04 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRwDIGYV 81
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALR-RIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKdikaRVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKD--SAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-229 |
2.23e-38 |
|
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: 142.13 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 15 TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRL----IETTEGSILIDGKDIQQYNINELRW----DIGYVLQQ-- 84
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDE 162
Cdd:COG4172 103 TSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 163 PFSALDPLsreqLQKDIVQLQKKIQKT----IVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG4172 183 PTTALDVT----VQAQILDLLKDLQRElgmaLLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
2.23e-38 |
|
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: 134.69 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyniNELRWDIGYVLQ-- 83
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 84 QIALFPHmTIAENIAVvpemrqwSKKDI---KARVDDLLHMvgLDPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03226 81 DYQLFTD-SVREELLL-------GLKELdagNEQAETVLKD--LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-221 |
2.90e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.83 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI----QQYNINE 73
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 74 LRWDIGYVLQqialFPHMTIAEN-----IAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVV 148
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-225 |
6.56e-38 |
|
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: 140.71 E-value: 6.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSY---EDGT-KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiQQYNINELRW 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGD-EWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 D--------IGYVLQQIALFPHMTIAENI--AVVPEMrqwSKKDIKARVDDLLHMVGLDPDIYR---DRMPDELSGGQKQ 143
Cdd:TIGR03269 358 DgrgrakryIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKAEeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 144 RVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEG 223
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
..
gi 1263193398 224 II 225
Cdd:TIGR03269 515 IV 516
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
7.22e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.59 E-value: 7.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN--INELRWDI 78
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQI--ALFPHmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEG--FENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-236 |
1.37e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 133.87 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQ 84
Cdd:PRK10895 8 NLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAVVPEMRQ-WSKKDIKARVDDLL---HMVGLdpdiyRDRMPDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMeefHIEHL-----RDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 161 DEPFSALDPLSREQLQKdIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFV---EEF 236
Cdd:PRK10895 162 DEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVylgEDF 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.37e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.86 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQI--ALFPhMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVL 159
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWD--FRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-216 |
1.44e-37 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 133.25 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE---L 74
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKgvsLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErakL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 R-WDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAA 153
Cdd:TIGR02211 81 RnKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRI--NHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLgDRICIMKEGKVV 216
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-216 |
1.69e-37 |
|
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: 132.62 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYedGTKAVDsLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELrwDIGYV 81
Cdd:cd03298 1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR--PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENI--AVVPEMRQWSKKdiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVL 159
Cdd:cd03298 76 FQENNLFAHLTVEQNVglGLSPGLKLTAED--RQAIEVALARVGLAG--LEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
2.77e-37 |
|
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: 132.94 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQynINE---- 73
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKgisLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDEdara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 74 -LRWD-IGYVLQQIALFPHMTIAENIAVVPEMRqwSKKDIKARVDDLLHMVGLDpdiyrDRM---PDELSGGQKQRVGVV 148
Cdd:COG4181 86 rLRARhVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLG-----HRLdhyPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEAlSLGDRICIMKEGKVVQ 217
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
2.78e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 133.62 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE-----TTEGSILIDGKDI--QQYNINEL 74
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 RWDIGYVLQQIALFPhMTIAENIAVVPEMRQWSKKdikARVDDLLHMVGLDPDIYRD------RMPDELSGGQKQRVGVV 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPK---LEIDDIVESALKDADLWDEikhkihKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKE-----GKVVQLDTPEG 223
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
250
....*....|....*..
gi 1263193398 224 IIHNPKNEFVEEFIGNR 240
Cdd:PRK14258 243 IFNSPHDSRTREYVLSR 259
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-218 |
3.67e-37 |
|
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: 131.91 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQynINELRWDIGYVLQQIALFPHMTIAENIA--VV 100
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSMLFQENNLFAHLTVRQNIGlgLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 101 PEMRQWSKKdiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIV 180
Cdd:TIGR01277 97 PGLKLNAEQ--QEKVVDAAQQVGIAD--YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1263193398 181 QLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQL 218
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-215 |
5.05e-37 |
|
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: 138.63 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHmTIAENIAVV 100
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVAENIARF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 101 PEMRQWSKKDIKARVDDLLHMV-----GLDPDIYRDRMPdeLSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQL 175
Cdd:TIGR01842 416 GENADPEKIIEAAKLAGVHELIlrlpdGYDTVIGPGGAT--LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQAL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1263193398 176 QKDIVQLQKKiQKTIVFVTHDMQeALSLGDRICIMKEGKV 215
Cdd:TIGR01842 494 ANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
5.89e-37 |
|
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: 129.86 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGY 80
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQqialfphmtiaeniavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03216 80 VYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-231 |
6.13e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 132.65 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT--------KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE 73
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 74 LRWDIGYVLQ--QIALFPHMTIAEnIAVVPEMR--QWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVR 149
Cdd:COG4167 85 RCKHIRMIFQdpNTSLNPRLNIGQ-ILEEPLRLntDLTAEEREERIFATLRLVGLLPE-HANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQ 242
|
..
gi 1263193398 230 NE 231
Cdd:COG4167 243 HE 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
6.57e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 132.52 E-value: 6.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqyninelRW 76
Cdd:COG1101 1 MLELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-------KL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 -------DIGYVLQ--QIALFPHMTIAEN--------------IAVVPEMRQWSKKDIKarvddLLHMvGLDpdiyrDRM 133
Cdd:COG1101 74 peykrakYIGRVFQdpMMGTAPSMTIEENlalayrrgkrrglrRGLTKKRRELFRELLA-----TLGL-GLE-----NRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 134 PDE---LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQ---LQKDIVQlQKKIqkTIVFVTHDMQEALSLGDRI 207
Cdd:COG1101 143 DTKvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALvleLTEKIVE-ENNL--TTLMVTHNMEQALDYGNRL 219
|
250
....*....|..
gi 1263193398 208 CIMKEGKVVqLD 219
Cdd:COG1101 220 IMMHEGRII-LD 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
1.27e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.08 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqQYNINE----LRW 76
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQQIALFPHMTIAENIAV-VPEMRQW--SKKDIKARVDDLLHMVGL--DPdiyrDRMPDELSGGQKQRVGVVRAL 151
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLgLEPTKGGrlDRKAARARIRELSERYGLdvDP----DAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-196 |
2.45e-36 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 129.08 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 11 YEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGK--DIQQYNINELRWDIGYVLQ----Q 84
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQdpddQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IaLFPhmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:TIGR01166 81 L-FAA--DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASG--LRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1263193398 165 SALDPLSREQLQKDIVQLQKKiQKTIVFVTHD 196
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAE-GMTVVISTHD 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-235 |
3.15e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 131.41 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElrwD 77
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNK---D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIAL---FPHM-----TIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVR 149
Cdd:PRK13649 80 IKQIRKKVGLvfqFPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLF-EKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHnpK 229
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ--D 235
|
....*.
gi 1263193398 230 NEFVEE 235
Cdd:PRK13649 236 VDFLEE 241
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
23-242 |
3.33e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 130.69 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGK---------------DIQQynINELRWDIGYVLQQIAL 87
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelvpaDRRQ--LQRIRTRLGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 88 FPHMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLdPDIyRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:COG4598 107 WSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGL-ADK-RDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 167 LDP-LSREQLqKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGNRGR 242
Cdd:COG4598 185 LDPeLVGEVL-KVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSLK 259
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
6.04e-36 |
|
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: 135.49 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHmTIAENIAVvpemrqwSKKDIK-ARVDDLLHMVGLD------PDIYrDRMPDE----LSGGQKQRVGVVRA 150
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRL-------ARPDASdAEIREALERAGLDefvaalPQGL-DTPIGEggagLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMqEALSLGDRICIM 210
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRL-ALAALADRIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-237 |
9.27e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 129.70 E-value: 9.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ-------------QYNINELRWDIGYVLQQIALFP 89
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIAVVP-EMRQWSKKDIKARVDDLLHMVGLDpDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:PRK10619 106 HMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 169 PlsreQLQKDIVQLQKKIQ---KTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK10619 185 P----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
1.42e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 128.98 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRwdigy 80
Cdd:PRK11231 2 TLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 vlQQIALFP-HMTIAENIAV--------VPEMRQW---SKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVV 148
Cdd:PRK11231 76 --RRLALLPqHHLTPEGITVrelvaygrSPWLSLWgrlSAED-NARVNQAMEQTRINH--LADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 149 RALAANPKIVLMDEPFSALDpLSRE-QLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-229 |
1.62e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ----QYNINE 73
Cdd:PRK13641 3 IKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 74 LRWDIGYVLQ--QIALFPHmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVRAL 151
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLI-SKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
2.61e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.54 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKA--DAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-227 |
9.92e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.82 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDG-------KDIQQyn 70
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 71 INELRWDIGYVLQ--QIALFPHmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLdPDIYRDRMPDELSGGQKQRVGVV 148
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 149 RALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHN 227
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-217 |
1.68e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.73 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGT-------KAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN-- 70
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhqhQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 71 -INELRWDIGYVLQQI--ALFPHMTIAENIAvvPEMRQW---SKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQR 144
Cdd:PRK10419 83 qRKAFRRDIQMVFQDSisAVNPRKTVREIIR--EPLRHLlslDKAERLARASEMLRAVDLDDSVL-DKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 145 VGVVRALAANPKIVLMDEPFSALDPLsreqLQKDIVQLQKKIQK----TIVFVTHDmqeaLSLGDRIC----IMKEGKVV 216
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLV----LQAGVIRLLKKLQQqfgtACLFITHD----LRLVERFCqrvmVMDNGQIV 231
|
.
gi 1263193398 217 Q 217
Cdd:PRK10419 232 E 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.68e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.84 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQ----QIAlfpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK13652 83 VFQnpddQIF---SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEE--LRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
2.55e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.12 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT----KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQ--------- 68
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 69 ---------------YNINELRWDIGYVLQ--QIALFpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDiYRD 131
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDES-YLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 132 RMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPlsreQLQKDIVQLQKKIQ---KTIVFVTHDMQEALSLGDRIC 208
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNkqgKTIILVTHDLDNVLEWTKRTI 236
|
250 260
....*....|....*....|....*..
gi 1263193398 209 IMKEGKVVQLDTPEGIIHNpkNEFVEE 235
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSD--NKFLIE 261
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-217 |
3.93e-34 |
|
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: 124.91 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDE----LSGGQKQRVGVVRALAANPK 156
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGY-DTIVGEqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMQeALSLGDRICIMKEGKVVQ 217
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLS-TVKNADRIIVMEKGRIVE 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-221 |
1.27e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.02 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 5 NHVSKSYedGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDgkdiqQYNINELRWDIGYVLQ 83
Cdd:PRK11247 16 NAVSKRY--GERTVlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 84 QIALFPHMTIAENIAVvpemrqWSKKDIKARVDDLLHMVGLDpdiyrDRM---PDELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:PRK11247 89 DARLLPWKKVIDNVGL------GLKGQWRDAALQALAAVGLA-----DRAnewPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKV---VQLDTP 221
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLP 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-238 |
1.84e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 130.24 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSIL-----IDGKDIqqyninELRWDIGYVLQQIALFPHM 91
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDI------ATRRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 TIAENIAV------VPEmrqwskKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVgvvrALAA----NPKIVLMD 161
Cdd:NF033858 355 TVRQNLELharlfhLPA------AEIAARVAEMLERFDLAD--VADALPDSLPLGIRQRL----SLAVavihKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKIQKTIvFV-THDMQEALSLgDRICIMKEGKVVQLDTPEGIIHNPKNEFVEE-FIG 238
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVTI-FIsTHFMNEAERC-DRISLMHAGRVLASDTPAALVAARGAATLEEaFIA 499
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.74e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.80 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGK--DIQQYNINELRWDI 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 GYVLQQI--ALFPhMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK13636 85 GMVFQDPdnQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-215 |
3.38e-33 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.74 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqYNINELRwDIGYV 81
Cdd:TIGR03740 1 LETKNLSKRFGKQT-AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDLH-KIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKkdikARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNT--GKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKdIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:TIGR03740 150 EPTNGLDPIGIQELRE-LIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-199 |
3.62e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 121.74 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHmT 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENIAVVPEMRQwSKKDIKARVDDLLHMvGLDPDIYRDRMpDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSR 172
Cdd:PRK10247 97 VYDNLIFPWQIRN-QQPDPAIFLDDLERF-ALPDTILTKNI-AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....*..
gi 1263193398 173 EQLQKDIVQLQKKIQKTIVFVTHDMQE 199
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-221 |
6.38e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.51 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 12 EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQI-ALFPH 90
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIAVVPEMRQWSKKDIKARVDDLLHMVG-LDpdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNmLD---FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 170 LSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTP 221
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-214 |
7.14e-33 |
|
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: 120.27 E-value: 7.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDG----TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwd 77
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPhMTIAENIavvpemrQWSKKDIKARVDDLLHMVGLDPDIyrDRMPD-------E----LSGGQKQRVG 146
Cdd:cd03250 68 IAYVSQEPWIQN-GTIRENI-------LFGKPFDEERYEKVIKACALEPDL--EILPDgdlteigEkginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 147 VVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQeALSLGDRICIMKEGK 214
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.33e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.40 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:PRK13648 7 IIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIA-LFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE--RADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTPEGI 224
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-221 |
2.04e-32 |
|
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: 127.44 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYVLQQIALFPHMTI 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 94 AENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSRE 173
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1263193398 174 QLQkDIVqLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:TIGR01257 1099 SIW-DLL-LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-237 |
2.49e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 126.12 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQ---YNINELRWDIGYVLQQ--IALFPHM 91
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 TIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPL 170
Cdd:PRK10261 419 TVGDSIMEPLRVhGLLPGKAAAARVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 171 SREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-228 |
2.83e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 122.68 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 35 GPSGCGKTTTMKMINRLIETTEGSILIDGK---DIQQyNIN---ELRwDIGYVLQQIALFPHMTIAENiavvpeMRQWSK 108
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK-GIClppEKR-RIGYVFQDARLFPHYKVRGN------LRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 109 KDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD-PLSRE---QLQKdivqLQK 184
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLL--DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLER----LAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1263193398 185 KIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-215 |
2.96e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.22 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 7 VSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIGYVLQQI 85
Cdd:COG4674 16 LTVSF-DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIaRLGIGRKFQKP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIA--------VVPEMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQR--VGVVraLAANP 155
Cdd:COG4674 95 TVFEELTVFENLElalkgdrgVFASLFARLTAEERDRIEEVLETIGLTDK--ADRLAGLLSHGQKQWleIGML--LAQDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:COG4674 171 KLLLLDEPVAGMTDAETERTAELLKSLAGK--HSVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
3.84e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDslhLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqQYNINELRWDIGY 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHMTIAENIA--VVPEMRQWSKKdiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGlgLNPGLKLNAAQ--REKLHAIARQMGIED--LLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDP-LSREQLQ--KDIVQLQkkiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK10771 152 LLDEPFSALDPaLRQEMLTlvSQVCQER---QLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-217 |
4.85e-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: 118.78 E-value: 4.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 3 QFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIGYV 81
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDL---LHMVgldpdiyRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELfpvLKEM-------LGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-229 |
7.11e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 7.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINrLIET-TEGSILIDGKDIQQYN---INELRWDIGYVLQQ--IALFP 89
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETpTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNpyGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTI----AENIAVVPEMrqwSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:PRK11308 108 RKKVgqilEEPLLINTSL---SAAERREKALAMMAKVGLRPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 166 ALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPK 229
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
7.58e-32 |
|
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: 117.03 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSY-EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWDIGY 80
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVvpemrqwskkdikarvddllhmvgldpdiyrdrmpdELSGGQKQRVGVVRALAANPKIVLM 160
Cdd:cd03247 80 LNQRPYLF-DTTLRNNLGR------------------------------------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQeALSLGDRICIMKEGKVV 216
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-237 |
1.30e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 123.66 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETtEGSILIDGKDIQQYNINEL---RWDIGYVLQ--QIALFPHM 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 T----IAENIAVvpEMRQWSKKDIKARVDDLLHMVGLDPDIyRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSAL 167
Cdd:PRK15134 380 NvlqiIEEGLRV--HQPTLSAAQREQQVIAVMEEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 168 DplsrEQLQKDIVQLQKKIQKT----IVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK15134 457 D----KTVQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-217 |
1.47e-31 |
|
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: 124.47 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHmTIAENIaVVPEMRQWSKKDIKARVDdllhMVGLDPDI------YRDRMPDE---LSGGQKQRVGVVRALA 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENL-LLGAKENVSQDEIWAACE----IAEIKDDIenmplgYQTELSEEgssISGGQKQRIALARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 153 ANPKIVLMDEPFSALDPLSREQLQKDIVQLQkkiQKTIVFVTHDMQEAlSLGDRICIMKEGKVVQ 217
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIE 688
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-226 |
2.83e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 118.68 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYED----GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSI----LIDGKDIQQYNIN 72
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 73 ELRWDIGYVLQ--QIALFPHmTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrDRMPDELSGGQKQRVGVVRA 150
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFW-EKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIH 226
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
3.07e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.52 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---Rwd 77
Cdd:COG4559 1 MLEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarrR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 igYVL-QQIAL-FPhMTIAEniaVVpEM----RQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRAL 151
Cdd:COG4559 78 --AVLpQHSSLaFP-FTVEE---VV-ALgrapHGSSAAQDRQIVREALALVGLAH--LAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 152 A-------ANPKIVLMDEPFSALDPlsREQLQkdIVQLQKKI--QKTIVF-VTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDL--AHQHA--VLRLARQLarRGGGVVaVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
.
gi 1263193398 222 E 222
Cdd:COG4559 225 E 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-216 |
3.24e-31 |
|
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: 115.73 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMIN--RLIETTEGSILIDGKDIQQYNINELrwdIG 79
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSFRKI---IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVL 159
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRG-------------------------------LSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHD-MQEALSLGDRICIMKEGKVV 216
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-240 |
3.76e-31 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 116.70 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIET----TEGSILIDGKDiqqYNINELRW-DIGYVLQ--QIALFP 89
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRP---LLPLSIRGrHIATIMQnpRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 169 PLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIGNR 240
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-217 |
4.51e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.38 E-value: 4.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENI------AVVPEMRQWSKKD-----IKARVDDLLHMVGldpdiYRDRMpdeLSGGQKQRVGVVRA 150
Cdd:PRK13657 415 FQDAGLF-NRSIEDNIrvgrpdATDEEMRAAAERAqahdfIERKPDGYDTVVG-----ERGRQ---LSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 151 LAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDM---QEAlslgDRICIMKEGKVVQ 217
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLstvRNA----DRILVFDNGRVVE 549
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
5.65e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.24 E-value: 5.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGT-KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIAVVpemrqwSKKDIKARVDDLLHMVGLDPDIYRDRMPD--------ELSGGQKQRVGVVRALA 152
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKGLNawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 153 ANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQeALSLGDRICIMKEGKVV 216
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQII 552
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-228 |
9.02e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.24 E-value: 9.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL-RWDIGYVLQQIALFPHMT 92
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENIAV----------------VPEMRQwSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK11300 97 VIENLLVaqhqqlktglfsgllkTPAFRR-AESEALDRAATWLERVGLLE--HANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-237 |
1.18e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 116.40 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 19 DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---RWDIGYVLQQIALFPHMTIAE 95
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 96 NIAV-VPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQ 174
Cdd:PRK11831 104 NVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAA--KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 175 LQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEfVEEFI 237
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.55e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKA--DARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
1.60e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.97 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE---LRWD 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLdPDIYRDrMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGL-LDKAKN-FPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 158 VLMDEPFSALDplsrEQLQKDIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK10908 159 LLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.77e-30 |
|
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: 120.16 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENIAVvpemrqwSKKDI-KARVDDLLHMVGLDPDIyrDRMPD-----------ELSGGQKQRVGVVR 149
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRL-------ARPDAtDEELWAALERVGLADWL--RALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIvqLQKKIQKTIVFVTHD 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-228 |
2.02e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.87 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILID----GKDIQQY------------NINELRWDIG 79
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQqialFPHM-----TIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:PRK13631 120 MVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDS-YLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 155 PKIVLMDEPFSALDPlSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK13631 195 PEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
4.25e-30 |
|
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: 113.74 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIAvvPEmRQWSKKDI---------KARVDDLLhmVGLDPDIyrDRMPDELSGGQKQRVGVVRAL 151
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLD--PF-GEYSDEELwqalervglKEFVESLP--GGLDTVV--EEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIvqlQKKI-QKTIVFVTHDMQEALSLgDRICIMKEGKVVQLDTP 221
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTI---REAFkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-216 |
8.16e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.06 E-value: 8.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL--- 74
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKgisLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 -RWDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAA 153
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV--EYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEAlSLGDRICIMKEGKVV 216
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-238 |
8.21e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.42 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEG-----SILIDGKDIQQY-NINELRWDIGYVLQQIAL 87
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 88 FPhMTIAENI-AVVPEMRQWSKKDIKARVDDLLHMVGLdPDIYRDRMPD---ELSGGQKQRVGVVRALAANPKIVLMDEP 163
Cdd:PRK14271 113 FP-MSIMDNVlAGVRAHKLVPRKEFRGVAQARLTEVGL-WDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 164 FSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-217 |
3.50e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 117.04 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDG-TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFpHMTIAENIAVVPEmRQWSKKDIK--AR-------VDDLLHmvGLDPDIYRDRMpdELSGGQKQRVGVVRAL 151
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYART-EQYSREQIEeaARmayamdfINKMDN--GLDTVIGENGV--LLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 152 AANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQeALSLGDRICIMKEGKVVQ 217
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-240 |
5.88e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHMT 92
Cdd:PRK10253 18 GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENIAV-----VPEMRQWSKKDIKArVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSAL 167
Cdd:PRK10253 98 VQELVARgryphQPLFTRWRKEDEEA-VTKAMQATGITH--LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 168 DPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIhnpKNEFVEEFIGNR 240
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV---TAELIERIYGLR 244
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
7.12e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 7.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---Rwd 77
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 igYVL-QQIAL-FPhMTIAEniaVVpEM----RQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRAL 151
Cdd:PRK13548 79 --AVLpQHSSLsFP-FTVEE---VV-AMgrapHGLSRAEDDALVAAALAQVDLAH--LAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 152 A------ANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
1.93e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.58 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIG 79
Cdd:PRK11614 5 MLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAV---VPEMRQWSKKdiKARVDDLLhmvgldPDIYRDRM--PDELSGGQKQRVGVVRALAAN 154
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMggfFAERDQFQER--IKWVYELF------PRLHERRIqrAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHN 227
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-220 |
6.02e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 113.66 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK--AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHmTIAENIAV---VPEMRQWSKKDIKARVDDLlhmVGLDPDIYrDRMPDE----LSGGQKQRVGVVRALA 152
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYgltDTPDEEIMAAAKAANAHDF---IMEFPNGY-DTEVGEkgsqLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 153 ANPKIVLMDEPFSALDPLSREQLQkdivQLQKKIQKTIVFVTHDmqeaLSL---GDRICIMKEGKVVQLDT 220
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHR----LSTverADQILVLKKGSVVEMGT 696
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
1.45e-27 |
|
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: 107.17 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYED--GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHmTIAENIAV----VPEMRQWSKKDiKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYglqsCSFECVKEAAQ-KAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKiqKTIVFVTHDMQeALSLGDRICIMKEGKV 215
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-202 |
3.11e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqyninelrwDIGYVLQQIAL---FP 89
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 hMTIAEniAVvpEMRQWSK--------KDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:NF040873 72 -LTVRD--LV--AMGRWARrglwrrltRDDRAAVDDALERVGLAD--LAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALS 202
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-237 |
4.26e-27 |
|
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: 111.64 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIG 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDpdIYRDRMPDELSGGQKQRVGVVRALAANPKIVL 159
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS--LYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLdtpeGIIHNPKNEFVEEFI 237
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCL----GTIQHLKSKFGDGYI 2166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
4.35e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.64 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN---INELrwD 77
Cdd:PRK09700 5 YISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAV----------VPeMRQWSKKDIKARVddLLHMVGLDPDIyrDRMPDELSGGQKQRVGV 147
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhltkkvcgVN-IIDWREMRVRAAM--MLLRVGLKVDL--DEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.18e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSY-----EDG---------------TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSIL 60
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 61 IDGKDIQQyNINELRWDIGYVL---QQiaLFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDEL 137
Cdd:COG4586 81 VLGYVPFK-RRKEFARRIGVVFgqrSQ--LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGE--LLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 138 SGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQ--EALSlgDRICIMKEGKV 215
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEALC--DRVIVIDHGRI 233
|
.
gi 1263193398 216 V 216
Cdd:COG4586 234 I 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-216 |
1.28e-26 |
|
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: 104.72 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSY-----EDGTK---------------AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILI 61
Cdd:cd03267 1 IEVSNLSKSYrvyskEPGLIgslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 62 DGKDIQQYNINELRwDIGYVL-QQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGG 140
Cdd:cd03267 81 AGLVPWKRRKKFLR-RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELL--DTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 141 QKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-216 |
2.82e-26 |
|
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: 103.50 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE---TTEGSILIDGkdiQQYNINELRWDIGYVLQQIALFPHMTIAENI 97
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AVVPEMR---QWSKKDIKARVDDLLHMVGLDPDIYRDRMPDeLSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQ 174
Cdd:cd03234 103 TYTAILRlprKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1263193398 175 LQKDIVQLQKKiqKTIVFVT-HdmQ---EALSLGDRICIMKEGKVV 216
Cdd:cd03234 182 LVSTLSQLARR--NRIVILTiH--QprsDLFRLFDRILLLSSGEIV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-217 |
3.45e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNIN---EL 74
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHnvsFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 R-WDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRdrMPDELSGGQKQRVGVVRALAA 153
Cdd:PRK11629 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANH--RPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLgDRICIMKEGKVVQ 217
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
3.59e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.32 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLI---ETTEGSILIDGKDIQQY-----NIN 72
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlarDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 73 ELRWDIGYVLQQIALFPHMTIAENIAV-----VPEMR---QWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQR 144
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIgalgsTPFWRtcfSWFTREQKQRALQALTRVGMVH--FAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 145 VGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
3.64e-26 |
|
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: 108.37 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFpHMTIAENIAV-VPEMrqwSKKDIK--ARVDDLLHMVGLDPDIYrDRMPDE----LSGGQKQRVGVVRALAAN 154
Cdd:COG5265 438 PQDTVLF-NDTIAYNIAYgRPDA---SEEEVEaaARAAQIHDFIESLPDGY-DTRVGErglkLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVfVTHdmqeALSL---GDRICIMKEGKVV 216
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAH----RLSTivdADEILVLEAGRIV 571
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.08e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRwdigy 80
Cdd:PRK09536 3 MIDVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 vlQQIALFPHMT-IAENIAV--VPEMRQ---------WSKKDIKArVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVV 148
Cdd:PRK09536 77 --RRVASVPQDTsLSFEFDVrqVVEMGRtphrsrfdtWTETDRAA-VERAMERTGVAQ--FADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 149 RALAANPKIVLMDEPFSALDpLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-234 |
1.79e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 103.67 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE----TTEGSILIDGKDIQQYNINELRWDIGYVLQQI------ 85
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIfqdpmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIAVVPEMRQW-SKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEP 163
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 164 FSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVE 234
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
2.55e-25 |
|
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: 100.97 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYE----DGTK--AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKD-------IQ 67
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 68 QYNINELRWD-IGYVLQQIALFPHMTiaeNIAVVPE---MRQWSKKDIKARVDDLLHMVGLDP---DIYrdrmPDELSGG 140
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVS---ALDVVAEpllERGVDREEARARARELLARLNLPErlwDLP----PATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 141 QKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLqKDIVQlQKKIQKT-IVFVTHDMQEALSLGDRICIMKEG 213
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIE-EAKARGTaIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-217 |
2.57e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 3 QFNHVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYV 81
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAV--VPEMRQW-SKKDIKARVDDLLHMVGLDPDiyrdrmPD----ELSGGQKQRVGVVRALAAN 154
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLgqLPHKGGIvNRRLLNYEAREQLEHLGVDID------PDtplkYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ 217
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-200 |
4.04e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.62 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSL---HLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNIN---EL 74
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILtgvELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 75 R-WDIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAA 153
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRL--DHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEA 200
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-215 |
5.09e-25 |
|
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: 99.04 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVL---QQIALFPHM 91
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 TIAENIAvvpemrqwskkdikarvddllhmvgldpdiyrdrMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLS 171
Cdd:cd03215 94 SVAENIA----------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1263193398 172 REQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-214 |
1.84e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.09 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE--TTEGSILIDGKDIQQYNINEL-RWD 77
Cdd:PRK13549 5 LLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTeRAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQWSKKD---IKARVDDLLHMVGLDPDIYRDRMpdELSGGQKQRVGVVRALAAN 154
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGGIMDydaMYLRAQKLLAQLKLDINPATPVG--NLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLqKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-234 |
2.94e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 15 TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSI-------------LIDGKDIQQYNINELRW-DIGY 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRGaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQ--IALFPHMTIAENIAVVPEMRQ-WSKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAANPK 156
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVE 234
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-219 |
7.43e-24 |
|
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: 96.83 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTK---------------------AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSIL 60
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 61 IDGKdiqqynineLRWDIGYvlqQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYrdrMP-DELSG 139
Cdd:cd03220 81 VRGR---------VSSLLGL---GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID---LPvKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 140 GQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLD 219
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-222 |
1.02e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 24 EIKKGEFFVLIGPSGCGKTTTMKMINRLIET---TEGSILIDGKDIqqyNINELRWDIGYVLQQIALFPHMTIAENIAVV 100
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 101 PEMR---QWSKKDIKARVDDLLHMVGL---------DPDIYRDrmpdeLSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:TIGR00955 124 AHLRmprRVTKKEKRERVDEVLQALGLrkcantrigVPGRVKG-----LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 169 PLSREQlqkdIVQLQKKIQ---KTIVFVTHD-MQEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:TIGR00955 199 SFMAYS----VVQVLKGLAqkgKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-228 |
1.04e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.55 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHMTIAENIAV- 99
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 100 -VP---EMRQWSKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQL 175
Cdd:PRK10575 110 rYPwhgALGRFGAAD-REKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 176 QKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-222 |
1.13e-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: 101.17 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFpHMTIAENI 97
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLF-EGTVRDNL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AV----VPE--MRQWSK-----KDIKARVDdllhmvGLDPDIYRDRMpdELSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:TIGR03796 574 TLwdptIPDadLVRACKdaaihDVITSRPG------GYDAELAEGGA--NLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 167 LDPLSreqlQKDIVQLQKKIQKTIVFVTHdmqeALSL---GDRICIMKEGKVVQLDTPE 222
Cdd:TIGR03796 646 LDPET----EKIIDDNLRRRGCTCIIVAH----RLSTirdCDEIIVLERGKVVQRGTHE 696
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-239 |
1.22e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.55 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqYNinelrwDIGYVLQQI---------A 86
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FG------DYSYRSQRIrmifqdpstS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 87 LFPHMTIAE--------NIAVVPEMRQwskkdikARVDDLLHMVGLDPDiYRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK15112 100 LNPRQRISQildfplrlNTDLEPEQRE-------KQIIETLRQVGLLPD-HASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFIG 238
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
.
gi 1263193398 239 N 239
Cdd:PRK15112 252 G 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-217 |
2.28e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.30 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTtmkMINRLIE--TTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFpH 90
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTS---LLNALLGflPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIAVV-PEMrqwSKKDI-----KARVDDLLHMV--GLDPDIyRDRMPDeLSGGQKQRVGVVRALAANPKIVLMDE 162
Cdd:PRK11174 437 GTLRDNVLLGnPDA---SDEQLqqaleNAWVSEFLPLLpqGLDTPI-GDQAAG-LSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 163 PFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMqEALSLGDRICIMKEGKVVQ 217
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQL-EDLAQWDQIWVMQDGQIVQ 563
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
3.95e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLH---------------------LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSI 59
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLKelllrrrrtrreefwalkdvsFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 60 LIDGKdiqqynineLRW--DIGYVLQqialfPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDrMP-DE 136
Cdd:COG1134 84 EVNGR---------VSAllELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGD--FID-QPvKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 137 LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
250
....*....|
gi 1263193398 217 QLDTPEGIIH 226
Cdd:COG1134 226 MDGDPEEVIA 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-213 |
1.09e-22 |
|
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: 93.93 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL----RWDIGYVLQQI 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFpHMTIAENIAVvpeMRQWSKKDIKARVDdllhMVGLDPDIyrDRMP--DE---------LSGGQKQRVGVVRALAAN 154
Cdd:cd03290 89 WLL-NATVEENITF---GSPFNKQRYKAVTD----ACSLQPDI--DLLPfgDQteigerginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALD-PLSREQLQKDIVQLQKKIQKTIVFVTHDMQeALSLGDRICIMKEG 213
Cdd:cd03290 159 TNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ-YLPHADWIIAMKDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
1.41e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 4 FNHVSKSYedGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGkdiqqyninelRWDIGYVL 82
Cdd:COG0488 1 LENLSKSF--GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 83 QQIALFPHMTIAENI--------AVVPEMRQWSKK------------------------DIKARVDDLLHMVGLdPDIYR 130
Cdd:COG0488 68 QEPPLDDDLTVLDTVldgdaelrALEAELEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSGLGF-PEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 131 DRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQkdivQLQKKIQKTIVFVTHD 196
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLE----EFLKNYPGTVLVVSHD 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
2.04e-21 |
|
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: 94.12 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE--TTEGSILIDGKDIQQYNINEL-RWD 77
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEM----RQWSKKDIKARVDDLLHMVGLDpDIYRDRMPDELSGGQKQRVGVVRALAA 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLD-ADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQkDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILL-DIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-221 |
3.34e-21 |
|
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: 89.39 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIAVVPEmrqWSKKDIKA--RVDDllhmVGLDpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIV 158
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE---YSDEEIYGalRVSE----GGLN-----------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLgDRICIMKEGKVVQLDTP 221
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNS--TILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-226 |
8.82e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYV----LQQiALFPHMTIAENI 97
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrKGE-GLVLDLSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 --AVVPEMRQW---SKKDIKARVDDLLHMVGLdpdiyrdRMPD------ELSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:COG1129 352 tlASLDRLSRGgllDRRRERALAEEYIKRLRI-------KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 167 LDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV-QLD----TPEGIIH 226
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVgELDreeaTEEAIMA 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-222 |
1.30e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.40 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 57 GSILIDGKDIQQYNINELRWDIGYVLQQIALFpHMTIAENIAVVPEmrQWSKKDIK-----ARVDDLLHMVGLDPDIYRD 131
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE--DATREDVKrackfAAIDEFIESLPNKYDTNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 132 RMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHdmqealslgdRIC-IM 210
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH----------RIAsIK 1423
|
170
....*....|..
gi 1263193398 211 KEGKVVQLDTPE 222
Cdd:PTZ00265 1424 RSDKIVVFNNPD 1435
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-216 |
1.61e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDI--------QQYNIn 72
Cdd:PRK15439 11 LLCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakaHQLGI- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 73 elrwdigY-VLQQIALFPHMTIAENIAVvpemRQWSKKDIKARVDDLLHMVG--LDPDIyrdrMPDELSGGQKQRVGVVR 149
Cdd:PRK15439 89 -------YlVPQEPLLFPNLSVKENILF----GLPKRQASMQKMKQLLAALGcqLDLDS----SAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-197 |
1.97e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.01 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVD---SLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILI-DGKDIQQYNINELRWD 77
Cdd:PTZ00265 383 IQFKNVRFHY-DTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHmTIAENIavvpEMRQWSKKDIKA-------------------------------------RVDDLLH 120
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNI----KYSLYSLKDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 121 M------------------------VGLDPDIYRDRM---PDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSRE 173
Cdd:PTZ00265 537 MrknyqtikdsevvdvskkvlihdfVSALPDKYETLVgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|....
gi 1263193398 174 QLQKDIVQLQKKIQKTIVFVTHDM 197
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAHRL 640
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-231 |
2.34e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTT----MKMINRLIETTEGSILIDGKDIQQyniNELRW-DIGYVLQ--QIALFPH 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAP---CALRGrKIATIMQnpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENiaVVPEMRQWSKKDIKARVDDLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:PRK10418 96 HTMHTH--ARETCLALGKPADDATLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 170 LSreqlQKDIVQLQKKIQKT----IVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNE 231
Cdd:PRK10418 174 VA----QARILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-221 |
3.91e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.67 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 5 NHVSKSYEDGtKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINEL---------R 75
Cdd:PRK11701 10 RGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 76 WDIGYVLQQIA--LFPHMTIAENI-----AVvpEMRQWSkkDIKARVDDLLHMVGLDPDiyR-DRMPDELSGGQKQRVGV 147
Cdd:PRK11701 89 TEWGFVHQHPRdgLRMQVSAGGNIgerlmAV--GARHYG--DIRATAGDWLERVEIDAA--RiDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQ-------LDT 220
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVEsgltdqvLDD 242
|
.
gi 1263193398 221 P 221
Cdd:PRK11701 243 P 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-202 |
5.01e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.55 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 9 KSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYninelrwdigyvlqqial 87
Cdd:COG2401 36 VELRVVERYVlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG------------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 88 fPHMTIAENIavvpemrqWSKKDIKARVDdLLHMVGL-DPDIYRdRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSA 166
Cdd:COG2401 98 -REASLIDAI--------GRKGDFKDAVE-LLNAVGLsDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1263193398 167 LDPLSREQLQKDIVQLQKKIQKTIVFVTH--DMQEALS 202
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-224 |
1.35e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.02 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 7 VSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQI 85
Cdd:PRK10982 4 ISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIAV---------VPEMRQWskKDIKARVDDLlhMVGLDPdiyRDRMPDeLSGGQKQRVGVVRALAANPK 156
Cdd:PRK10982 83 NLVLQRSVMDNMWLgryptkgmfVDQDKMY--RDTKAIFDEL--DIDIDP---RAKVAT-LSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGI 224
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-217 |
1.93e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.62 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHmTIAEN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 97 IAV-VPEMRQwskKDIK--ARV----DDLLHMvgldPDIY------RDRMpdeLSGGQKQRVGVVRALAANPKIVLMDEP 163
Cdd:PRK10789 409 IALgRPDATQ---QEIEhvARLasvhDDILRL----PQGYdtevgeRGVM---LSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 164 FSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQeALSLGDRICIMKEGKVVQ 217
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQ 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-237 |
2.22e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIET-----TEGSILIDGKDIQQYNINELRW----DIGYVLQQ--IA 86
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 87 LFPHMTIAENIAVVPEM-RQWSKKDIKARVDDLLHMVGLDPDIYRDR-MPDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTdYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 165 SALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-228 |
2.98e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.70 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKSYEDG-TKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIET---TEGSILIDGKDI---QQYNINELRWD- 77
Cdd:PRK09473 19 RVTFSTPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlPEKELNKLRAEq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQ--IALFPHMTIAENIAvvpEMRQWSKKDIKA-------RVDDLLHMvgldPDIyRDRM---PDELSGGQKQRV 145
Cdd:PRK09473 99 ISMIFQDpmTSLNPYMRVGEQLM---EVLMLHKGMSKAeafeesvRMLDAVKM----PEA-RKRMkmyPHEFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 146 GVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
...
gi 1263193398 226 HNP 228
Cdd:PRK09473 251 YQP 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
3.34e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIdGKDIQqyninelrwdIGY 80
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQ-QIALFPHMTIAEniavvpEMRQWSKKDIKARVDDLLHMVGLDPDiyRDRMP-DELSGGQKQRVGVVRALAANPKIV 158
Cdd:COG0488 383 FDQhQEELDPDKTVLD------ELRDGAPGGTEQEVRGYLGRFLFSGD--DAFKPvGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDPLSREQLqkdiVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLD 219
Cdd:COG0488 455 LLDEPTNHLDIETLEAL----EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-216 |
4.06e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 12 EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELR-WDIGYVL---QQIAL 87
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPedrLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 88 FPHMTIAENIAV----VPEMRQW---SKKDIKARVDDLLhmvgldpDIYRDRMPDE------LSGGQKQRVGVVRALAAN 154
Cdd:COG3845 348 VPDMSVAENLILgryrRPPFSRGgflDRKAIRAFAEELI-------EEFDVRTPGPdtparsLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-219 |
6.13e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIAVVPemrqwskkdikARVDDLLHMVGLDP--DIYRDRMPD-ELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANP-----------ALVEKWLERLKMAHklELEDGRISNlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDmQEALSLGDRICIMKEGKVVQLD 219
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSELT 531
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-214 |
8.02e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEdGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDG--------KDIQQYNIn 72
Cdd:PRK10762 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfngpKSSQEAGI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 73 elrwdiGYVLQQIALFPHMTIAENIAVVPEMR------QWSKkdIKARVDDLLHMVGLDPDiyRDRMPDELSGGQKQRVG 146
Cdd:PRK10762 82 ------GIIHQELNLIPQLTIAENIFLGREFVnrfgriDWKK--MYAEADKLLARLNLRFS--SDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 147 VVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGK 214
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-228 |
8.14e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.34 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIET----TEGSILIDGKDIQQYNINELR----WDIGYVLQ--QI 85
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRkiigREIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 ALFPHMTIAENIA-VVP---------EMRQWSKKDIKArvddLLHMVGL-DPDIYRDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:COG4170 101 CLDPSAKIGDQLIeAIPswtfkgkwwQRFKWRKKRAIE----LLHRVGIkDHKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNP 228
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-214 |
1.03e-18 |
|
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: 80.96 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGtKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqyninelrwDIGYV 81
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQqialfphmtiaeniavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdeLSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03221 69 EQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDPLSREQLQKDIvqlqKKIQKTIVFVTHDmQEALS-LGDRICIMKEGK 214
Cdd:cd03221 96 EPTNHLDLESIEALEEAL----KEYPGTVILVSHD-RYFLDqVATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-175 |
1.15e-18 |
|
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: 82.41 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWDIGYVLQQIALFPHMT 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENIAVVPEMRQWSKKDIkarvDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSR 172
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTI----EDALAAVGLTG--FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
...
gi 1263193398 173 EQL 175
Cdd:TIGR01189 164 ALL 166
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-237 |
1.51e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.47 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI----NRLIETTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHM 91
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 TI--AENIA--VVPEMRQWSKKDI--------KARVDDLLHMVGL-DP-DIYRDrMPDELSGGQKQRVGVVRALAANPKI 157
Cdd:PRK15093 101 CLdpSERVGrqLMQNIPGWTYKGRwwqrfgwrKRRAIELLHRVGIkDHkDAMRS-FPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 158 VLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIHNPKNEFVEEFI 237
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
1.70e-18 |
|
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: 81.05 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqyninelrwDIGYV 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQiALFPHMTIAENIAvvpemRQWSkkdikarvddllhmvgldpdiyrdrmpDELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03223 70 PQR-PYLPLGTLREQLI-----YPWD---------------------------DVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 1263193398 162 EPFSALDplsrEQLQKDIVQLQKKIQKTIVFVTH 195
Cdd:cd03223 117 EATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-195 |
2.14e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILI-DGKDI----QQyninelr 75
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpQR------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 76 wdiGYV----LQQIALFPHMTiaeniavvpemRQWSKKDIKArvddLLHMVGLDPDIYR----DRMPDELSGGQKQRVGV 147
Cdd:COG4178 435 ---PYLplgtLREALLYPATA-----------EAFSDAELRE----ALEAVGLGHLAERldeeADWDQVLSLGEQQRLAF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPLSREQLQKdivQLQKKIQK-TIVFVTH 195
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQ---LLREELPGtTVISVGH 542
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-168 |
2.76e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 24 EIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqynINELRWDIGYVLQQIALFPHMTIAENIAVvpem 103
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHRNAMKPALTVAENLEF---- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 104 rqWS--KKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:PRK13539 97 --WAafLGGEELDIAAALEAVGLAPLA--HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-235 |
4.38e-18 |
|
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: 81.69 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYEDGTKAVDSLHLEIKKGEF-----FVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyninelrwdiGYVLQQ 84
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IalfphmtiaeniavvpemrqwsKKDIKARVDDLLHmvGLDPDIYR------------------DRMPDELSGGQKQRVG 146
Cdd:cd03237 70 I----------------------KADYEGTVRDLLS--SITKDFYThpyfkteiakplqieqilDREVPELSGGELQRVA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 147 VVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIM--KEGKVVQLDTPEGI 224
Cdd:cd03237 126 IAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFegEPSVNGVANPPQSL 205
|
250
....*....|.
gi 1263193398 225 IHNpKNEFVEE 235
Cdd:cd03237 206 RSG-MNRFLKN 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-221 |
9.04e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 11 YEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGK--DIQQYNINELRWDIGYVLQ----Q 84
Cdd:PRK13638 11 YQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQdpeqQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IAlfpHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVglDPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:PRK13638 90 IF---YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 165 SALDPLSREQLqkdIVQLQKKIQK--TIVFVTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:PRK13638 165 AGLDPAGRTQM---IAIIRRIVAQgnHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-222 |
1.17e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQIALFPHMT------I 93
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDErARAGIFLAFQYPVEIPGVSvsnflrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 94 AENIAVVPEMrqwSKKDIKARVDDLLHMVGLDPDiYRDRMPDE-LSGGQKQRVGVVRALAANPKIVLMDEPFSALD---- 168
Cdd:COG0396 101 ALNARRGEEL---SAREFLKLLKEKMKELGLDED-FLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidal 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 169 -PLSREqlqkdIVQLQKKiQKTIVFVTH-----DMQEAlslgDRICIMKEGKVVQLDTPE 222
Cdd:COG0396 177 rIVAEG-----VNKLRSP-DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-236 |
2.14e-17 |
|
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: 82.54 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYeDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRL--IETTEGSIL------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 61 ---------IDGKDIQQYNINE-----LRWDIGYVLQQ-IALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLD 125
Cdd:TIGR03269 80 epcpvcggtLEPEEVDFWNLSDklrrrIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 126 PDIYRdrMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGD 205
Cdd:TIGR03269 160 HRITH--IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270
....*....|....*....|....*....|.
gi 1263193398 206 RICIMKEGKVVQLDTPEGIIhnpkNEFVEEF 236
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVV----AVFMEGV 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
5.13e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYN-----------INELRWDIGYVLQqia 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 87 lfphMTIAENIAVvPEMRQWSKKDIKAR-------VDDLLHMVGLD-PDiyRDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK10762 345 ----MSVKENMSL-TALRYFSRAGGSLKhadeqqaVSDFIRLFNIKtPS--MEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 159 LMDEPFSALDPLSReqlqKDIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:PRK10762 418 ILDEPTRGVDVGAK----KEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-225 |
8.54e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE--TTEGSILIDGKDIQQYNINELRwDIGYVL--QQIALFP 89
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCRFKDIRDSE-ALGIVIihQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIAVVPEMRQ-----WSKKDIKARvdDLLHMVGLDPDiyrdrmPDELSG----GQKQRVGVVRALAANPKIVLM 160
Cdd:NF040905 92 YLSIAENIFLGNERAKrgvidWNETNRRAR--ELLAKVGLDES------PDTLVTdigvGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 161 DEPFSALDPLSREQLQKDIVQLQKK-IqkTIVFVTHDMQEALSLGDRICIMKEGKVVQ-LDTPEGII 225
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQgI--TSIIISHKLNEIRRVADSITVLRDGRTIEtLDCRADEV 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-232 |
1.29e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIG 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHmTIAENIAVVPEMRQ---WSKKDiKARVDDLL--HMVGLDPDIYRDrmPDELSGGQKQRVGVVRALAAN 154
Cdd:PLN03232 1314 IIPQSPVLFSG-TVRFNIDPFSEHNDadlWEALE-RAHIKDVIdrNPFGLDAEVSEG--GENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLgDRICIMKEGKVVQLDTPEGIIHNPKNEF 232
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-216 |
2.46e-16 |
|
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: 76.15 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 12 EDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETT---EGSILIDGKDIQQyNINELRWDIGYVLQQIALF 88
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVPEMRQwskkdikarvddllhmvgldpdiyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:cd03233 96 PTLTVRETLDFALRCKG-------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1263193398 169 PLSREQLQKdIVQLQKKIQKTIVFVT--HDMQEALSLGDRICIMKEGKVV 216
Cdd:cd03233 151 SSTALEILK-CIRTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-216 |
5.86e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELrwdIGYV 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIAL---FPhmTIAENIAVVPE------MRQWSKKDiKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALA 152
Cdd:PRK15056 84 PQSEEVdwsFP--VLVEDVVMMGRyghmgwLRRAKKRD-RQIVTAALARVDMVE--FRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 153 ANPKIVLMDEPFSALDPlsreQLQKDIVQLQKKIQ---KTIVFVTHDMQEALSLGDrICIMKEGKVV 216
Cdd:PRK15056 159 QQGQVILLDEPFTGVDV----KTEARIISLLRELRdegKTMLVSTHNLGSVTEFCD-YTVMVKGTVL 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-216 |
6.58e-16 |
|
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: 74.87 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQYNINE-LRWDIGYVLQQIALFP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAeniavvpemrqwskkdikarvdDLLHMVGldpdiyrdrmpDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:cd03217 91 GVKNA----------------------DFLRYVN-----------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 170 LSREQLQKDIVQLQKKiQKTIVFVTHdMQEALSL--GDRICIMKEGKVV 216
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRIV 184
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-221 |
2.00e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.70 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKminrliettegsiLIDG-KDIQQYNINELRWDIG- 79
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS-------------LIAGaRKIQQGRVEVLGGDMAd 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 -----YVLQQIA---------LFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRV 145
Cdd:NF033858 68 arhrrAVCPRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 146 GVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFV-THDMQEALSLgDRICIMKEGKVVQLDTP 221
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-214 |
2.04e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 28 GEFFVLIGPSGCGKTTTMKMINRLIETT--EGSILIDGKDIQQYNINElrwdIGYVLQQIALFPHMTIAENIAVVPEMR- 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR----TGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 105 -QWSKKDIKARV-DDLLHMVGL---DPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDI 179
Cdd:PLN03211 170 pKSLTKQEKILVaESVISELGLtkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190
....*....|....*....|....*....|....*.
gi 1263193398 180 VQLQKKiQKTIVFVTHD-MQEALSLGDRICIMKEGK 214
Cdd:PLN03211 250 GSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-216 |
2.38e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 20 SLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIeTTEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHMTIAENIAV 99
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 100 -VPEMRQwsKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRAL-----AANP--KIVLMDEPFSALDPLS 171
Cdd:PRK03695 93 hQPDKTR--TEAVASALNEVAEALGLDDKL--GRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1263193398 172 REQLQKDIVQL-QKKIqkTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK03695 169 QAALDRLLSELcQQGI--AVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-218 |
3.49e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQ-QYNINELRWDIGYVLQ---QIALFPHM 91
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 92 TIAENIAVVPEMRQWSKKDIKARVDDllHMVGLDPDIYRDRMP----------DELSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:PRK09700 357 SIAQNMAISRSLKDGGYKGAMGLFHE--VDEQRTAENQRELLAlkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 162 EPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQL 218
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-241 |
4.57e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYedGTKAVDS-LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqynineLRwdIG 79
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLSdVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFPHM--TIAENIAVVPEMRqwsKKDIK---ARVDdLLHMVgldpdiyrDRMPDELSGGQKQRVGVVRALAAN 154
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRPGTK---KEDILpalKRVQ-AGHLI--------DAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 155 PKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQ-------EALSLGDRICIMkegkvvqlDTPEGIIHN 227
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHlvmaktdEVLCLNHHICCS--------GTPEVVSLH 210
|
250
....*....|....
gi 1263193398 228 PknEFVEEFiGNRG 241
Cdd:PRK09544 211 P--EFISMF-GPRG 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-216 |
6.63e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETtEGSILIDGKDIQQYNINELRWDIGYVLQQIALFPHMTIAENI 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 AV-VPemRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRAL-----AANP--KIVLMDEPFSALdp 169
Cdd:COG4138 91 ALhQP--AGASSEAVEQLLAQLAEALGLED--KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSL-- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 170 lsreqlqkDIVQ---LQKKIQK------TIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:COG4138 165 --------DVAQqaaLDRLLRElcqqgiTVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-232 |
9.54e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIAVVPEMRQ---WSKKDiKARVDDLL--HMVGLDPDIYRDrmPDELSGGQKQRVGVVRALAANP 155
Cdd:PLN03130 1318 IPQAPVLFSG-TVRFNLDPFNEHNDadlWESLE-RAHLKDVIrrNSLGLDAEVSEA--GENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMQEALSLgDRICIMKEGKVVQLDTPEGIIHNPKNEF 232
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSC--TMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-225 |
4.74e-14 |
|
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: 70.71 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIAvvPEM-----RQWSKKDIkARVDDLLHMV--GLDPDIYRDrmPDELSGGQKQRVGVVRALAA 153
Cdd:cd03288 100 ILQDPILFSG-SIRFNLD--PECkctddRLWEALEI-AQLKNMVKSLpgGLDAVVTEG--GENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 154 NPKIVLMDEPFSALDPLSREQLQKdiVQLQKKIQKTIVFVTHDMQEALSlGDRICIMKEGKVVQLDTPEGII 225
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQK--VVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-227 |
5.25e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYEDGTKAVDS---------LHLEIKKGEFFVLIGPSGCGKTTTMK-MINRLIETTEGSILIDGKdiqqyninelrwdIG 79
Cdd:PLN03130 616 SIKNGYFSWDSkaerptlsnINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 80 YVLQQIALFpHMTIAENI---AVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDeLSGGQKQRVGVVRALAANPK 156
Cdd:PLN03130 683 YVPQVSWIF-NATVRDNIlfgSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 157 IVLMDEPFSALDP-LSREQLQKDIV-QLQkkiQKTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEGIIHN 227
Cdd:PLN03130 761 VYIFDDPLSALDAhVGRQVFDKCIKdELR---GKTRVLVTNQLH-FLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-223 |
5.66e-14 |
|
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: 72.14 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSY--EDGTK--AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRwd 77
Cdd:COG4615 328 LELRGVTYRYpgEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 igyvlQQIA-------LFPHMtIAENIAVVPEmrqwskkdikaRVDDLLHMVGLD--PDIYRDRMPD-ELSGGQKQRVGV 147
Cdd:COG4615 406 -----QLFSavfsdfhLFDRL-LGLDGEADPA-----------RARELLERLELDhkVSVEDGRFSTtDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEG 223
Cdd:COG4615 469 LVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGPAA 543
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-175 |
6.99e-14 |
|
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: 69.06 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWDIGYVLQQIALFPHMT 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 IAENiavvpeMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSR 172
Cdd:cd03231 90 VLEN------LRFWHADHSDEQVEEALARVGLNG--FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
...
gi 1263193398 173 EQL 175
Cdd:cd03231 162 ARF 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-279 |
1.04e-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: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 18 VDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQiALFPHMTIAENI 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 ---AVVPEMRQWSKKDIKARVDDLLHMVGLDpdiyRDRMPDE---LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLS 171
Cdd:TIGR00957 720 lfgKALNEKYYQQVLEACALLPDLEILPSGD----RTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 172 REQLQKDIVQLQKKIQ-KTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEGIIHnpKNEFVEEFIGNRGRTWYEGKSV 250
Cdd:TIGR00957 796 GKHIFEHVIGPEGVLKnKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQ--RDGAFAEFLRTYAPDEQQGHLE 872
|
250 260 270
....*....|....*....|....*....|....
gi 1263193398 251 ADVLPLD-----ESVQLEgQALSLHASLQEALVR 279
Cdd:TIGR00957 873 DSWTALVsgegkEAKLIE-NGMLVTDVVGKQLQR 905
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-242 |
1.11e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMK-MINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQIALFpHMTIAENIAV 99
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQVSWIF-NATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 100 VPEM---RQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDeLSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQ 176
Cdd:PLN03232 702 GSDFeseRYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 177 KDIVQLQKKiQKTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEGIIHNpkNEFVEEFIGNRGR 242
Cdd:PLN03232 781 DSCMKDELK-GKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELSKS--GSLFKKLMENAGK 842
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-207 |
2.43e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYEDGTKAVDSLHL-----EIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQ 84
Cdd:PRK13409 342 EYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIAvvpemrqwskkDIKARVD------DLLHMVGLDPdIYrDRMPDELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK13409 409 IKPDYDGTVEDLLR-----------SITDDLGssyyksEIIKPLQLER-LL-DKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHD--MQEALSlgDRI 207
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDiyMIDYIS--DRL 524
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-220 |
3.36e-13 |
|
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: 68.34 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIeTTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIavvPEMRQWSKKDIKARVDDllhmVGLDPDIyrDRMPDEL-----------SGGQKQRVGVVR 149
Cdd:cd03289 82 IPQKVFIFSG-TFRKNL---DPYGKWSDEEIWKVAEE----VGLKSVI--EQFPGQLdfvlvdggcvlSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIqkTIVFVTHDMqEALSLGDRICIMKEGKVVQLDT 220
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRI-EAMLECQRFLVIEENKVRQYDS 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-220 |
4.16e-13 |
|
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: 69.94 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIeTTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIavvPEMRQWSKKDIKARVDDllhmVGLDPDIyrDRMPDEL-----------SGGQKQRVGVVR 149
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNL---DPYEQWSDEEIWKVAEE----VGLKSVI--EQFPDKLdfvlvdggyvlSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKdivQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDT 220
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRK---TLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-264 |
9.32e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYV 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIA-----LFPHMTIAENIAvvpEMRQWskkdikarvdDLLHMVGLdPDIYRDrMPD-----------ELSGGQKQRV 145
Cdd:PRK10790 421 QQDPVvladtFLANVTLGRDIS---EEQVW----------QALETVQL-AELARS-LPDglytplgeqgnNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 146 GVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKkiQKTIVFVTHDMQ---EAlslgDRICIMKEGKVVQLDTpe 222
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStivEA----DTILVLHRGQAVEQGT-- 557
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1263193398 223 giiHnpknefvEEFIGNRGRTW--YEGKSVADVLPLDESVQLEG 264
Cdd:PRK10790 558 ---H-------QQLLAAQGRYWqmYQLQLAGEELAASVREEESL 591
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-215 |
9.83e-13 |
|
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: 68.31 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETT-EGSILIDGKDIQQYN-INELRWDIGYV---LQQIALFPH 90
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVpedRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 MTIAENIAVvPEMRQWSKKdikARVDDLLHMVGLDPDIYRDRM----PD----ELSGGQKQRVGVVRALAANPKIVLMDE 162
Cdd:TIGR02633 354 LGVGKNITL-SVLKSFCFK---MRIDAAAELQIIGSAIQRLKVktasPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 163 PFSALDPLSREQLQKDIVQL-QKKIqkTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLaQEGV--AIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-216 |
2.41e-12 |
|
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: 64.57 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 25 IKKGEFFVLIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQyninELRWDIGYVLQQIALFPHMTIAENIAVVPE 102
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLagRKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLTVREALRFSAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 103 MRqwskkdikarvddllhmvgldpdiyrdrmpdELSGGQKQRVGVVRALAANPKIVLMDEPFSALDplSREQLQkdIVQL 182
Cdd:cd03232 106 LR-------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD--SQAAYN--IVRF 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1263193398 183 QKKIQ---KTIVFVTHDMQEAL-SLGDRICIMKE-GKVV 216
Cdd:cd03232 151 LKKLAdsgQAILCTIHQPSASIfEKFDRLLLLKRgGKTV 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-216 |
2.92e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 4 FNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIE----TTEGSILIDGkdIQQYNI-NELRWD 77
Cdd:TIGR00956 62 FRKLKKFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG--ITPEEIkKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 78 IGYVLQQIALFPHMTIAENIAVVPEMRQ-------WSKKDIKARVDDL-LHMVGLDpdIYRD-RMPDEL----SGGQKQR 144
Cdd:TIGR00956 140 VVYNAETDVHFPHLTVGETLDFAARCKTpqnrpdgVSREEYAKHIADVyMATYGLS--HTRNtKVGNDFvrgvSGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 145 VGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIvQLQKKIQKTIVFVT--HDMQEALSLGDRICIMKEGKVV 216
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-213 |
3.37e-12 |
|
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: 65.65 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQIALFPHmTI 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 94 AENIAVVPEMRQWSKKD-IKArvddllhmVGLDPDIyrDRMPDE-----------LSGGQKQRVGVVRALAANPKIVLMD 161
Cdd:cd03291 115 KENIIFGVSYDEYRYKSvVKA--------CQLEEDI--TKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 162 EPFSALDPLSREQL-QKDIVQLQKkiQKTIVFVTHDMqEALSLGDRICIMKEG 213
Cdd:cd03291 185 SPFGYLDVFTEKEIfESCVCKLMA--NKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-209 |
3.54e-12 |
|
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: 63.16 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 27 KGEFFVLIGPSGCGKTTTMKMI-NRLIETTEGSILIDGKDIQQYNINELRwdigyvlqqialfphmtiaeniavvpemrq 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 106 wskkdikarvddllhmvgldpDIYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIV----- 180
Cdd:smart00382 51 ---------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|....*....
gi 1263193398 181 QLQKKIQKTIVFVTHDMQEALSLGDRICI 209
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-195 |
3.88e-12 |
|
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: 66.70 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDiqqyninelrwDIGY 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQialfPHM---TIAENIaVVPE------MRQWSKKDIKARVD--DLLHMV--GLDPDIYRDRMpDELSGGQKQRVGV 147
Cdd:TIGR00954 520 VPQR----PYMtlgTLRDQI-IYPDssedmkRRGLSDKDLEQILDnvQLTHILerEGGWSAVQDWM-DVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1263193398 148 VRALAANPKIVLMDEPFSALDPlsreQLQKDIVQLQKKIQKTIVFVTH 195
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-225 |
4.67e-12 |
|
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: 66.89 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGY 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 81 VLQQIALFPHmTIAENIavvPEMRQWSKKDIKARVdDLLHMVGldpdiYRDRMPDE-----------LSGGQKQRVGVVR 149
Cdd:TIGR00957 1365 IPQDPVLFSG-SLRMNL---DPFSQYSDEEVWWAL-ELAHLKT-----FVSALPDKldhecaeggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 150 ALAANPKIVLMDEPFSALDpLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLgDRICIMKEGKVVQLDTPEGII 225
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
5.06e-12 |
|
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: 66.35 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLhlEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYV 81
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGG--EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQIALFPHMTIAENIavvpemrqwsKKDIKARVD------DLLHMVGLDPdIYrDRMPDELSGGQKQRVGVVRALAANP 155
Cdd:COG1245 407 PQYISPDYDGTVEEFL----------RSANTDDFGssyyktEIIKPLGLEK-LL-DKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1263193398 156 KIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHD--MQEALSlgDRI 207
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiyLIDYIS--DRL 526
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-216 |
7.24e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.34 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQiALFPHMTIAENIAVVPE 102
Cdd:PTZ00243 681 VSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQ-AWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 103 MRQwskkdikARVDDLLHMVGLDPDIYR--DRMPDE-------LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSRE 173
Cdd:PTZ00243 747 EDA-------ARLADAVRVSQLEADLAQlgGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1263193398 174 QLQKDIVqLQKKIQKTIVFVTHDMQeALSLGDRICIMKEGKVV 216
Cdd:PTZ00243 820 RVVEECF-LGALAGKTRVLATHQVH-VVPRADYVVALGDGRVE 860
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-195 |
7.74e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 19 DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNiNELRWDIGYVLQQIALFPHMTIAENIA 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 99 VVPEMRQWSKKDikaRVDDLLHMVGLDPdiyRDRMP-DELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQK 177
Cdd:PRK13538 97 FYQRLHGPGDDE---ALWEALAQVGLAG---FEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|
gi 1263193398 178 divQLQKKIQK--TIVFVTH 195
Cdd:PRK13538 171 ---LLAQHAEQggMVILTTH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-215 |
1.44e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI-----NRlietTEGSILIDGKDIQQYNINE-LRWDIGYVLQ---QIA 86
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKIRNPQQaIAQGIAMVPEdrkRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 87 LFPHMTIAENIAVvPEMRQWSKKdikARVDDLLHMVGLDPDIYRDRM----PD----ELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK13549 352 IVPVMGVGKNITL-AALDRFTGG---SRIDDAAELKTILESIQRLKVktasPElaiaRLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-213 |
1.51e-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: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 14 GTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrwdIGYVLQQIALFPHmTI 93
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 94 AENIAVVPEMRQWskkdikaRVDDLLHMVGLDPDIY----RDRMP-----DELSGGQKQRVGVVRALAANPKIVLMDEPF 164
Cdd:TIGR01271 504 KDNIIFGLSYDEY-------RYTSVIKACQLEEDIAlfpeKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 165 SALDPLSreqlQKDIVQ---LQKKIQKTIVFVTHDMqEALSLGDRICIMKEG 213
Cdd:TIGR01271 577 THLDVVT----EKEIFEsclCKLMSNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
3.11e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElRWDIGYVL-----QQIALFPHMTIAE 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 96 NIA--VVPEMRQWSK-KDIKARVDDLLHMVGL---DPDiyrdRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:PRK15439 361 NVCalTHNRRGFWIKpARENAVLERYRRALNIkfnHAE----QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1263193398 170 LSReqlqKDIVQLQKKIQK---TIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:PRK15439 437 SAR----NDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
5.03e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKminrliettegsiLIDGKDIQQYNiNELR------ 75
Cdd:PRK10938 261 IVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS-------------LITGDHPQGYS-NDLTlfgrrr 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 76 ------WDI----GYVLQQIalfpHMTIAENIAV-----------------VPEmRQWSKkdikarVDDLLHMVGLDpdi 128
Cdd:PRK10938 326 gsgetiWDIkkhiGYVSSSL----HLDYRVSTSVrnvilsgffdsigiyqaVSD-RQQKL------AQQWLDILGID--- 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1263193398 129 yrDRMPD----ELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEA 200
Cdd:PRK10938 392 --KRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
95-223 |
6.17e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 95 ENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIyrDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQ 174
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAA--GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 175 LQKDIVQLQKKiQKTIVFVTHDMQEA------LSLGDRICIMKEGKVVQLDTPEG 223
Cdd:NF000106 183 VWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKVG 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-225 |
6.23e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI-NRLIE-------TTEGSILIDGKDIQQYNINELRwDIGYVLQQ 84
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGggaprgaRVTGDVTLNGEPLAAIDAPRLA-RLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IA--LFPHMtiAENIAVV---PEMRQWSKKDIKAR--VDDLLHMVGLDPDIYRDRMpdELSGGQKQRVGVVRALA----- 152
Cdd:PRK13547 91 AAqpAFAFS--AREIVLLgryPHARRAGALTHRDGeiAWQALALAGATALVGRDVT--TLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 153 ----ANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGII 225
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-216 |
6.94e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 19 DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIettegsILIDGKDIQQYNINELRwdigyvLQQ-----IALFPHMTI 93
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEV------LLDDGRIIYEQDLIVAR------LQQdpprnVEGTVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 94 AENIAVVPE------------MRQWSKKDIK------------------ARVDDLLHMVGLDPDiyrdRMPDELSGGQKQ 143
Cdd:PRK11147 88 AEGIEEQAEylkryhdishlvETDPSEKNLNelaklqeqldhhnlwqleNRINEVLAQLGLDPD----AALSSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 144 RVGVVRALAANPKIVLMDEPFSALDPLSREQLQkdivQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLE----GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-169 |
7.16e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 21 LHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQqyNINELRWdIGYVLQQIALFPHMTIAENIAVV 100
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRF-MAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 101 PEMRQWSKKDIKArvdDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDP 169
Cdd:PRK13543 107 CGLHGRRAKQMPG---SALAIVGLAG--YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-216 |
7.70e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 7 VSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSIlidgkdiqqyninelRW----DIGYVL 82
Cdd:PRK15064 325 LTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------------KWsenaNIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 83 QQIAlfphMTIAENIAVVPEMRQWSK-KDikarvDDLL--HMVGldpdiyrdRM---PDE-------LSGGQKQRVGVVR 149
Cdd:PRK15064 389 QDHA----YDFENDLTLFDWMSQWRQeGD-----DEQAvrGTLG--------RLlfsQDDikksvkvLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 150 ALAANPKIVLMDEPFSALDPLSREQLQKDIvqlqKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-185 |
8.11e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 20 SLHLeiKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQyNINELRWDIGYVLQQIALFPHMTIAENIav 99
Cdd:PRK13540 21 SFHL--PAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYLTLRENC-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 100 vpeMRQWSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDI 179
Cdd:PRK13540 96 ---LYDIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
....*.
gi 1263193398 180 VQLQKK 185
Cdd:PRK13540 171 QEHRAK 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-216 |
1.22e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 23 LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIqqyNINELRWDI--GYVL-----QQIALFPHMTIAE 95
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 96 NIAvvpemrqwskkdIKARVDDLLHMVGLDP-------DIYRDRM------PDE----LSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK11288 351 NIN------------ISARRHHLRAGCLINNrweaenaDRFIRSLniktpsREQlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1263193398 159 LMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-242 |
1.33e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 4 FNHVSKSYEDGTKAV-DSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINELRWDIGYVL 82
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 83 QQIALFPHmTIAENiaVVPEMRQWSkkdikARVDDLLHMVGLdpdiyRDRMPDELSG--------------GQKQRVGVV 148
Cdd:PTZ00243 1391 QDPVLFDG-TVRQN--VDPFLEASS-----AEVWAALELVGL-----RERVASESEGidsrvleggsnysvGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 149 RA-LAANPKIVLMDEPFSALDPLSREQLQKDIvqLQKKIQKTIVFVTHDMQeALSLGDRICIMKEGKVVQLDTPEGIIHN 227
Cdd:PTZ00243 1458 RAlLKKGSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLH-TVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
250
....*....|....*..
gi 1263193398 228 PKNEFVE--EFIGNRGR 242
Cdd:PTZ00243 1535 RQSIFHSmvEALGRSEA 1551
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-215 |
3.47e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 24 EIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKDIQQYNINElRWDIGYVL-----QQIALFPHMTIAENiA 98
Cdd:PRK10982 270 DLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGFALvteerRSTGIYAYLDIGFN-S 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 99 VVPEMRQW-------SKKDIKARVDDLLhmvgldpDIYRDRMPDE------LSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:PRK10982 348 LISNIRNYknkvgllDNSRMKSDTQWVI-------DSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1263193398 166 ALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKV 215
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-209 |
6.63e-10 |
|
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: 57.20 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 11 YEDGTKAVDSLHL-----EIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDgkdiqqyninelRWDIGYVLQQI 85
Cdd:cd03222 3 YPDCVKRYGVFFLlvelgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 86 alfphmtiaeniavvpemrqwskkdikarvddllhmvgldpdiyrdrmpdELSGGQKQRVGVVRALAANPKIVLMDEPFS 165
Cdd:cd03222 71 --------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1263193398 166 ALDPLSREQLQKDIVQLQKKIQKTIVFVTHDMQEALSLGDRICI 209
Cdd:cd03222 101 YLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-213 |
9.38e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 25 IKKGEFFVLIGPSGCGKTTTMKMINRLIET---TEGSILIDGKDIQQyninELRWDIGYVLQQIALFPHMTIAENIAVVP 101
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLPTSTVRESLRFSA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 102 EMRQWSKKDIKAR---VDDLLHMVGLDPdiYRDRM---PDE-LSGGQKQRVGVVRALAANPK-IVLMDEPFSALDplsrE 173
Cdd:TIGR00956 862 YLRQPKSVSKSEKmeyVEEVIKLLEMES--YADAVvgvPGEgLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLD----S 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1263193398 174 QLQKDIVQLQKKIQK---TIVFVTHD-----MQEAlslgDRICIMKEG 213
Cdd:TIGR00956 936 QTAWSICKLMRKLADhgqAILCTIHQpsailFEEF----DRLLLLQKG 979
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-216 |
1.06e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 13 DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQYNiNELRWDIGYVL--QQIALF 88
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PHMTIAENIAVVPEMRQwsKKDIKARVDDL---------LHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAANPKIVL 159
Cdd:CHL00131 97 PGVSNADFLRLAYNSKR--KFQGLPELDPLefleiinekLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHdMQEALS--LGDRICIMKEGKVV 216
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH-YQRLLDyiKPDYVHVMQNGKII 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
3.01e-09 |
|
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: 57.64 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 5 NHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLieTTEgsilIDGKDIQQYNINelrwdIGYVLQQ 84
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--DKD----FNGEARPQPGIK-----VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 85 IALFPHMTIAENIavvpEMRQWSKKDIKARVDDLlHMVGLDPDIYRD--------------------------------R 132
Cdd:TIGR03719 77 PQLDPTKTVRENV----EEGVAEIKDALDRFNEI-SAKYAEPDADFDklaaeqaelqeiidaadawdldsqleiamdalR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 133 MPD------ELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQkdivQLQKKIQKTIVFVTHD 196
Cdd:TIGR03719 152 CPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE----RHLQEYPGTVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-168 |
1.48e-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: 55.71 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIdGKDIQqyninelrwdIGYV 81
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQ-IALFPHMTIAENIAVVPEMRQWSKKDIKARV---------DDLLHMVGldpdiyrdrmpdELSGGQKQRVGVVRAL 151
Cdd:TIGR03719 391 DQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG------------QLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 1263193398 152 AANPKIVLMDEPFSALD 168
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
107-239 |
2.20e-08 |
|
The ATP-binding cassette domain 1 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, RLIs 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: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 107 SKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKi 186
Cdd:cd03236 112 KKKDERGKLDELVDQLELRH--VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED- 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 187 QKTIVFVTHDMQEALSLGDRICIMkegkvvqLDTPE--GIIHNPK------NEFVEEFIGN 239
Cdd:cd03236 189 DNYVLVVEHDLAVLDYLSDYIHCL-------YGEPGayGVVTLPKsvregiNEFLDGYLPT 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-236 |
2.57e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 17 AVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGkdiqqyninelrwDIGYVLQQIALFPHMTIAEN 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 97 IAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDrmPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPlSREQLQ 176
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ-TFAQKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 177 KDIVQLQKKIQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPEGIIhnPKNE-FVEEF 236
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYEaFLNDF 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-223 |
3.67e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 33 LIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQYNINELRwdiGYVLQQIALFPHMTIAENIAVVPEMR---QWS 107
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQETFARIS---GYCEQNDIHSPQVTVRESLIYSAFLRlpkEVS 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 108 KKDIKARVDDLLHMVGLDPdiYRDR---MP--DELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKdIVQL 182
Cdd:PLN03140 988 KEEKMMFVDEVMELVELDN--LKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR-TVRN 1064
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1263193398 183 QKKIQKTIVFVTH----DMQEALslgDRICIMKEGKVVQLDTPEG 223
Cdd:PLN03140 1065 TVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGPLG 1106
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-215 |
6.15e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKD----IQQYNINELRW 76
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 77 DIGYVLQQIALFPHmtiaeniavVPEMRqwskkdIKARVDDLlhmvGLDPDIYRDRMPdELSGGQKQRVGVVRALAANPK 156
Cdd:PLN03073 588 SSNPLLYMMRCFPG---------VPEQK------LRAHLGSF----GVTGNLALQPMY-TLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 157 IVLMDEPFSALDPLSREQLQKDIVQLQKKiqktIVFVTHDmqEALSLG--DRICIMKEGKV 215
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQGG----VLMVSHD--EHLISGsvDELWVVSEGKV 702
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-180 |
7.55e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 35 GPSGCGKTTTMKMINRLIETTEGSILIdgKDIQQYNINELRwdIGYVLQQIALFPHMTIAENIAVVPEMRQwSKKDIKA- 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLKFWSEIYN-SAETLYAa 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1263193398 114 ----RVDDLlhmvgLDPDIYRdrmpdeLSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIV 180
Cdd:PRK13541 108 ihyfKLHDL-----LDEKCYS------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-168 |
1.02e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 33 LIGPSGCGKTTTMKMINRLIETTEGSILID-----GKDIQ-QYNINELR------------WDIGYVLQQIALFPHMT-- 92
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQdQFAFEEFTvldtvimghtelWEVKQERDRIYALPEMSee 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 93 ----IAENIAVVPEMRQWSKKdikARVDDLLHMVGLDPDIYRDRMpDELSGGQKQRVGVVRALAANPKIVLMDEPFSALD 168
Cdd:PRK15064 112 dgmkVADLEVKFAEMDGYTAE---ARAGELLLGVGIPEEQHYGLM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-198 |
3.17e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 10 SYE-DGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIDGKdiqqyninelrWDIGYVLQ-QIAL 87
Cdd:PRK11147 326 NYQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----------LEVAYFDQhRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 88 FPHMTIAENIAVvpemrqwSKKDI----KARvddllHMVGLDPDIY----RDRMP-DELSGGQKQRVGVVRALAANPKIV 158
Cdd:PRK11147 395 DPEKTVMDNLAE-------GKQEVmvngRPR-----HVLGYLQDFLfhpkRAMTPvKALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1263193398 159 LMDEPFSALDPLSREQLQkdivQLQKKIQKTIVFVTHDMQ 198
Cdd:PRK11147 463 ILDEPTNDLDVETLELLE----ELLDSYQGTVLLVSHDRQ 498
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-197 |
5.37e-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: 47.86 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 26 KKGEFFVLIGPSGCGKTTTMKMI------NRLIETTEGSI--LID---GKDIQQY--NI--NELRwdIGYVLQQIALFPH 90
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsgelkpNLGDYDEEPSWdeVLKrfrGTELQDYfkKLanGEIK--VAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 91 M---TIAENIavvpemrqwSKKDIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSAL 167
Cdd:COG1245 175 VfkgTVRELL---------EKVDERGKLDELAEKLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 1263193398 168 DPLSREQLQKDIVQLQKKiQKTIVFVTHDM 197
Cdd:COG1245 244 DIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-197 |
1.21e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 25 IKKGEFFVLIGPSGCGKTTTMKMI------NRLIETTEGSI--LID---GKDIQQY-----NiNELRwdIGYVLQQIALF 88
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipNLGDYEEEPSWdeVLKrfrGTELQNYfkklyN-GEIK--VVHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 89 PhmtiaenIAVVPEMRQWSKK-DIKARVDDLLHMVGLDPdiYRDRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSAL 167
Cdd:PRK13409 173 P-------KVFKGKVRELLKKvDERGKLDEVVERLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 1263193398 168 DPLSREQLQKDIVQLQKKiqKTIVFVTHDM 197
Cdd:PRK13409 244 DIRQRLNVARLIRELAEG--KYVLVVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-168 |
1.79e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTkAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILIdGKDIQqyninelrwdIGYV 81
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 82 LQQ-IALFPHMTIAENIAVVPEMRQWSKKDIKARVddllhmvgldpdiYRDRM----PD------ELSGGQKQRVGVVRA 150
Cdd:PRK11819 393 DQSrDALDPNKTVWEEISGGLDIIKVGNREIPSRA-------------YVGRFnfkgGDqqkkvgVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 1263193398 151 LAANPKIVLMDEPFSALD 168
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-196 |
2.99e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQF----NHVSKSYEDGTKAVDSLHLEikkgeFF------VLiGPSGCGKTTTMKminrliettegsIL--IDgKDIQq 68
Cdd:PRK11819 2 MAQYiytmNRVSKVVPPKKQILKDISLS-----FFpgakigVL-GLNGAGKSTLLR------------IMagVD-KEFE- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 69 yniNELRWD----IGYVLQQIALFPHMTIAENIavvpEMRQWSKKDIKARVDDLLHMVGlDPDIYRDRMPDE-------- 136
Cdd:PRK11819 62 ---GEARPApgikVGYLPQEPQLDPEKTVRENV----EEGVAEVKAALDRFNEIYAAYA-EPDADFDALAAEqgelqeii 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 137 ------------------------------LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQkdivQLQKKI 186
Cdd:PRK11819 134 daadawdldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE----QFLHDY 209
|
250
....*....|
gi 1263193398 187 QKTIVFVTHD 196
Cdd:PRK11819 210 PGTVVAVTHD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
58-229 |
3.86e-05 |
|
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: 45.39 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 58 SILIDGKDIQQYnineLRWDIGYV---LQQIALFP-HMTIAENIAvvpemrqwskKDIKARVDDLLHmVGLDPdIYRDRM 133
Cdd:TIGR00630 422 AVTVGGKSIADV----SELSIREAhefFNQLTLTPeEKKIAEEVL----------KEIRERLGFLID-VGLDY-LSLSRA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 134 PDELSGGQKQRVGVVRALAANPKIVL--MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDmQEALSLGDRICIMK 211
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHD-EDTIRAADYVIDIG 563
|
170 180
....*....|....*....|....
gi 1263193398 212 E------GKVVQLDTPEGIIHNPK 229
Cdd:TIGR00630 564 PgagehgGEVVASGTPEEILANPD 587
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-168 |
5.67e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 1 MIQFNHVSKSYEDgTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMI--NRLIETTEGSILIDGKDIQQYNINElRWDI 78
Cdd:PRK09580 1 MLSIKDLHVSVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED-RAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 79 G------YVLQQIALFPHMTIAENIAVVPEMRQWS---KKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVR 149
Cdd:PRK09580 79 GifmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEpldRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQ 158
|
170
....*....|....*....
gi 1263193398 150 ALAANPKIVLMDEPFSALD 168
Cdd:PRK09580 159 MAVLEPELCILDESDSGLD 177
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-254 |
6.75e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 25 IKKGEFFVLIGPSGCGKTTTMKMINRLIETT---EGSILIDGkdiqqYNINEL--RWDIGYVLQQIALFPHMTIAENI-- 97
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG-----YRLNEFvpRKTSAYISQNDVHVGVMTVKETLdf 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 98 ------------------------AVVPE------MRQWSKKDIKARV--DDLLHMVGLD---PDIYRDRMPDELSGGQK 142
Cdd:PLN03140 263 sarcqgvgtrydllselarrekdaGIFPEaevdlfMKATAMEGVKSSLitDYTLKILGLDickDTIVGDEMIRGISGGQK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 143 QRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKIQKTIVF-VTHDMQEALSLGDRICIMKEGKVVQLDTP 221
Cdd:PLN03140 343 KRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLSEGQIVYQGPR 422
|
250 260 270
....*....|....*....|....*....|...
gi 1263193398 222 EGIIhnpknEFVEEFignrGRTWYEGKSVADVL 254
Cdd:PLN03140 423 DHIL-----EFFESC----GFKCPERKGTADFL 446
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-216 |
7.37e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 16 KAVDSLHLEIKKGEFFVLIGPSGCGKT-TTMKMINRLIET-TEGSILIDGKDIQQYNINE-LRWDIGYVLQ---QIALFP 89
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDaIDAGLAYVTEdrkGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 90 HMTIAENIaVVPEMRQWSKKDIkarVDDllHMVGLDPDIYRDRM----PD------ELSGGQKQRVGVVRALAANPKIVL 159
Cdd:NF040905 354 IDDIKRNI-TLANLGKVSRRGV---IDE--NEEIKVAEEYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 160 MDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVV 216
Cdd:NF040905 428 LDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-236 |
1.01e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 2 IQFNHVSKSYEDGTKAVDSLH-------------------LEIKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILID 62
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKdlffrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 63 GKdiqqyninelrwdIGYVLQQIALFPHMTIAENIAVVPEMRQWSKKDIKARVDDLLHMVGLDPDIYRDrmPDELSGGQK 142
Cdd:PRK13545 85 GS-------------AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQP--VKTYSSGMK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 143 QRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFVTHDMQEALSLGDRICIMKEGKVVQLDTPE 222
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
250
....*....|....
gi 1263193398 223 GIIHNpKNEFVEEF 236
Cdd:PRK13545 229 EVVDH-YDEFLKKY 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-193 |
1.23e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1263193398 137 LSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKiQKTIVFV 193
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
106-207 |
1.23e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 106 WSKKDIKARVDDLLHmVGLDpDIYRDRMPDELSGGQKQRVGVVRALAANPKIVL--MDEPFSALDPLSREQLQKDIVQLq 183
Cdd:cd03270 109 FARVGIRERLGFLVD-VGLG-YLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL- 185
|
90 100
....*....|....*....|....
gi 1263193398 184 KKIQKTIVFVTHDmQEALSLGDRI 207
Cdd:cd03270 186 RDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
137-207 |
1.88e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1263193398 137 LSGGQKQRVGVVRALAANPK--IVLMDEPFSALDPlsrEQLQKDIVQLQKKIQK--TIVFVTHDMqEALSLGDRI 207
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ---QDINQLLEVIKGLIDLgnTVILIEHNL-DVLSSADWI 158
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
132-196 |
2.33e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 2.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1263193398 132 RMPDELSGGQKQ------RVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVQLQKKI-QKTIVFVTHD 196
Cdd:cd03240 111 DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQkNFQLIVITHD 182
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
6-130 |
4.03e-04 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 41.87 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 6 HVSKsYEDGTKAVDSLHLEIKKGEFFVLIGPSGCGKTTTMKMINR-----LIETTEGSILIDGKDiqQYNINELRWD-IG 79
Cdd:TIGR00602 89 HKKK-IEEVETWLKAQVLENAPKRILLITGPSGCGKSTTIKILSKelgiqVQEWSNPTLPDFQKN--DHKVTLSLEScFS 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1263193398 80 YVLQQIALFPHMTI--AENIAVVPEMRQWSKKDIkaRVDDLLHMVGLDPDIYR 130
Cdd:TIGR00602 166 NFQSQIEVFSEFLLraTNKLQMLGDDLMTDKKII--LVEDLPNQFYRDTRALH 216
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
102-196 |
1.06e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 102 EMRQWSKKDIKARVDDLLHMVGLDPDIYRDRMPDELSGGQKQRVGVVRALAANPK---IVLMDEPFSALDPlsreQLQKD 178
Cdd:pfam13304 202 LGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHP----KLLRR 277
|
90 100
....*....|....*....|...
gi 1263193398 179 IVQL-----QKKIQktIVFVTHD 196
Cdd:pfam13304 278 LLELlkelsRNGAQ--LILTTHS 298
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
25-61 |
2.45e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.92 E-value: 2.45e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1263193398 25 IKKGEFFVLIGPSGCGKTTTMKMINRLIETTEGSILI 61
Cdd:cd17933 9 VLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVL 45
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
112-195 |
9.34e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.53 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1263193398 112 KARVDDLLHMVGLDPDIYRdRMPDELSGGQKQRVGVVRALAANPKIVLMDEPFSALDPLSREQLQKDIVqlqkKIQKTIV 191
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFI 395
|
....
gi 1263193398 192 FVTH 195
Cdd:PLN03073 396 VVSH 399
|
|
| |
