|
Name |
Accession |
Description |
Interval |
E-value |
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-352 |
0e+00 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 648.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLELDFTQTLGSHCLQIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGY 80
Cdd:PRK11144 1 MLELNFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 81 VFQDARLFPHYKVRGNLQYGMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 161 IPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVMHPWLPAEQQSTILSATVA 240
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 241 AQHPQYAMTALALGDQLLWVNRLERPAGDTARIRIQASDVSLTLAQPSGTSIRNILRAEVVQYLEVNGQIEVQLRVSGRL 320
Cdd:PRK11144 241 EHHPHYAMTALALGDQHLWVNKLDAPLGTALRIRIQASDVSLVLQPPQQSSIRNILRAKVVEIYDDNGQVEVKLEVGGKT 320
|
330 340 350
....*....|....*....|....*....|..
gi 488984369 321 LWARISPWARDDLAIAPGQQVFAQIKSVSIAA 352
Cdd:PRK11144 321 LWARITPWARDELALKPGQWLYAQIKSVSITQ 352
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-352 |
9.86e-179 |
|
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: 499.24 E-value: 9.86e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLELDFTQTLGSHCLQIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGY 80
Cdd:COG4148 2 MLEVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 81 VFQDARLFPHYKVRGNLQYGM----AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepl 156
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRkrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRAllssprlllmdepl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 157 ASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVMHPWLPAEQQSTILS 236
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 237 ATVAAQHPQYAMTALALGDQLLWVNRLERPAGDTARIRIQASDVSLTLAQPSGTSIRNILRAEVVQ-YLEVNGQIEVQLR 315
Cdd:COG4148 242 ATVAAHDPDYGLTRLALGGGRLWVPRLDLPPGTRVRVRIRARDVSLALEPPEGSSILNILPGRVVEiEPADGGQVLVRLD 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 488984369 316 VSGRLLWARISPWARDDLAIAPGQQVFAQIKSVSIAA 352
Cdd:COG4148 322 LGGQTLLARITRRSADELGLAPGQTVYAQIKSVALLR 358
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-351 |
7.78e-170 |
|
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: 476.91 E-value: 7.78e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 2 LELDFTQTLGSHCLQIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYV 81
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 82 FQDARLFPHYKVRGNLQYGMAKSMVSQ----FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLA 157
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARPSErrisFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 158 SLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVMhPWLPAEQQSTILSA 237
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL-PWLAREDQGSLIEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 238 TVAAQHPQYAMTALALGDQLLWVNRLERPAGDTARIRIQASDVSLTLAQPSGTSIRNILRAEVVQYLEVN-GQIEVQLRV 316
Cdd:TIGR02142 240 VVAEHDQHYGLTALRLGGGHLWVPENLGPTGARLRLRVPARDVSLALQKPEATSIRNILPARVVEIEDSDiGRVGVVLES 319
|
330 340 350
....*....|....*....|....*....|....*
gi 488984369 317 SGRLLWARISPWARDDLAIAPGQQVFAQIKSVSIA 351
Cdd:TIGR02142 320 GGKTLWARITRWARDELGIAPGTPVFAQIKAVALR 354
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-211 |
2.82e-71 |
|
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: 221.01 E-value: 2.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLELDFTQTLGSHCLQIRETLPaSGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGY 80
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 81 VFQDARLFPHYKVRGNLQYGMAK----SMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRkrnrEDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 157 ASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-350 |
3.78e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.40 E-value: 3.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdtaqrICLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:COG1118 24 EIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRERRVGFVFQHYALFPHMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVS------QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLAS-------------LD 160
Cdd:COG1118 99 GLRVRPPSkaeiraRVEELLELVQLEGLADRYPSQLSGGQRQRVALARA-------------LAVepevllldepfgaLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 161 IPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSsvmhpwlPAEQQSTILSATVA 240
Cdd:COG1118 166 AKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR-------PATPFVARFLGCVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 241 AQHPQYAMTALALGDQLLWVNrlERPAGDTARIRIQASDVSLtLAQPSGtsiRNILRAEVVQYLEVNGQIEVQLRV---S 317
Cdd:COG1118 239 VLRGRVIGGQLEADGLTLPVA--EPLPDGPAVAGVRPHDIEV-SREPEG---ENTFPATVARVSELGPEVRVELKLedgE 312
|
330 340 350
....*....|....*....|....*....|...
gi 488984369 318 GRLLWARISPWARDDLAIAPGQQVFAQIKSVSI 350
Cdd:COG1118 313 GQPLEAEVTKEAWAELGLAPGDPVYLRPRPARV 345
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-211 |
2.25e-48 |
|
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: 161.92 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPERRNIGMVFQDYALFPHLTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVS------QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:cd03259 96 GLKLRGVPkaeiraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKE 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03259 176 LQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
26-346 |
1.52e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.72 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYG----- 100
Cdd:COG3842 33 FVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPPEKRNVGMVFQDYALFPHLTVAENVAFGlrmrg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA-------------SLDIPRKRE 166
Cdd:COG3842 107 VPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA-------------LApeprvllldeplsALDAKLREE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 167 LLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSsvmhpwlPAEQ-------QSTILSATV 239
Cdd:COG3842 174 MREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER-------PATRfvadfigEANLLPGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 240 AAQHPQYAMTAlalGDQLLWVNRLERPAGDTARIRIQASDVSLTLAQPsgtsiRNILRAEVVQYLEVNGQIEVQLRV-SG 318
Cdd:COG3842 247 LGDEGGGVRTG---GRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGP-----ENGLPGTVEDVVFLGSHVRYRVRLgDG 318
|
330 340
....*....|....*....|....*...
gi 488984369 319 RLLWARISPwaRDDLAIAPGQQVFAQIK 346
Cdd:COG3842 319 QELVVRVPN--RAALPLEPGDRVGLSWD 344
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-219 |
1.14e-44 |
|
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: 153.26 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMAKSMVS 107
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN------LPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 --QFDKLVD----LLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIP 181
Cdd:cd03299 103 kkEIERKVLeiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVT 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:cd03299 183 VLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
27-345 |
2.17e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.30 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYG--MAKS 104
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD------LPPKDRNIAMVFQSYALYPHMTVYENIAFPlkLRKV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 MVSQFDKLV----DLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplasldIPRKRELL----P------- 169
Cdd:COG3839 106 PKAEIDRRVreaaELLGLEDLLDRKPKQLSGGQRQRVALGRA------------------LVREPKVFlldePlsnldak 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 170 -------YLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSsvmhpwlPA---------EQQST 233
Cdd:COG3839 168 lrvemraEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR-------PAnlfvagfigSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 234 ILSATVAAQHpqyamtaLALGDQLLWVN-RLERPAGDTARIRIQASDVslTLAQPSGTSIRniLRAEVVQYLevNGQIEV 312
Cdd:COG3839 241 LLPGTVEGGG-------VRLGGVRLPLPaALAAAAGGEVTLGIRPEHL--RLADEGDGGLE--ATVEVVEPL--GSETLV 307
|
330 340 350
....*....|....*....|....*....|...
gi 488984369 313 QLRVSGRLLWARISPwardDLAIAPGQQVFAQI 345
Cdd:COG3839 308 HVRLGGQELVARVPG----DTRLRPGDTVRLAF 336
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-215 |
5.38e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.05 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLELD-FTQTLGSHCLQIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAqriclaPEQRRIG 79
Cdd:COG3840 1 MLRLDdLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 80 YVFQDARLFPHYKVRGNLQYGMAKSM---VSQFDKLVDLL---GIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLkltAEQRAQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 154 EPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEE 215
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-206 |
5.71e-37 |
|
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: 131.16 E-value: 5.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03229 22 NIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL--PPLRRRIGMVFQDFALFPHLTVLENIAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GmaksmvsqfdklvdllgiaplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:cd03229 100 G----------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLG 151
|
170 180
....*....|....*....|....*..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGK 206
Cdd:cd03229 152 ITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-219 |
1.55e-35 |
|
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: 129.38 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDV---PVQERNVGFVFQHYALFRHMTVFDNVAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 M----------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03296 99 LrvkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:cd03296 179 LRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-216 |
1.35e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.72 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQ- 98
Cdd:COG1131 22 TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-----RRRIGYVPQEPALYPDLTVRENLRf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 ----YGMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:COG1131 97 farlYGLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984369 174 LAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1131 177 LAAEGKT-VLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
30-211 |
2.14e-34 |
|
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: 125.44 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 30 FGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYG--MAKSMVS 107
Cdd:cd03301 32 LGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD------LPPKDRDIAMVFQNYALYPHMTVYDNIAFGlkLRKVPKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 QFDKLV----DLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPML 183
Cdd:cd03301 106 EIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTI 185
|
170 180
....*....|....*....|....*...
gi 488984369 184 YVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03301 186 YVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-218 |
1.79e-33 |
|
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: 123.85 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTaQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL-SGKELRKARRRIGMIFQHFNLLSSRTVFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -----GMAKSMV-SQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:cd03258 106 pleiaGVPKAEIeERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:cd03258 186 INRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-209 |
1.03e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.51 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAqriclapeqRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:COG1116 33 TVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---------PDRGVVFQEPALLPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVS------QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA-------------SLD 160
Cdd:COG1116 104 GLELRGVPkaerreRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA-------------LAndpevllmdepfgALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984369 161 IPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEA--GKVKA 209
Cdd:COG1116 171 ALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-211 |
1.89e-32 |
|
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: 120.29 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvLNDTAqricLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTA----APPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSM----VSQ--FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:cd03298 94 GLSPGLkltaEDRqaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-216 |
3.02e-32 |
|
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: 120.52 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLND-TAQRIClapeqRRIGYVFQDAR--LFpHYKVR-- 94
Cdd:COG1122 23 SIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELR-----RKVGLVFQNPDdqLF-APTVEed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 ---GNLQYGMAKS-MVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIgralltapelllldeplAS------------ 158
Cdd:COG1122 97 vafGPENLGLPREeIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI-----------------AGvlamepevlvld 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984369 159 -----LDIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1122 160 eptagLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-216 |
5.06e-32 |
|
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: 120.35 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-----RRQIGVLPDERGLYDRLTVRENIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -GMAKSMVSQ-----FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:COG4555 98 fAELYGLFDEelkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984369 174 LAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG4555 178 LKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-142 |
2.06e-31 |
|
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: 115.82 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD----DERKSLRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 100 G------MAKSMVSQFDKLVDLLGIAPLLDRLPGR----LSGGEKQRVAIGRA 142
Cdd:pfam00005 83 GlllkglSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARA 135
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
26-209 |
5.04e-30 |
|
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: 114.11 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTaqriclapeQRRIGYVFQDARLFPHYKVRGNLQYGM---- 101
Cdd:cd03293 32 FVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP---------GPDRGYVFQQDALLPWLTVLDNVALGLelqg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 --AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:cd03293 103 vpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETG 182
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEA--GKVKA 209
Cdd:cd03293 183 KTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-207 |
1.12e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQ--RRIGYVFQDARLFPHyKVRGNL 97
Cdd:COG4619 22 TLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA------MPPPEwrRQVAYVPQEPALWGG-TVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGM-AKSMVSQFDKLVDLL---GIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:COG4619 95 PFPFqLRERKFDRERALELLerlGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLR 174
|
170 180 190
....*....|....*....|....*....|....*
gi 488984369 173 RLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:COG4619 175 EYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-207 |
1.40e-29 |
|
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: 113.01 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclAPEQRRIGYVFQDARLFPHYKVRGNLQY------ 99
Cdd:cd03262 28 VVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI--NELRQKVGMVFQQFNLFPHLTVLENITLapikvk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQF-DKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEi 178
Cdd:cd03262 106 GMSKAEAEERaLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE- 184
|
170 180
....*....|....*....|....*....
gi 488984369 179 HIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03262 185 GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-216 |
2.01e-29 |
|
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: 113.36 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclaPEQRRIGYVFQDAR--LFPHYKVRGNL 97
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----AFRRRVQMVFQDPYasLHPRHTVDRIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 -----QYGMAKSMvSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:COG1124 103 aeplrIHGLPDRE-ERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 172 QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1124 182 KDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-209 |
2.09e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.83 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQR------RIGYVFQDARLFPHYKV 93
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS------LSERELarlrrrHIGFVFQFFNLLPELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNLQYGM------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplASLDIPRKREL 167
Cdd:COG1136 104 LENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAlvnrpkliladeptGNLDSKTGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 168 LPYLQRLAQEIHIPMLYVSHSLdEIQHLADRVLVLEAGKVKA 209
Cdd:COG1136 184 LELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-211 |
2.53e-29 |
|
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: 112.26 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtaQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ------SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSM---VSQFDKLVDL---LGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:TIGR01277 94 GLHPGLklnAEQQEKVVDAaqqVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-217 |
4.61e-29 |
|
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: 111.95 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMA-------- 102
Cdd:cd03300 33 GPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------LPPHKRPVNTVFQNYALFPHLTVFENIAFGLRlkklpkae 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 -KSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIP 181
Cdd:cd03300 107 iKERVAEALDLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGIT 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:cd03300 184 FVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-219 |
8.42e-29 |
|
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: 116.54 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLAPEQRRIGYVFQD--ARLFPHYKVRGNL 97
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS-LRELRRRVQMVFQDpySSLNPRMTVGDII 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGM----------AKSMVsqfDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA--------- 157
Cdd:COG1123 366 AEPLrlhgllsraeRRERV---AELLERVGLPPdLADRYPHELSGGQRQRVAIARA-------------LAlepkllild 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 158 ----SLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:COG1123 430 eptsALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-221 |
1.89e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.44 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAqriclaPEQRRIGYVFQDARLFPHYKVRGNLQYGMA---KS 104
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------PSRRPVSMLFQENNLFSHLTVAQNIGLGLNpglKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 MVSQFDKLVDL---LGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIP 181
Cdd:PRK10771 103 NAAQREKLHAIarqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSV 221
Cdd:PRK10771 183 LLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-206 |
2.30e-28 |
|
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: 109.48 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLapeqRRIGYVFQDARL-FPHYKVRGNLQ 98
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDDqFFGPTVEEEVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMAKSMVSQFD------KLVDLLGIAPLLDRLPGRLSGGEKQRVAIgralltapelllldeplAS-------------- 158
Cdd:cd03225 99 FGLENLGLPEEEieerveEALELVGLEGLRDRSPFTLSGGQKQRVAI-----------------AGvlamdpdillldep 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984369 159 ---LDIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGK 206
Cdd:cd03225 162 tagLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
26-207 |
5.61e-28 |
|
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: 108.73 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLAPEQRR-IGYVFQDARLFPHYKVRGNLQYGM--- 101
Cdd:cd03255 32 FVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAFRRRhIGFVFQSFNLLPDLTALENVELPLlla 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 ---AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEI 178
Cdd:cd03255 111 gvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEA 190
|
170 180
....*....|....*....|....*....
gi 488984369 179 HIPMLYVSHSlDEIQHLADRVLVLEAGKV 207
Cdd:cd03255 191 GTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
26-216 |
3.65e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 107.00 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclaPEQRR-IGYVFQDARLFPHYKVRGNLQYG---- 100
Cdd:COG1126 29 VVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDI---NKLRRkVGMVFQQFNLFPHLTVLENVTLApikv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 --------MAKSMvsqfdKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA-------------SL 159
Cdd:COG1126 106 kkmskaeaEERAM-----ELLERVGLADKADAYPAQLSGGQQQRVAIARA-------------LAmepkvmlfdeptsAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 160 DIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1126 168 DPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-226 |
3.75e-27 |
|
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: 106.82 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLnDTAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03261 22 DVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI-SGLSEAELYRLRRRMGMLFQSGALFDSLTVFENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 G------MAKSMVSQF--DKLvDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:cd03261 101 PlrehtrLSEEEIREIvlEKL-EAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 172 QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvmHPWL 226
Cdd:cd03261 180 RSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD--DPLV 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-216 |
8.05e-27 |
|
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: 106.67 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiCLApeqRRIGYVFQDARLFPHYKVR----- 94
Cdd:COG1120 23 SLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR-ELA---RRIAYVPQEPPAPFGLTVRelval 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 GNLQYGMAKSMVSQFDKLV-----DLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA------------ 157
Cdd:COG1120 99 GRYPHLGLFGRPSAEDREAveealERTGLEHLADRPVDELSGGERQRVLIARA-------------LAqepplllldept 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 158 -SLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1120 166 sHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-218 |
9.32e-27 |
|
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: 105.59 E-value: 9.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 11 GSHCLQ-IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQR-R--IGYVFQDAR 86
Cdd:cd03224 12 KSQILFgVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG------LPPHERaRagIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 87 LFPHYKVRGNLQYGMAKSMVSQFDKLVD-LLGIAPLL----DRLPGRLSGGEKQRVAIGRALLTAPELLLldeplasLDI 161
Cdd:cd03224 86 IFPELTVEENLLLGAYARRRAKRKARLErVYELFPRLkerrKQLAGTLSGGEQQMLAIARALMSRPKLLL-------LDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984369 162 PRK-------RELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:cd03224 159 PSEglapkivEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-207 |
1.51e-26 |
|
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: 105.28 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLAPEQRRIGYVFQDAR--LFPHYKVR--- 94
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL-RKIRRKEIQMVFQDPMssLNPRMTIGeqi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 -------GNLQYGMAKSMVsQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:cd03257 106 aeplrihGKLSKKEARKEA-VLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 168 LPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03257 185 LDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-214 |
2.78e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.42 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VF-GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYGM--AKSM 105
Cdd:PRK11000 33 VFvGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPPAERGVGMVFQSYALYPHLSVAENMSFGLklAGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VSQFDKLV----DLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIP 181
Cdd:PRK11000 107 KEEINQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRT 186
|
170 180 190
....*....|....*....|....*....|....
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFG-PLE 214
Cdd:PRK11000 187 MIYVTHDQVEAMTLADKIVVLDAGRVAQVGkPLE 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-217 |
3.27e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 7 TQTLGSHCLQIretlPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQricLAPEQRRIGYVFQDAR 86
Cdd:PRK10851 15 TQVLNDISLDI----PSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSR---LHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 87 LFPHYKVRGNLQYGM----------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:PRK10851 85 LFRHMTVFDNIAFGLtvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 157 ASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-216 |
4.02e-26 |
|
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: 104.06 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR-VLNDTAQRIClapeQRRIGYVFQDARLFPHYKVRGNLQ 98
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPHEIA----RLGIGRTFQIPRLFPELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YG----------------MAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:cd03219 98 VAaqartgsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984369 163 RKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03219 178 ETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-211 |
5.33e-26 |
|
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: 103.60 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNG-RVLNDTAQriclapEQRRIGYVFQDARLFPHYKVRGNLQY----- 99
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAE------ARRRLGFVSDSTGLYDRLTARENLEYfagly 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEI 178
Cdd:cd03266 107 GLKGDELTArLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALG 186
|
170 180 190
....*....|....*....|....*....|...
gi 488984369 179 HIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03266 187 KC-ILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-218 |
1.05e-25 |
|
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: 104.07 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdTAQRICLAPEQRRIGYVFQdarlFPHYK-----VR-----G 95
Cdd:TIGR04521 33 FVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDIT-AKKKKKLKDLRKKVGLVFQ----FPEHQlfeetVYkdiafG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGMAKSMVSQ-FDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIgralltapelllldeplAS--------------- 158
Cdd:TIGR04521 108 PKNLGLSEEEAEErVKEALELVGLDEeYLERSPFELSGGQMRRVAI-----------------AGvlamepevlildept 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984369 159 --LDiPR-KRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:TIGR04521 171 agLD-PKgRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-207 |
1.80e-25 |
|
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: 100.55 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeqRRIGYVFQDARLFPHYKVRGNLqy 99
Cdd:cd03230 22 TVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----RRIGYLPEEPSLYENLTVRENL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 gmaksmvsqfdklvdllgiaplldrlpgRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEiH 179
Cdd:cd03230 95 ----------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-G 145
|
170 180
....*....|....*....|....*...
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03230 146 KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-204 |
2.12e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLEL-DFTQTLGSHCL--QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQA---GRIVLNGRVLNDtaqricLAPE 74
Cdd:COG4136 1 MLSLeNLTITLGGRPLlaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTA------LPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 75 QRRIGYVFQDARLFPHYKVRGNLQYGMA--------KSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTA 146
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALPptigraqrRARVEQALEEAGLAGFA---DRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 147 PELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQhLADRVLVLEA 204
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGN 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-226 |
2.18e-25 |
|
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: 102.37 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQRICLapeQRRIGYVFQDARLFPHYKVRGNLQYGM-- 101
Cdd:COG1127 33 ILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYEL---RRRIGMLFQGGALFDSLTVFENVAFPLre 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 --------AKSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:COG1127 110 htdlseaeIRELVLEKLELVGLPGAA---DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvmHPWL 226
Cdd:COG1127 187 LRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD--DPWV 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-216 |
3.45e-25 |
|
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: 101.99 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 23 ASGITAVF-GVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQricLAPEQ--RRIGYVFQDARLFPHYKVRGN--- 96
Cdd:cd03295 25 AKGEFLVLiGPSGSGKTTTMKMINRLIEPTSGEIFIDGE---DIRE---QDPVElrRKIGYVIQQIGLFPHMTVEENial 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 ----LQYGMAK--SMVSQFDKLVDLlGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03295 99 vpklLKWPKEKirERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03295 178 FKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-286 |
8.43e-25 |
|
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: 104.99 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQA---GRIVLNGRVLNDTAQRIClapeQRRIGYVFQD--ARLFPHyKVR 94
Cdd:COG1123 28 TIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR----GRRIGMVFQDpmTQLNPV-TVG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 GNLQYGMAKSMVSQFD------KLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:COG1123 103 DQIAEALENLGLSRAEararvlELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 169 PYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSssvmhpwlpaeQQSTILSATVAAQHPQYAM 248
Cdd:COG1123 183 DLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA-----------APQALAAVPRLGAARGRAA 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 488984369 249 TALALGDQLLWVNRLERPAGDTARIRIQA-SDVSLTLAQ 286
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYPVRGKGGVRAvDDVSLTLRR 290
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-207 |
1.02e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.52 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLAPEQRRIGYVFQDARLFPHYKVRGNL-- 97
Cdd:COG3638 25 EIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRA-LRRLRRRIGMIFQQFNLVPRLSVLTNVla 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 ----QYGMAKSMVSQFDK--------LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplASLDIPRKR 165
Cdd:COG3638 104 grlgRTSTWRSLLGLFPPedreraleALERVGLADKAYQRADQLSGGQQQRVAIARAlvqepkliladepvASLDPKTAR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 166 ELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:COG3638 184 QVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-237 |
1.36e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.08 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQricLAPEQRRIGYVFQDARLFPHYKVRGNLQY---- 99
Cdd:COG1135 33 IFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERE---LRAARRKIGMIFQHFNLLSSRTVAENVALplei 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -GMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldepLAS-------------LDiPRK 164
Cdd:COG1135 110 aGVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA-------------LANnpkvllcdeatsaLD-PET 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 165 -RELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS-----------SSVMHPWLPAEQQS 232
Cdd:COG1135 176 tRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAnpqseltrrflPTVLNDELPEELLA 255
|
....*
gi 488984369 233 TILSA 237
Cdd:COG1135 256 RLREA 260
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-216 |
4.38e-24 |
|
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: 99.64 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMAKSM 105
Cdd:cd03294 52 IFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VSQFDKL------VDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:cd03294 132 VPRAEREeraaeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ 211
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03294 212 KTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-217 |
6.23e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYG--MAK----- 103
Cdd:PRK09452 47 GPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH------VPAENRHVNTVFQSYALFPHMTVFENVAFGlrMQKtpaae 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 --SMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIP 181
Cdd:PRK09452 121 itPRVMEALRMVQLEEFA---QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGIT 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK09452 198 FVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-211 |
6.54e-24 |
|
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: 96.74 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTaQRICLApeqRRIGYVFQdarlfphykvrgnlqy 99
Cdd:cd03214 21 SIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELA---RKIAYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 gmaksmvsqfdkLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:cd03214 81 ------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERG 148
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03214 149 KTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-211 |
7.17e-24 |
|
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: 97.58 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQ-YGMAKS 104
Cdd:cd03263 30 IFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-----RQSLGYCPQFDALFDELTVREHLRfYARLKG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 -----MVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQeiH 179
Cdd:cd03263 105 lpkseIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--G 182
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03263 183 RSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-216 |
1.51e-23 |
|
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: 97.80 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLND-TAQRIClapeQRRIGYVFQDARLFPHYKVRGNL- 97
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIA----RLGIARTFQNPRLFPELTVLENVl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 ---QYGMAKSMVSQF-----------------DKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLA 157
Cdd:COG0411 102 vaaHARLGRGLLAALlrlprarreereareraEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 158 SLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG0411 182 GLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-222 |
4.78e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.01 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLND-TAQRIclapeQRRIGYVFQDA-RLFPHYKVRGNLQYGMAKS- 104
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEeTVWDV-----RRQVGMVFQNPdNQFVGATVQDDVAFGLENIg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 -----MVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-ELLPYLQRLAQEI 178
Cdd:PRK13635 112 vpreeMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD-PRGRrEVLETVRQLKEQK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 179 HIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK13635 191 GITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
29-218 |
9.45e-23 |
|
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: 96.79 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlNDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGNLQYGMA------ 102
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG---EDVTNV---PPHLRHINMVFQSYALFPHMTVEENVAFGLKmrkvpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ---KSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:TIGR01187 75 aeiKPRVLEALRLVQLEEFA---DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-217 |
1.00e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:PRK11432 28 TIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHR---SIQQRDICMVFQSYALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMA---------KSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:PRK11432 102 GLKmlgvpkeerKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK11432 179 IRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-206 |
1.15e-22 |
|
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: 92.69 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdtaqRICLAPEQRRIGYVFQdarlfphykvrgnlqy 99
Cdd:cd00267 21 TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 gmaksmvsqfdklvdllgiaplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEiH 179
Cdd:cd00267 81 -----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-G 130
|
170 180
....*....|....*....|....*..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGK 206
Cdd:cd00267 131 RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-216 |
1.22e-22 |
|
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: 94.94 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdTAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMA--- 102
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN-KLKGKALRQLRRQIGMIFQQFNLIERLSVLENVLSGRLgrr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ---KSMVSQFDK--------LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:cd03256 108 stwRSLFGLFPKeekqralaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 172 QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03256 188 KRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-142 |
1.65e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VF--GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQ-----RRIGYVFQDARLFPHYKVRGNLQYGM 101
Cdd:COG2884 31 VFltGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR------LKRREipylrRRIGVVFQDFRLLPDRTVYENVALPL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488984369 102 ------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:COG2884 105 rvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-244 |
2.19e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.02 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR---VLNDTAqricLAPEQRRIGYVFQDARLFPHYKVRGN 96
Cdd:PRK11153 27 HIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKE----LRKARRQIGMIFQHFNLLSSRTVFDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 LQY-----GMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:PRK11153 103 VALplelaGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS-----------SSVMHPWLPAEQQSTILSATV 239
Cdd:PRK11153 183 LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFShpkhpltrefiQSTLHLDLPEDYLARLQAEPT 262
|
....*
gi 488984369 240 AAQHP 244
Cdd:PRK11153 263 TGSGP 267
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-215 |
2.44e-22 |
|
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: 97.91 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFpHYKVRGNLQY 99
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD----LDPASWRRQIAWVPQNPYLF-AGTIRENLRL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:COG4988 434 GRPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984369 169 PYLQRLAQEiHIpMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:COG4988 514 QALRRLAKG-RT-VILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-214 |
3.63e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNLQYG-----MAKSM 105
Cdd:PRK11650 37 GPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------LEPADRDIAMVFQNYALYPHMSVRENMAYGlkirgMPKAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplasldIPRK------RELLPYL------- 171
Cdd:PRK11650 111 IEErVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA------------------IVREpavflfDEPLSNLdaklrvq 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 172 -----QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG-PLE 214
Cdd:PRK11650 173 mrleiQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGtPVE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-223 |
5.36e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 93.23 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtaqriCLAPEQRRIGYVFQDA---RLFP------- 89
Cdd:COG1121 28 TIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---------PPRRARRRIGYVPQRAevdWDFPitvrdvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 90 ---HYKVRGNLQyGMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplASLDIPRKRE 166
Cdd:COG1121 99 lmgRYGRRGLFR-RPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAlaqdpdlllldepfAGVDAATEEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 167 LLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLeAGKVKAFGPLEEVWSSSVMH 223
Cdd:COG1121 178 LYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLS 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-211 |
1.47e-21 |
|
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: 91.10 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 24 SGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQY---- 99
Cdd:cd03264 25 PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-----RRRIGYLPQEFGVYPNFTVREFLDYiawl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -GMAKSMV-SQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRE-LLPYLQRLAQ 176
Cdd:cd03264 100 kGIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD-PEERIrFRNLLSELGE 178
|
170 180 190
....*....|....*....|....*....|....*
gi 488984369 177 EiHIPMLyVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03264 179 D-RIVIL-STHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
25-216 |
3.99e-21 |
|
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: 90.82 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 25 GITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMA-- 102
Cdd:TIGR02315 29 EFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK-LRGKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLgy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ----KSMVSQFDK--------LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:TIGR02315 108 kptwRSLLGRFSEedkeralsALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:TIGR02315 188 LKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-216 |
4.59e-21 |
|
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: 90.22 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdtaqriclAPEQRRIgYVFQDARLFPHYKVRGNLQYG------- 100
Cdd:TIGR01184 15 SLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--------EPGPDRM-VVFQNYSLLPWLTVRENIALAvdrvlpd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQF-DKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:TIGR01184 86 LSKSERRAIvEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHR 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:TIGR01184 166 VTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-216 |
5.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvLNDTAQRICLAPEQRRIGYVFQdarlFPHYKV----------RGNL 97
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSDIRKKVGLVFQ----YPEYQLfeetiekdiaFGPI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSMVS-QFDKLVDLLGIA--PLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-ELLPYLQR 173
Cdd:PRK13637 111 NLGLSEEEIEnRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD-PKGRdEILNKIKE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK13637 190 LHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-218 |
6.35e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN-DTAQRIclapeQRRIGYVFQDA-RLFPHYKVRGNLQYGMA--- 102
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDI-----RHKIGMVFQNPdNQFVGATVEDDVAFGLEnkg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ---KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK13650 112 iphEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQ 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 180 IPMLYVSHSLDEIQhLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13650 192 MTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
31-206 |
1.26e-20 |
|
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: 88.84 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiCLAPEQRRIGYVFQDARLFPHYKVRGNLQYGM------AKS 104
Cdd:TIGR02673 35 GPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR-QLPLLRRRIGVVFQDFRLLPDRTVYENVALPLevrgkkERE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 MVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEiHIPMLY 184
Cdd:TIGR02673 114 IQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIV 192
|
170 180
....*....|....*....|..
gi 488984369 185 VSHSLDEIQHLADRVLVLEAGK 206
Cdd:TIGR02673 193 ATHDLSLVDRVAHRVIILDDGR 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-216 |
1.83e-20 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 90.15 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQricLAPEQ--RRIGYVFQDARLFPHYKVRGN- 96
Cdd:COG1125 24 TIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE---DIRD---LDPVElrRRIGYVIQQIGLFPHMTVAENi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 -----LQyGMAKSMVSQ-FDKLVDLLGIAP--LLDRLPGRLSGGEKQRVAIGRAlltapelllldepLAS---------- 158
Cdd:COG1125 98 atvprLL-GWDKERIRArVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARA-------------LAAdppillmdep 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 159 ---LD-IPRKR---ELLpylqRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1125 164 fgaLDpITREQlqdELL----RLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEI 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-216 |
2.45e-20 |
|
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: 88.01 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGL-----TRPQAGRIVLNGRVLNDTAQRICLAPeqRRIGYVFQDARLFPhYKVRG 95
Cdd:cd03260 23 IPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR--RRVGMVFQKPNPFP-GSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYG-----MAKSmvSQFDKLV-DLLGIAPL----LDRLPGR-LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:cd03260 100 NVAYGlrlhgIKLK--EELDERVeEALRKAALwdevKDRLHALgLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIST 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 165 RELLPYLQRLAQEIHIPMlyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03260 178 AKIEELIAELKKEYTIVI--VTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-207 |
6.35e-20 |
|
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: 86.69 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiCLAPEQRRIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR-AIPYLRRKIGVVFQDFRLLPDRNVYENVAFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQFD------KLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLpylqRL 174
Cdd:cd03292 103 LEVTGVPPREirkrvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM----NL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 175 AQEIH---IPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03292 179 LKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-231 |
7.38e-20 |
|
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: 90.66 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR--IGYVFQDARLFpHYKVRGNL 97
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ------IDPASLRrqIGVVLQDVFLF-SGTIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSMVSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRAlltapelllldeplASLDIPRKRE 166
Cdd:COG2274 570 TLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAllrnprilildeatSALDAETEAI 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 167 LLPYLQRLAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSSSVMHPWLPAEQQ 231
Cdd:COG2274 650 ILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-216 |
1.25e-19 |
|
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: 86.57 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR---IGYVFQDARLFPHYKVRGN 96
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG------LPPHRIArlgIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 LQYG-MAKSMVSQFDKLVD-LLGIAPLL----DRLPGRLSGGEKQRVAIGRALLTAPELLLldeplasLDIPRK------ 164
Cdd:COG0410 99 LLLGaYARRDRAEVRADLErVYELFPRLkerrRQRAGTLSGGEQQMLAIGRALMSRPKLLL-------LDEPSLglapli 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 165 -RELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG0410 172 vEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-218 |
1.38e-19 |
|
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: 87.10 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQRICLAPEQRRIGYVFQD------ARLfphykVRGNLQYG 100
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLDEENLWEIRKKVGMVFQNpdnqfvGAT-----VEDDVAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 M------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIgralltapelllldeplAS---------------- 158
Cdd:TIGR04520 103 LenlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI-----------------AGvlamrpdiiildeats 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 159 -LDiPR-KRELLPYLQRLAQEIHIPMLYVSHSLDEIqHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:TIGR04520 166 mLD-PKgRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-215 |
2.05e-19 |
|
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: 85.50 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR-VLNDTAQriclapEQRRIGYVFQDARLFPHYKVRGNLQ 98
Cdd:cd03265 22 RVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPRE------VRRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 -----YGMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:cd03265 96 iharlYGVPGAERRErIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984369 173 RLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEE 215
Cdd:cd03265 176 KLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-208 |
3.35e-19 |
|
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: 84.62 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtaqRICLAPEQRRIGYVFQDarlfPHYK-----VR 94
Cdd:cd03226 22 DLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-------PIKAKERRKSIGYVMQD----VDYQlftdsVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 GNLQYGM--AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:cd03226 91 EELLLGLkeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 173 RLAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVK 208
Cdd:cd03226 171 ELAAQGKA-VIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
4.95e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQ--DARLFPHYKVR--- 94
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEETVEKdic 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 -GNLQYGMAKSMVSQF-DKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-ELLPY 170
Cdd:PRK13634 109 fGPMNFGVSEEDAKQKaREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKGRkEMMEM 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13634 188 FYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-211 |
5.21e-19 |
|
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: 84.12 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqriclapEQRRIGYVFQDA---RLFPhYKVR-- 94
Cdd:cd03235 21 EVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRsidRDFP-ISVRdv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 ---GNLQYGMAKSMVSQFDK-----LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:cd03235 91 vlmGLYGHKGLFRRLSKADKakvdeALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQED 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 167 LLPYLQRLAQEIHIpMLYVSHSLDEIQHLADRVLVLeAGKVKAFG 211
Cdd:cd03235 171 IYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-224 |
1.47e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 85.66 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAqriclaPEQRRIGYVFQDARLFPHYKVRGNLQYGMAKSM 105
Cdd:PRK11607 47 IFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP------PYQRPINMMFQSYALFPHMTVEQNIAFGLKQDK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VSQ---FDKLVDLLGIAPLLD---RLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP-RKR---ELLPYLQRLA 175
Cdd:PRK11607 121 LPKaeiASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRmqlEVVDILERVG 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 176 qeihIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSssvmHP 224
Cdd:PRK11607 201 ----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE----HP 241
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-215 |
2.36e-18 |
|
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: 85.97 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQ--RRIGYVFQDARLFpHYKVRGNL 97
Cdd:COG4987 357 TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD------LDEDDlrRRIAVVPQRPHLF-DTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QygMAKSMVSQfDKLVDLL---GIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:COG4987 430 R--LARPDATD-EELWAALervGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 164 KRELLPYLQRLAQEIHIpmLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:COG4987 507 EQALLADLLEALAGRTV--LLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-218 |
3.83e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclapEQRR-IGYVFQ--DARLFPHYKVR----GNLQYG 100
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR-----EVRKfVGLVFQnpDDQIFSPTVEQdiafGPINLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVS-QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK13652 109 LDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYG 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13652 189 MTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-219 |
5.44e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLnGRVLNDTAqrICLAPEQRRI-------GYVFQDARLFPHYKVRGNLQ 98
Cdd:PRK11264 31 VVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTA--RSLSQQKGLIrqlrqhvGFVFQNFNLFPHRTVLENII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMA-------KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:PRK11264 108 EGPVivkgepkEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984369 172 QRLAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK11264 188 RQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-206 |
7.17e-18 |
|
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: 79.73 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeQRRIGYVFQDARLFpHYKVRGNLqy 99
Cdd:cd03228 24 TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTIRENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 gmaksmvsqfdklvdllgiaplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:cd03228 97 -----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKT 147
|
170 180
....*....|....*....|....*..
gi 488984369 180 IpmLYVSHSLDEIQHlADRVLVLEAGK 206
Cdd:cd03228 148 V--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-207 |
1.42e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVlngrvlndtAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:PRK11247 35 IPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---------AGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHI 180
Cdd:PRK11247 106 LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGF 185
|
170 180
....*....|....*....|....*..
gi 488984369 181 PMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK11247 186 TVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-216 |
1.57e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.52 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 7 TQTLGSHCLQIRetlpASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLApeQRRIGYVFQDAR 86
Cdd:PRK09493 14 TQVLHNIDLNID----QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI--RQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 87 LFPHYKVRGNLQYG------MAKSMVSQFDK-LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK09493 88 LFPHLTALENVMFGplrvrgASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 160 DIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-206 |
4.28e-17 |
|
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: 78.67 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQ- 98
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE-----PIRDAREDYRRRLAYLGHADGLKPELTVRENLRf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 ----YGMAKSMvSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTapelllldepLASLDIPRKRELLPYLQRL 174
Cdd:COG4133 99 waalYGLRADR-EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSpaplwlldepFTALDAAGVALLAELIAAH 177
|
170 180 190
....*....|....*....|....*....|....*
gi 488984369 175 AQE---IhipmLYVSHslDEIQHLADRVLVLEAGK 206
Cdd:COG4133 178 LARggaV----LLTTH--QPLELAAARVLDLGDFK 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-231 |
6.02e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 23 ASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNG---RVLNDTAQRICLAPEQR------RIGYVFQDARLFPHYKV 93
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLKVADKNQlrllrtRLTMVFQHFNLWSHMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNLQ------YGMAKSMV-SQFDKLVDLLGIAPLL-DRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK10619 110 LENVMeapiqvLGLSKQEArERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 166 ELLPYLQRLAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSsvmhPWLPAEQQ 231
Cdd:PRK10619 190 EVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN----PQSPRLQQ 250
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-207 |
6.11e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 23 ASGITAVF-GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN----DTAQRICLApeQRRIGYVFQDARLFPHYKVRGNL 97
Cdd:PRK11124 26 PQGETLVLlGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktPSDKAIREL--RRNVGMVFQQYNLWPHLTVQQNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 ------QYGMAKS-MVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:PRK11124 104 ieapcrVLGLSKDqALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984369 171 LQRLaQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK11124 184 IREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-211 |
7.68e-17 |
|
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: 78.40 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlNDTAQrICLAPEQRRIGYVFQDARLFpHYKVRGNLQYGMAKSMVS 107
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQ-LDPADLRRNIGYVPQDVTLF-YGTLRDNITLGAPLADDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 QFDKLVDLLGIAPLLDRLP----------GR-LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAq 176
Cdd:cd03245 109 RILRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL- 187
|
170 180 190
....*....|....*....|....*....|....*
gi 488984369 177 eIHIPMLYVSHSLDEIQhLADRVLVLEAGKVKAFG 211
Cdd:cd03245 188 -GDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-205 |
1.19e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.75 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNdtaqriclAPEQRRiGYVFQDARLFPHYKVRGNLQY 99
Cdd:COG4525 29 TIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--------GPGADR-GVVFQKDALLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -----GMAKS----MVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD-IPRKR--EL 167
Cdd:COG4525 100 glrlrGVPKAerraRAEELLALVGLADFA---RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDaLTREQmqEL 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 168 lpyLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAG 205
Cdd:COG4525 177 ---LLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.12 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 3 ELDFTQTLGSHCLQ-IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRicLAPEQRRIGYV 81
Cdd:PRK13636 10 ELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG--LMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 82 FQ--DARLFPHyKVRGNLQYGMA------KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:PRK13636 88 FQdpDNQLFSA-SVYQDVSFGAVnlklpeDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 154 EPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-215 |
1.25e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 80.92 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 22 PASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFPHyKVRGNLQYG- 100
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD----YTLASLRRQVALVSQDVVLFND-TIANNIAYGr 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:TIGR02203 431 TEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 170 YLQRLAQEihIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:TIGR02203 511 ALERLMQG--RTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-224 |
1.79e-16 |
|
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: 78.94 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQA---GRIVLNGRVLNDtaqricLAPEQ------RRIGYVFQD--ARLFPHYKVR 94
Cdd:COG0444 33 TLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLK------LSEKElrkirgREIQMIFQDpmTSLNPVMTVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 ----------GNLQYGMAKSMVsqfDKLVDLLGIAP---LLDRLPGRLSGGEKQRVAIGRAlltapelllldepLAS--- 158
Cdd:COG0444 107 dqiaeplrihGGLSKAEARERA---IELLERVGLPDperRLDRYPHELSGGMRQRVMIARA-------------LALepk 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 159 ----------LDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHP 224
Cdd:COG0444 171 lliadepttaLDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP-RHP 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-214 |
4.03e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN-DTAQRIclapeQRRIGYVFQDA-RLFPHYKVRGNLQYGMA-- 102
Cdd:PRK13632 38 VAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEI-----RKKIGIIFQNPdNQFIGATVEDDIAFGLEnk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ----KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEI 178
Cdd:PRK13632 113 kvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTR 192
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984369 179 HIPMLYVSHSLDEIQhLADRVLVLEAGKVKAFG-PLE 214
Cdd:PRK13632 193 KKTLISITHDMDEAI-LADKVIVFSEGKLIAQGkPKE 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-207 |
4.79e-16 |
|
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: 74.77 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclAPEQRRIGYVFQdarlfphykvrgnlqygmaksm 105
Cdd:cd03216 28 VHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR---DARRAGIAMVYQ---------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 vsqfdklvdllgiaplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEiHIPMLYV 185
Cdd:cd03216 83 -----------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFI 138
|
170 180
....*....|....*....|..
gi 488984369 186 SHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03216 139 SHRLDEVFEIADRVTVLRDGRV 160
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-215 |
4.83e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.05 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQ--RRIGYVFQDARLFpHYKVRGNL 97
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD------LTLESlrRQIGVVPQDTFLF-SGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRAlltapelllldeplASLDIPRKRE 166
Cdd:COG1132 435 RYGRPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARAllkdppilildeatSALDTETEAL 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 167 LLPYLQRLAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:COG1132 515 IQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-207 |
5.39e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQRiclAPEQRRIGYVFQDA--RLFPHYKVRGNLQYGM-- 101
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQR---KAFRRDIQMVFQDSisAVNPRKTVREIIREPLrh 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 -----AKSMVSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:PRK10419 119 llsldKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQ 198
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 176 QEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK10419 199 QQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
16-211 |
5.98e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNG------RVLNDTAQRIClapeQRRIGYVFQDARLFP 89
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL----RQKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 90 HYKVRGNLQ------YGMAKSM-VSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:COG4161 96 HLTVMENLIeapckvLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 163 RKRELLPYLQRLAQeIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:COG4161 176 ITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-216 |
6.09e-16 |
|
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: 76.11 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFPHyKVRGNLQY 99
Cdd:cd03254 25 SIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD----ISRKSLRSMIGVVLQDTFLFSG-TIMENIRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELl 168
Cdd:cd03254 100 GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID-TETEKL- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 169 pyLQRLAQEIhipM-----LYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEV 216
Cdd:cd03254 178 --IQEALEKL---MkgrtsIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-249 |
6.56e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.77 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQricLAPEQRR-----IGYVFQDA--RLFPHYKVRGNLQYG 100
Cdd:TIGR02769 41 GLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQ---DLYQ---LDRKQRRafrrdVQLVFQDSpsAVNPRMTVRQIIGEP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 M-------AKSMVSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:TIGR02769 115 LrhltsldESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLR 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 173 RLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvmHPwlpaeqQSTILSATVAAQHPQYAMT 249
Cdd:TIGR02769 195 KLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFK--HP------AGRNLQSAVLPEHPVRRSI 263
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-219 |
9.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRR-IGYVFQdarlFPHYK-----V 93
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKeIGLVFQ----FPEYQlfqetI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNLQYG---MAKSMVSQFDKLVDLLGIAPL----LDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK13645 109 EKDIAFGpvnLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 167 LLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-216 |
1.42e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQYGMAKSM 105
Cdd:PRK10070 56 IFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VS---QFDKLVDLL---GIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK10070 136 INaeeRREKALDALrqvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQ 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK10070 216 RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-211 |
2.20e-15 |
|
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: 73.85 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclapeqrRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03269 22 SVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN--------RIGYLPEERGLYPKMKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -----GMAKSMV-SQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR 173
Cdd:cd03269 94 laqlkGLKKEEArRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD-PVNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03269 173 ELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-222 |
2.65e-15 |
|
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: 74.35 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVlngRVLNDTAQRICLAPEQRRIGYVfqDARLfpHYKVRGNLQ-------- 98
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLPPTYGNDV---RLFGERRGGEDVWELRKRIGLV--SPAL--QLRFPRDETvldvvlsg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 -YGMA-------KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:COG1119 105 fFDSIglyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:COG1119 185 LDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-207 |
2.85e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTrPQAGRIVLNGRVLNDtaqricLAPEQ--RRIGYVFQDARLFpHYKVRGNL 97
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRE------LDPESwrKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSMVSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 167 LLPYLQRLAQeiHIPMLYVSHSLDEIQHLaDRVLVLEAGKV 207
Cdd:PRK11174 524 VMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-228 |
3.16e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 19 ETLpasgitAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR-----IGYVFQD--ARLFPHY 91
Cdd:PRK15079 48 ETL------GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG------MKDDEWRavrsdIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 92 KVrGNL--------QYGMAKSMVSQFDK-LVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK15079 116 TI-GEIiaeplrtyHPKLSRQEVKDRVKaMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 162 PRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPWLPA 228
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP-LHPYTKA 260
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-202 |
5.02e-15 |
|
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: 73.03 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlnDTAQRICLAPEQ--RR--IGYVFQDARLFPHYKVRG 95
Cdd:TIGR03608 20 TIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG----QETPPLNSKKASkfRRekLGYLFQNFALIENETVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGMAKSMVSQFDK---LVDLL---GIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:TIGR03608 96 NLDLGLKYKKLSKKEKrekKKEALekvGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLD 175
|
170 180 190
....*....|....*....|....*....|...
gi 488984369 170 YLQRLAQEIHIpMLYVSHSLdEIQHLADRVLVL 202
Cdd:TIGR03608 176 LLLELNDEGKT-IIIVTHDP-EVAKQADRVIEL 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-219 |
7.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNG-RVLNDTAQRIclapeQRRIGYVFQDarlfPHYKVRGNL-Q 98
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqAITDDNFEKL-----RKHIGIVFQN----PDNQFVGSIvK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMA-------------KSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK13648 103 YDVAfglenhavpydemHRRVSEALKQVDMLERA---DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984369 166 ELLPYLQRLAQEIHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-215 |
7.70e-15 |
|
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: 73.03 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFpHYKVRGNLQY 99
Cdd:cd03253 23 TIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE----VTLDSLRRAIGVVPQDTVLF-NDTIGYNIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:cd03253 98 GRPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984369 169 PYLQRLAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:cd03253 178 AALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-207 |
8.19e-15 |
|
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: 71.69 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR--VLNDTAQRIclapeQRRIGYVFQDAR---LFPHYKVRGNLqyg 100
Cdd:cd03215 28 IVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAI-----RAGIAYVPEDRKregLVLDLSVAENI--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 maksmvsqfdklvdllgiaplldRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQE--- 177
Cdd:cd03215 100 -----------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgka 156
|
170 180 190
....*....|....*....|....*....|
gi 488984369 178 IhipmLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03215 157 V----LLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-221 |
9.24e-15 |
|
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: 72.58 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlndtaQRICLAPEQRR----IGYVFQDARLFPHYKVRGNL---- 97
Cdd:cd03218 28 IVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-------QDITKLPMHKRarlgIGYLPQEASIFRKLTVEENIlavl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 --QYGMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:cd03218 101 eiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 176 QEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSV 221
Cdd:cd03218 181 DR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-220 |
1.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLndTAQRICLApeQRRIGYVFQDA-RLFPHYKVRGNLQYGMA---- 102
Cdd:PRK13642 37 SIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL--TAENVWNL--RRKIGMVFQNPdNQFVGATVEDDVAFGMEnqgi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 --KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHI 180
Cdd:PRK13642 113 prEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 181 PMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSSS 220
Cdd:PRK13642 193 TVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-215 |
1.34e-14 |
|
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: 72.26 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFpHYKVRGNLQY 99
Cdd:cd03251 24 DIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD----YTLASLRRQIGLVSQDVFLF-NDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GmaKSMVSQfDKLVDLLGIAPLLD---RLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:cd03251 99 G--RPGATR-EEVEEAARAANAHEfimELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984369 166 ELLPYLQRLAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:cd03251 176 LVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-217 |
1.60e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQ--DARLFPHYKVR----GNLQYG 100
Cdd:PRK13643 35 TALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEETVLKdvafGPQNFG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQF--DKLvDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQE 177
Cdd:PRK13643 115 IPKEKAEKIaaEKL-EMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 178 IHIPMLyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK13643 194 GQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-211 |
2.18e-14 |
|
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: 70.66 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQA--GRIVLNGRvlNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQYGmAK 103
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGR--PLDKRSF-----RKIIGYVPQDDILHPTLTVRETLMFA-AK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 smvsqfdklvdllgiaplldrLPGrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPML 183
Cdd:cd03213 109 ---------------------LRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIIC 166
|
170 180
....*....|....*....|....*...
gi 488984369 184 YVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03213 167 SIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-205 |
2.62e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 17 IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNG-RVLNDTAQRiclapeqrriGYVFQDARLFPHYKVRG 95
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkPVEGPGAER----------GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGMAKSMVS---------QFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK11248 90 NVAFGLQLAGVEkmqrleiahQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 167 LLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAG 205
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-202 |
3.13e-14 |
|
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: 73.47 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFPHyKVRGNLQY 99
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD----ADADSWRDQIAWVPQHPFLFAG-TIAENIRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:TIGR02857 419 ARPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180 190
....*....|....*....|....*....|....
gi 488984369 169 PYLQRLAQEIHIpmLYVSHSLdEIQHLADRVLVL 202
Cdd:TIGR02857 499 EALRALAQGRTV--LLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-218 |
3.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQriclAPEQRRI-GYVFQDARL-FPHYKVRGNLQYGMAKSMV 106
Cdd:PRK13644 33 IIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK----LQGIRKLvGIVFQNPETqFVGRTVEEDLAFGPENLCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 107 --SQFDKLVDL----LGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaQEIHI 180
Cdd:PRK13644 109 ppIEIRKRVDRalaeIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGK 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984369 181 PMLYVSHSLDEIqHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13644 188 TIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-207 |
4.55e-14 |
|
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: 69.55 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR--IGYVFQDARLFPHyKVRGNL 97
Cdd:cd03246 24 SIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ------WDPNELGdhVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 qygmaksmvsqfdklvdllgiaplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaQE 177
Cdd:cd03246 97 -------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KA 144
|
170 180 190
....*....|....*....|....*....|
gi 488984369 178 IHIPMLYVSHSLDEIQhLADRVLVLEAGKV 207
Cdd:cd03246 145 AGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-216 |
5.34e-14 |
|
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: 72.91 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRivLNGRVLNDTAQRICLAPEQR-----RIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGE--VNVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPHRTVLDNLTEA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQFD--KLVDLLGIA--------PLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:TIGR03269 390 IGLELPDELArmKAVITLKMVgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 171 LQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:TIGR03269 470 ILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-224 |
5.45e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.69 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 19 ETLpasgitAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtAQRICLAPEQRRIGYVFQD--ARLFPHYKVRGN 96
Cdd:COG4608 45 ETL------GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG-LSGRELRPLRRRMQMVFQDpyASLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 LQYGM-------AKSMVSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:COG4608 118 IAEPLrihglasKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 169 PYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHP 224
Cdd:COG4608 198 NLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP-LHP 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-216 |
7.66e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLApeqRRIGYVFQDARL-FPhYKVRGNLQ 98
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA---RRRAVLPQHSSLsFP-FTVEEVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMA--KSMVSQFDKLVD----LLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEP------LASLDIPRKRE 166
Cdd:PRK13548 99 MGRAphGLSRAEDDALVAaalaQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPPRWllldepTSALDLAHQHH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984369 167 LLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK13548 179 VLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
26-142 |
9.18e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.00 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlndtaQRICLAPEQRR----IGYVFQDARLFPHYKVRGNL---- 97
Cdd:TIGR04406 29 IVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDG-------QDITHLPMHERarlgIGYLPQEASIFRKLTVEENImavl 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488984369 98 --QYGMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:TIGR04406 102 eiRKDLDRAEREErLEALLEEFQISHLRDNKAMSLSGGERRRVEIARA 149
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-225 |
1.07e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.14 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQ--RRIGYVFQDARL-FPhYKVR-- 94
Cdd:COG4559 23 TLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA------WSPWElaRRRAVLPQHSSLaFP-FTVEev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 ---GNLQYGMAKSmvsQFDKLV----DLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEP-------LASLD 160
Cdd:COG4559 96 valGRAPHGSSAA---QDRQIVrealALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGPRwlfldepTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 161 IPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVMHPW 225
Cdd:COG4559 173 LAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-207 |
1.16e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR--VLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQYGMAK 103
Cdd:COG3845 33 IHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAI-----ALGIGMVHQHFMLVPNLTVAENIVLGLEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 SMVSQFDK---------LVDLLGIAPLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplasL----DI--------- 161
Cdd:COG3845 108 TKGGRLDRkaararireLSERYGLDVDPDAKVEDLSVGEQQRVEILKA----------------LyrgaRIlildeptav 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 162 --PR-KRELLPYLQRLAQE---IhipmLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:COG3845 172 ltPQeADELFEILRRLAAEgksI----IFITHKLREVMAIADRVTVLRRGKV 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-219 |
1.21e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeQRRIGYVFQDARLFPHYKVRGNLQYGMAKSM 105
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLSFEFDVRQVVEMGRTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 vSQFDKL-----------VDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK09536 107 -SRFDTWtetdraaveraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 175 AQEIHIPMLYVsHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK09536 186 VDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-207 |
1.28e-13 |
|
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: 69.67 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaQRICLApeqRRIGYVF-QDARLFPHYKVRGNLQ 98
Cdd:cd03267 43 TIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK--RRKKFL---RRIGVVFgQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 -----YGMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:cd03267 118 llaaiYDLPPARFKKrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLK 197
|
170 180 190
....*....|....*....|....*....|....*
gi 488984369 173 RLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03267 198 EYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-207 |
1.44e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 27 TAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQ--DARLFPHYKVR----GNLQYG 100
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEETVLKdvafGPQNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 MAKSMVSQF--DKLVdLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQE 177
Cdd:PRK13649 116 VSQEEAEALarEKLA-LVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS 194
|
170 180 190
....*....|....*....|....*....|
gi 488984369 178 iHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK13649 195 -GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-226 |
1.57e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 24 SGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLnDTAQRICLAPEQRrIGYVFQDA--RLFpHYKVRGNLQY-- 99
Cdd:PRK13638 27 SPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQ-VATVFQDPeqQIF-YTDIDSDIAFsl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 ---GMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL- 174
Cdd:PRK13638 104 rnlGVPEAEITRrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIv 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 175 AQEIHIpmLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS-------SSVMHPWL 226
Cdd:PRK13638 184 AQGNHV--IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFActeameqAGLTQPWL 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
3.21e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAP---EQRRIGYVFQDARLFPHYKVRGN 96
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR------LTPakaHQLGIYLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 LQYGMAKSMVSQ--FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK15439 107 ILFGLPKRQASMqkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 175 aQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEE 215
Cdd:PRK15439 187 -LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-207 |
4.03e-13 |
|
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: 67.63 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRRIGYVFQDARLFPHYKVRGNL-- 97
Cdd:cd03268 22 HVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK------NIEALRRIGALIEAPGFYPNLTARENLrl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 ---QYGMAKSMVsqfDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:cd03268 96 larLLGIRKKRI---DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL 172
|
170 180 190
....*....|....*....|....*....|...
gi 488984369 175 AQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:cd03268 173 RDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-204 |
4.62e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR--IGYVFQDARLFPHyKVRGNL 97
Cdd:PRK10247 29 SLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST------LKPEIYRqqVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYG-MAKSMVSQFDKLVDLLGIAPL----LDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:PRK10247 102 IFPwQIRNQQPDPAIFLDDLERFALpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIH 181
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 173 RLAQEIHIPMLYVSHSLDEIQHlADRVLVLEA 204
Cdd:PRK10247 182 RYVREQNIAVLWVTHDKDEINH-ADKVITLQP 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-207 |
7.99e-13 |
|
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: 67.11 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeQRRIGYVFQDARLFPHyKVRGNLQY 99
Cdd:cd03248 36 TLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GM----------------AKSMVSQFDKlvdllGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:cd03248 111 GLqscsfecvkeaaqkahAHSFISELAS-----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 164 KRELLPYLQRLAQEIHIpmLYVSHSLDEIQHlADRVLVLEAGKV 207
Cdd:cd03248 186 EQQVQQALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
28-142 |
8.31e-13 |
|
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: 67.07 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQRicLAPEQRRIGYVFQDARLFPHYKVRGN------LQy 99
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDAR--ARLRARHVGFVFQSFQLLPTLTALENvmlpleLA- 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488984369 100 GMAKSmvsqFDKLVDLL---GIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:COG4181 119 GRRDA----RARARALLervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-216 |
1.00e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGNL-------Q 98
Cdd:COG1129 32 VHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR---DAQAAGIAIIHQELNLVPNLSVAENIflgreprR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGM--AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQ 176
Cdd:COG1129 109 GGLidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 177 EiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1129 189 Q-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-222 |
1.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.52 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQA---GRIVLNGRVLN-DTAQRIclapeQRRIGYVFQDA-RLFPH 90
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTaKTVWDI-----REKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 91 YKVRGNLQYGMA------KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:PRK13640 100 ATVGDDVAFGLEnravprPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 165 RELLPYLQRLAQEIHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
28-238 |
1.44e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR--VLNDTAQRICLapeQRRIGYVFQD--ARLFPHYKVRGNLQYGM-- 101
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQdlLKADPEAQKLL---RQKIQIVFQNpyGSLNPRKKVGQILEEPLli 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 -----AKSMVSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:PRK11308 122 ntslsAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQ 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984369 176 QEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPWLPAeqqstILSAT 238
Cdd:PRK11308 202 QELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP-RHPYTQA-----LLSAT 258
|
|
| Mop |
TIGR00638 |
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ... |
290-350 |
1.68e-12 |
|
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins. [Transport and binding proteins, Anions]
Pssm-ID: 273189 [Multi-domain] Cd Length: 69 Bit Score: 61.99 E-value: 1.68e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 290 TSIRNILRAEVVQYLEVNGQIEVQLRVSG-RLLWARISPWARDDLAIAPGQQVFAQIKSVSI 350
Cdd:TIGR00638 3 TSARNQLKGKVVAIEDGDVNAEVDLLLGGgTKLTAVITLESVAELGLKPGKEVYAVIKAPWV 64
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-222 |
1.84e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIcLApeqRRIGYVFQD----ARL-------- 87
Cdd:COG4604 23 TIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-LA---KRLAILRQEnhinSRLtvrelvaf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 --FPHYKVRGNLQygmAKSMVsqfDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIgralltapelllldeplASLDIPRKR 165
Cdd:COG4604 99 grFPYSKGRLTAE---DREII---DEAIAYLDLEDLADRYLDELSGGQRQRAFIamvlaqdtdyvlldeplNNLDMKHSV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 166 ELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:COG4604 173 QMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVL 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
1.98e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVL--NDTAQRICLAPEQRRIGYVFQDARLFPHYKVRGNLQ 98
Cdd:PRK14246 33 IPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMAKSMVS---QFDKLVD----LLGI-APLLDRL---PGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK14246 113 YPLKSHGIKekrEIKKIVEeclrKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 168 LPYLQRLAQEIHIpmLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK14246 193 EKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-222 |
2.96e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLND-----TAQRICLAPEQ--RRIGYVFQDARLFPHYK 92
Cdd:PRK10575 33 TFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskaFARKVAYLPQQlpAAEGMTVRELVAIGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 93 VRGNL-QYGMAKSmvSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:PRK10575 113 WHGALgRFGAADR--EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984369 172 QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-225 |
3.49e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLnDTAQRICLAPEQRRIGYVFQD--ARLFPHY----------KVRG 95
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLQALRRDIQFIFQDpyASLDPRQtvgdsimeplRVHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGMAKSMVSQFDKLVDLLGIAPLldRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:PRK10261 433 LLPGKAAAARVAWLLERVGLLPEHAW--RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984369 176 QEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPW 225
Cdd:PRK10261 511 RDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP-QHPY 559
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-226 |
5.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.62 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQ--DARLFPHYKVR----GNLQYGM 101
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFENTVLKdvefGPKNFGF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 ----AKSMVSQFDKLVDLlgIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQE 177
Cdd:PRK13641 117 sedeAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 178 IHIPMLyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvmhPWL 226
Cdd:PRK13641 195 GHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK---EWL 239
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-207 |
6.04e-12 |
|
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: 66.69 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 3 ELDFTQTLGSHCLQ-IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeQRRIGYV 81
Cdd:TIGR01193 478 DVSYSYGYGSNILSdISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 82 FQDARLFPHyKVRGNLQYGmAKSMVSQ--FDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPE 148
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLG-AKENVSQdeIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 149 LLLLDEPLASLDIPRKRELLPYLQRLAqeiHIPMLYVSHSLdEIQHLADRVLVLEAGKV 207
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-140 |
6.18e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRP---QAGRIVLNGRVLNdtaqriclAPEQRRI-GYVFQDARLFPHYKVRGNLQYgMA- 102
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--------AKEMRAIsAYVQQDDLFIPTLTVREHLMF-QAh 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 103 ------------KSMVSQFDKLVDLLGIAPLLDRLPGR---LSGGEKQRVAIG 140
Cdd:TIGR00955 126 lrmprrvtkkekRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFA 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-211 |
6.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 3 ELDFTQTLGSHCLQ-IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclapEQR-RIGY 80
Cdd:PRK13647 9 DLHFRYKDGTKALKgLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-----WVRsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 81 VFQDarlfPHYKVR----------GNLQYGMAKSMV-SQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPEL 149
Cdd:PRK13647 84 VFQD----PDDQVFsstvwddvafGPVNMGLDKDEVeRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 150 LLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLyVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIV-ATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-141 |
6.66e-12 |
|
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: 64.21 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 24 SG-ITAVFGVSGAGKTSFINAISGLTRPQA---GRIVLNGRVLNdtaqriclaPE--QRRIGYVFQDARLFPHYKVRGNL 97
Cdd:cd03234 32 SGqVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK---------PDqfQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 98 QY-----------GMAKSMVSQFDKLVDLlGIAPLLDRLPGRLSGGEKQRVAIGR 141
Cdd:cd03234 103 TYtailrlprkssDAIRKKRVEDVLLRDL-ALTRIGGNLVKGISGGERRRVSIAV 156
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-142 |
8.72e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 22 PASGItAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQRICLapEQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKL--RAKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488984369 100 -----GMA-KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:PRK10584 112 pallrGESsRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-222 |
9.90e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDT-----AQRICLAPEQRrigyvfqdarLFPH-YKV 93
Cdd:PRK11231 24 SLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssrqlARRLALLPQHH----------LTPEgITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNLQYGMAKSM-----VSQFDK-LVDL----LGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:PRK11231 94 RELVAYGRSPWLslwgrLSAEDNaRVNQameqTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 164 KRELLPYLQRLAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK11231 174 QVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-209 |
1.26e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVL--NDTAQRIclapeQRRIGYVFQDAR---LFPHYKVRGNL--- 97
Cdd:COG1129 280 ILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDAI-----RAGIAYVPEDRKgegLVLDLSIRENItla 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 ---QYGMA-----KSMVSQFDKLVDLLGI-APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLldeplasLDIP-R---- 163
Cdd:COG1129 355 sldRLSRGglldrRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI-------LDEPtRgidv 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984369 164 --KRELLPYLQRLAQE---IhipmLYVSHSLDEIQHLADRVLVLEAGKVKA 209
Cdd:COG1129 428 gaKAEIYRLIRELAAEgkaV----IVISSELPELLGLSDRILVMREGRIVG 474
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-216 |
1.45e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlndtaQRICLAPEQR--RIGYV--FQDARLF------------P 89
Cdd:PRK11300 33 IVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG-------QHIEGLPGHQiaRMGVVrtFQHVRLFremtvienllvaQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 90 HYKVRGNLQYGMAKSMV---SQFDKL------VDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK11300 106 HQQLKTGLFSGLLKTPAfrrAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 161 IPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK11300 186 PKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-219 |
1.98e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 12 SHCLQIRETLpasgitAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLN--DTAQRiclapeQRRIGYVFQDA--RL 87
Cdd:PRK15112 33 SFTLREGQTL------AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYR------SQRIRMIFQDPstSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 FPHYKVRGNLQYGM-------AKSMVSQFDKLVDLLGIAP-LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK15112 101 NPRQRISQILDFPLrlntdlePEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 160 DIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| TOBE |
pfam03459 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
292-350 |
2.03e-11 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 427310 [Multi-domain] Cd Length: 60 Bit Score: 58.83 E-value: 2.03e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 292 IRNILRAEVVQYLEVNGQIEVQLRVSGRL-LWARISPWARDDLAIAPGQQVFAQIKSVSI 350
Cdd:pfam03459 1 ARNQLPGTVTVIEPLGSEVEVRVDLGGGLtLTARITRDSAEELGLAPGDEVWALIKATKV 60
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-214 |
2.10e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRI----VLNGRVLNDTAQRICLAPEQ--------RRIGYVFQdarlFPHYKV 93
Cdd:PRK13631 54 IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKiknfkelrRRVSMVFQ----FPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 R----------GNLQYGMAKSMVSQFDKL-VDLLGI-APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13631 130 FkdtiekdimfGPVALGVKKSEAKKLAKFyLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984369 162 PRKRELLPyLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGK-VKAFGPLE 214
Cdd:PRK13631 210 KGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKiLKTGTPYE 262
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-199 |
2.20e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQDARLFPHYKVRGN----LQYGMAK 103
Cdd:PRK11629 39 AIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENvampLLIGKKK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 SMVSQfDKLVDLLGIAPLLDRL---PGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHI 180
Cdd:PRK11629 119 PAEIN-SRALEMLAAVGLEHRAnhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGT 197
|
170
....*....|....*....
gi 488984369 181 PMLYVSHSLdeiqHLADRV 199
Cdd:PRK11629 198 AFLVVTHDL----QLAKRM 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-219 |
2.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRP-----QAGRIVLNGRVLNDTAQRICLapeQRRIGYVFQDARLFPH 90
Cdd:PRK14271 39 QVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEF---RRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 91 YKVRGNLQYGMAKSMVSQFD-------KLVDLLGIAPLLDRL---PGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEfrgvaqaRLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 161 IPRKRELLPYLQRLAQEIHIpmLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
3.39e-11 |
|
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: 64.32 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 15 LQIR--ETLpasgitAVFGVSGAGKTSFINAISGLTrPQAGRIVLNGRVLnDTAQRICLAPEQRRIGYVFQD--ARLFPH 90
Cdd:COG4172 307 LTLRrgETL------GLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDL-DGLSRRALRPLRRRMQVVFQDpfGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 91 YKVRGNLQYGMA-----KSMVSQFDKLVDLL---GIAP-LLDRLPGRLSGGEKQRVAIGRAlltapelllldepLA---- 157
Cdd:COG4172 379 MTVGQIIAEGLRvhgpgLSAAERRARVAEALeevGLDPaARHRYPHEFSGGQRQRIAIARA-------------LIlepk 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 158 ---------SLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG4172 446 llvldeptsALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-215 |
4.96e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 8 QTLGSHCLQIRETLPASGIT---------AVFGVSGAGKTSFINAISGltRPQA----GRIVLNGRVLNDtaqriclaPE 74
Cdd:PLN03211 69 PKISDETRQIQERTILNGVTgmaspgeilAVLGPSGSGKSTLLNALAG--RIQGnnftGTILANNRKPTK--------QI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 75 QRRIGYVFQDARLFPHYKVRGNLQY----GMAKSMVSQ-----FDKLVDLLGIAPLLDRLPGR-----LSGGEKQRVAIG 140
Cdd:PLN03211 139 LKRTGFVTQDDILYPHLTVRETLVFcsllRLPKSLTKQekilvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 141 RALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEE 215
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-142 |
8.11e-11 |
|
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: 63.15 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 17 IRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQriclAPEQRRIGYVFQDARLFpHYKVRGN 96
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ----DEVRRRVSVCAQDAHLF-DTTVREN 428
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 97 LQYGMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRA 142
Cdd:TIGR02868 429 LRLARPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-217 |
8.23e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTR--PQA---GRIVLNGRvlNDTAQRICLAPEQRRIGYVFQDARLFPHYKVRG 95
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGR--NIYSPDVDPIEVRREVGMVFQYPNPFPHLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYG-----MAKSMvSQFDKLVD-LLGIAPLLD----RL---PGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:PRK14267 105 NVAIGvklngLVKSK-KELDERVEwALKKAALWDevkdRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 163 RKRELLPYLQRLAQEIHIpmLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK14267 184 GTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-207 |
9.22e-11 |
|
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: 61.02 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqricLAPEQRR--IGYVFQDARLFPHyKVRGNL 97
Cdd:cd03249 25 TIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD------LNLRWLRsqIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSMVSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:cd03249 98 RYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 167 LLPYLQRLAQEIHIpmLYVSHSLDEIQHlADRVLVLEAGKV 207
Cdd:cd03249 178 VQEALDRAMKGRTT--IVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-207 |
9.46e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndTAQRICLA----PEQRRI-----GYVFQDAR--LFPHYKVRGN 96
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMR----DGQLRDLYalseAERRRLlrtewGFVHQHPRdgLRMQVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 L----------QYGMAKSMVSQFDKLVDllgIAPL-LDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK11701 112 IgerlmavgarHYGDIRATAGDWLERVE---IDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 166 ELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK11701 189 RLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-207 |
1.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQ--DARLFPHYKVR----GNLQYGM 101
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVEReiifGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 AKSMVSQ--FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK13646 117 NLDEVKNyaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEN 196
|
170 180
....*....|....*....|....*...
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK13646 197 KTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-223 |
1.65e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLA------PEQRRIGYVFQDARLFPH-----YKVRGNLQY 99
Cdd:PRK15439 296 GVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvylPEDRQSSGLYLDAPLAWNvcaltHNRRGFWIK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVsqFDKLVDLLGIA-PLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEi 178
Cdd:PRK15439 376 PARENAV--LERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ- 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 179 HIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVMH 223
Cdd:PRK15439 453 NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMR 497
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-230 |
1.81e-10 |
|
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: 60.19 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlNDTAQrICLAPEQRRIGYVFQDARLFpHYKVRGNLQYGMAKSM 105
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLAL-ADPAWLRRQVGVVLQENVLF-NRSIRDNIALADPGMS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 106 VSQFDKLVDLLGIAPLLDRLP-----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:cd03252 105 MERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 175 AQEIHIpmLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWSSSVMHPWLPAEQ 230
Cdd:cd03252 185 CAGRTV--IIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-160 |
1.94e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 1 MLELDFTQTLGSHCLQIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTaqricLAPEQRRIGY 80
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-----LCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 81 VFQDARLFPHYKVRGNLQYGMAKSMVS-QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAvGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
.
gi 488984369 160 D 160
Cdd:PRK13540 159 D 159
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-207 |
2.13e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRicLAPEQRR-IGYVFQDARLFPHYKVRGNLQYGMAKSMVSQF 109
Cdd:PRK10908 35 GHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR--EVPFLRRqIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 110 D---KLVDLLGIAPLLDR---LPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLpylqRLAQE---IHI 180
Cdd:PRK10908 113 DirrRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL----RLFEEfnrVGV 188
|
170 180
....*....|....*....|....*..
gi 488984369 181 PMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK10908 189 TVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-219 |
2.70e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQaGRIVLNGRVLNDTAQRICLaPEQRRIGYVFQD--ARLFPHYKVRGNLQYGM------- 101
Cdd:PRK15134 319 GESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLL-PVRHRIQVVFQDpnSSLNPRLNVLQIIEEGLrvhqptl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 -AKSMVSQFDKLVDLLGIAPLL-DRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK15134 397 sAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQ 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSS 219
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-209 |
4.10e-10 |
|
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: 60.99 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQ-AGRIVLNGRVLN------DTAQRICLAPEQR-RIGYVfqdarlfPHYKVRGNL 97
Cdd:TIGR02633 288 ILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaqAIRAGIAMVPEDRkRHGIV-------PILGVGKNI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 QYGMAKSM--VSQFDKLVDLLGIAPLLDRLP----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:TIGR02633 361 TLSVLKSFcfKMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 166 ELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKA 209
Cdd:TIGR02633 441 EIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-216 |
4.93e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapEQRRIGYVFQDARLFPHYKVRGNLQYGMA--- 102
Cdd:PRK09700 33 IHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA---AQLGIGIIYQELSVIDELTVLENLYIGRHltk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ----------KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:PRK09700 110 kvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 173 RLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK09700 190 QLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-203 |
6.04e-10 |
|
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: 58.96 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 7 TQTLGSHCLQIRE-TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclAPEQRriGYVfqda 85
Cdd:cd03237 7 KKTLGEFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI--KADYE--GTV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 86 RLFPHYKVRGNLQYgmaksmvSQFD-KLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:cd03237 79 RDLLSSITKDFYTH-------PYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 165 RELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLE 203
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-221 |
6.87e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 24 SGITAVFGVSGAGKTSFINAISGLTRPQaGRIVLNGRV----LNDTAQRICLAPEQRRIGYVFQDARLFPhYKVRGNLQY 99
Cdd:PRK14258 33 SKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnQNIYERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMakSMVS-----QFDKLVD-LLGIAPLLDRLPGR-------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK14258 111 GV--KIVGwrpklEIDDIVEsALKDADLWDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 167 LLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEA-----GKVKAFGPLEEVWSSSV 221
Cdd:PRK14258 189 VESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-216 |
9.18e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.17 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVlndtaqriclAP--EqrrIGYVFQdarlfPHYKVRGN-----LQYGMAK 103
Cdd:COG1134 59 GRNGAGKSTLLKLIAGILEPTSGRVEVNGRV----------SAllE---LGAGFH-----PELTGRENiylngRLLGLSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 SMV-SQFDKLVDLLGIAPLLDrLP-GRLSGGEKQRVAIGRAlltapelllldeplASL--------------DIPRKREL 167
Cdd:COG1134 121 KEIdEKFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVA--------------TAVdpdillvdevlavgDAAFQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 168 LPYLQRLAQEIHIpMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG1134 186 LARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-216 |
9.77e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.31 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTrPQAGRIVLNGRVLNDtaqriCLAPEQRRI-GYVFQDARLFPHYKVRGNLQYGMAKS 104
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSD-----WSAAELARHrAYLSQQQSPPFAMPVFQYLALHQPAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 MVSQ-----FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEP-------LASLDIPRKRELLPYLQ 172
Cdd:COG4138 98 ASSEaveqlLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQlllldepMNSLDVAQQAALDRLLR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 173 RLAQE-IHIPMlyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG4138 178 ELCQQgITVVM--SSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
16-208 |
9.83e-10 |
|
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: 57.79 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTaqriclapEQRRIGYVFQDARLFPHYKVRG 95
Cdd:TIGR03740 18 NISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRK--------DLHKIGSLIESPPLYENLTARE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQY-----GMAKSMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD---IPRKREL 167
Cdd:TIGR03740 90 NLKVhttllGLPDSRIDEVLNIVDLTNTG---KKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpigIQELREL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 168 LpylqRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVK 208
Cdd:TIGR03740 167 I----RSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
9.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTR--PQA---GRIVLNGRVLNdtaqRICLAPEQRRIGYVFQDARLFPHYKVRG 95
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIF----KMDVIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYG-----MAKSMVSQFDKLVDLLGIAPL-------LDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:PRK14247 102 NVALGlklnrLVKSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 164 KRELLPYLQRLAQEIHIPMlyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK14247 182 TAKIESLFLELKKDMTIVL--VTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-216 |
1.40e-09 |
|
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: 59.38 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQricLAPEQ--RRIGYVFQDARLFPhykvrgnl 97
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQ---WDREElgRHIGYLPQDVELFD-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 qyGMAKSMVSQF-----DKLVD---LLGIAPLLDRLP-----------GRLSGGEKQRVAIGRAlltapelllldeplAS 158
Cdd:COG4618 420 --GTIAENIARFgdadpEKVVAaakLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARAlygdprlvvldepnSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 159 LDIPRKRELLPYLQRLAQEIHIPMLyVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATVVV-ITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-207 |
2.18e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.82 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDtaqrICLAPEQRRIGYVFQDARLFpHYKVRGNLQYGMAKSMVs 107
Cdd:PRK13657 365 AIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT----VTRASLRRNIAVVFQDAGLF-NRSIEDNIRVGRPDATD- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 qfDKLVDLLGIAPLLD---RLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK13657 439 --EEMRAAAERAQAHDfieRKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
170 180 190
....*....|....*....|....*....|....
gi 488984369 174 LAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKV 207
Cdd:PRK13657 517 LMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-207 |
2.51e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQRiclaPEQRR---IGYVFQDARL--FPHYKV---------R 94
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKL----PEYKRakyIGRVFQDPMMgtAPSMTIeenlalayrR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 G---NLQYGMAKSMVSQFDKLVDLLGIApLLDRLP---GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELL 168
Cdd:COG1101 110 GkrrGLRRGLTKKRRELFRELLATLGLG-LENRLDtkvGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD-PKTAALV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984369 169 PYL-QRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:COG1101 188 LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| MopI |
COG3585 |
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism]; |
260-350 |
2.75e-09 |
|
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
Pssm-ID: 442804 [Multi-domain] Cd Length: 141 Bit Score: 55.08 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 260 VNRLERPAGDTARIRIQASDVSLTLAQPSGTSIRNILRAEV--VQYLEVNGQIEVQLrVSGRLLWARISPWARDDLAIAP 337
Cdd:COG3585 44 AELLGLVGGKEVAALKKASVVILATDDAMKLSARNQLKGTVtrIERGAVNSEVVLDL-GGGTTLTAVITNESVEELGLKE 122
|
90
....*....|...
gi 488984369 338 GQQVFAQIKSVSI 350
Cdd:COG3585 123 GDEVTALFKASSV 135
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-222 |
2.78e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlnDTAQRICLAPEQRRIGYVFQDARL------------ 87
Cdd:PRK10253 29 EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG----EHIQHYASKEVARRIGLLAQNATTpgditvqelvar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 --FPHYKV----RGNLQYGMAKSMVSQfdklvdllGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK10253 105 grYPHQPLftrwRKEDEEAVTKAMQAT--------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 162 PRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-207 |
2.82e-09 |
|
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: 58.29 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKtsfinaiSGLTR-------PQAGRIVLNGRVLNDTAQriclAPEQRRIGYVFQDARLFpHYK 92
Cdd:COG5265 380 EVPAGKTVAIVGPSGAGK-------STLARllfrfydVTSGRILIDGQDIRDVTQ----ASLRAAIGIVPQDTVLF-NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 93 VRGNLQYGMAKSMVSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:COG5265 448 IAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984369 162 PRKRELLPYLQRLAQeiHIPMLYVSHSLDEIQHlADRVLVLEAGKV 207
Cdd:COG5265 528 RTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-207 |
3.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRI--VLNGRVLNDTAQRICLAPE------------------QRRIGYVFQdarl 87
Cdd:PRK13651 37 AIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVLEklviqktrfkkikkikeiRRRVGVVFQ---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 FPHYK----------VRGNLQYGM----AKSMVSQFDKLVDLlgiaPL--LDRLPGRLSGGEKQRVAIGRALLTAPELLL 151
Cdd:PRK13651 113 FAEYQlfeqtiekdiIFGPVSMGVskeeAKKRAAKYIELVGL----DEsyLQRSPFELSGGQKRRVALAGILAMEPDFLV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 152 LDEPLASLDIPRKRELLPYLQRLAQEIHIPMLyVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK13651 189 FDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
10-216 |
5.81e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 10 LGSHCLQIRetlpASGITAVFGVSGAGKTSFINAISGLTrPQAGRIVLNGRVLNDTAqriclAPEQ-RRIGYVFQDARLF 88
Cdd:PRK03695 12 LGPLSAEVR----AGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWS-----AAELaRHRAYLSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 89 PHYKVRGNLQ-YGMAKSMVSQFDKLVD----LLGIAPLLDRLPGRLSGGEKQRV-------AIGRALLTAPELLLLDEPL 156
Cdd:PRK03695 82 FAMPVFQYLTlHQPDKTRTEAVASALNevaeALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 157 ASLDIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-211 |
6.03e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQricLApeQRRIGYVFQDARLFPHYKVRGNLQ-YGMAKSMVS 107
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR---LA--RARIGVVPQFDNLDLEFTVRENLLvFGRYFGMST 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 QFDKLV--DLLGIAPLLDRLPGR---LSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR--LAQEIHI 180
Cdd:PRK13536 147 REIEAVipSLLEFARLESKADARvsdLSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHLIWERLRslLARGKTI 225
|
170 180 190
....*....|....*....|....*....|.
gi 488984369 181 pmLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:PRK13536 226 --LLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
28-211 |
8.36e-09 |
|
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: 54.24 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPhykvrgnlqygmaksmvs 107
Cdd:cd03247 32 ALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-----SSLISVLNQRPYLFD------------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 qfdklvdllgiAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIpmLYVSH 187
Cdd:cd03247 89 -----------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITH 155
|
170 180
....*....|....*....|....
gi 488984369 188 SLDEIQHlADRVLVLEAGKVKAFG 211
Cdd:cd03247 156 HLTGIEH-MDKILFLENGKIIMQG 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-221 |
9.39e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclapEQRRIGYVFQDARLFPHYKVRGNLQ-----YGMAK 103
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-----ARQRVGVVPQFDNLDPDFTVRENLLvfgryFGLSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 SmvsQFDKLV-DLLGIAPL---LDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR--LAQE 177
Cdd:PRK13537 113 A---AARALVpPLLEFAKLenkADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD-PQARHLMWERLRslLARG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 178 IHIpmLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSV 221
Cdd:PRK13537 189 KTI--LLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-207 |
1.07e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVL--NDTAQRIclapeQRRIGYVFQDaRL---------------- 87
Cdd:COG3845 286 ILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERR-----RLGVAYIPED-RLgrglvpdmsvaenlil 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 ----FPHYKVRGNLQYG----MAKSMVSQFDklvdllgI-APLLDRLPGRLSGGEKQRVAIGRAlltapelllldeplas 158
Cdd:COG3845 360 gryrRPPFSRGGFLDRKairaFAEELIEEFD-------VrTPGPDTPARSLSGGNQQKVILARE---------------- 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 159 ldIPRKRELLpylqrLA------------QEIH----------IPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:COG3845 417 --LSRDPKLL-----IAaqptrgldvgaiEFIHqrllelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-216 |
1.25e-08 |
|
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: 56.35 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLT--RPQAGRIVLN-------GRV-LNDTAQRIC------LAPEQ-------------- 75
Cdd:TIGR03269 28 VLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcGYVeRPSKVGEPCpvcggtLEPEEvdfwnlsdklrrri 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 76 -RRIGYVFQdaRLFPHY---KVRGN-------LQYGMAKSMvsqfDKLVDLLGIAPLLDR---LPGRLSGGEKQRVAIGR 141
Cdd:TIGR03269 108 rKRIAIMLQ--RTFALYgddTVLDNvlealeeIGYEGKEAV----GRAVDLIEMVQLSHRithIARDLSGGEKQRVVLAR 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 142 ALLTAPELLLLDEPLASLDiPRKRELL-PYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:TIGR03269 182 QLAKEPFLFLADEPTGTLD-PQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-216 |
1.39e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlndtaQRICLAP----EQRRIGYVFQDARLFPHYKVRGNLQYGM 101
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLLPlharARRGIGYLPQEASIFRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 -------AKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK10895 104 qirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 175 aQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK10895 184 -RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-216 |
1.53e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISG-LTRPQA-------GRIVLNGRVLN--DTAQRICLA---PEQRRIGYVFQDARL----- 87
Cdd:PRK13547 29 VTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAaiDAPRLARLRavlPQAAQPAFAFSAREIvllgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 FPHYKVRGNLQY---GMAksmvsqfDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEP--------- 155
Cdd:PRK13547 109 YPHARRAGALTHrdgEIA-------WQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPPHDAAQPpryllldep 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 156 LASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK13547 182 TAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-228 |
1.58e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLT----RPQAGRIVLNGRVLNDtaqricLAPEQRR------IGYVFQDA--RLFPHYKV 93
Cdd:PRK11022 35 VVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQR------ISEKERRnlvgaeVAMIFQDPmtSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNL-------QYGMAKSMVSQFDKLVDLLGI---APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:PRK11022 109 GFQImeaikvhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 164 KRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPWLPA 228
Cdd:PRK11022 189 QAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP-RHPYTQA 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-142 |
2.34e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLnDTAQRICLAPEQRRIGYVFQDARLFPHYKVRG 95
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 96 NLQY----------GMAKSMVSQFDKLVDLLGIAPLldrLPGRLSGGEKQRVAIGRA 142
Cdd:PRK11831 104 NVAYplrehtqlpaPLLHSTVMMKLEAVGLRGAAKL---MPSELSGGMARRAALARA 157
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-207 |
2.75e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLND--TAQ----RICLAPEQRRIgyvfqdarlFPHYKVRGNLQY 99
Cdd:PRK11614 33 IVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKimreAVAIVPEGRRV---------FSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQF-DKLVDLLGIAP-LLDR---LPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK11614 104 GGFFAERDQFqERIKWVYELFPrLHERriqRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|...
gi 488984369 175 AQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK11614 184 REQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-142 |
3.60e-08 |
|
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: 52.86 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtaqriclapeqrrIGYVFQDARLFPHyKVRGNLQY 99
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQNG-TIRENILF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 100 GmaksmvSQFD-----KLVDLLGIAPLLDRLPGR-----------LSGGEKQRVAIGRA 142
Cdd:cd03250 89 G------KPFDeeryeKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARA 141
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-219 |
4.83e-08 |
|
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: 54.31 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 15 LQIR--ETLpasgitAVFGVSGAGKTSFINAISGLTRPQA----GRIVLNGRVLNDtaqriclAPEQ-------RRIGYV 81
Cdd:COG4172 31 FDIAagETL------ALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLG-------LSERelrrirgNRIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 82 FQD--ARLFPHYKVrGN-------LQYGM----AKSMVSQfdkLVDLLGI---APLLDRLPGRLSGGEKQRVAIGRAllt 145
Cdd:COG4172 98 FQEpmTSLNPLHTI-GKqiaevlrLHRGLsgaaARARALE---LLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 146 apelllldepLAS-------------LDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGP 212
Cdd:COG4172 171 ----------LANepdlliadepttaLDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
....*..
gi 488984369 213 LEEVWSS 219
Cdd:COG4172 241 TAELFAA 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-220 |
5.78e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQR--ICLAPEQRRIGYVF----QDARLFPHYKV 93
Cdd:PRK15056 29 TVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFpvlvEDVVMMGRYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 94 RGNLQYGMAK--SMVSQFDKLVDLLgiaPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:PRK15056 109 MGWLRRAKKRdrQIVTAALARVDMV---EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 172 QRLAQEIHIpMLYVSHSLDEIQHLADRVlVLEAGKVKAFGPLEEVWSSS 220
Cdd:PRK15056 186 RELRDEGKT-MLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-207 |
6.31e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.09 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 6 FTQTLGSHCLQIreTLPASGITAVFGVSGAGKTSFINAISGLT---RPQAGRIVLNGRVLNDTAQricLAPEQRR----I 78
Cdd:PRK09984 14 FNQHQALHAVDL--NIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGR---LARDIRKsranT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 79 GYVFQDARLFPHYKVRGNLQYG------MAKSMVSQFDKL--------VDLLGIAPLLDRLPGRLSGGEKQRVAIGRALL 144
Cdd:PRK09984 89 GYIFQQFNLVNRLSVLENVLIGalgstpFWRTCFSWFTREqkqralqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984369 145 TAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-229 |
6.50e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLapeQRRIGYVFQDAR---LFPHYKVRGN------LQYGM 101
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITESRRdngFFPNFSIAQNmaisrsLKDGG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 102 AKSMVSQFD---------KLVDLLGI-APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:PRK09700 373 YKGAMGLFHevdeqrtaeNQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 172 QRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKA-FGPLEEVWSSSVMHPWLPAE 229
Cdd:PRK09700 453 RQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNRDDMSEEEIMAWALPQE 510
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-207 |
6.77e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.96 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 16 QIRETLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGR---VLNDTAqricLAPEQRR-IGYVFQDARLFPHY 91
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADA----LAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 92 KVRGNLQY-----GMAKSM-VSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK10535 102 TAAQNVEVpavyaGLERKQrLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 166 ELLPYLQRLAQEIHIpMLYVSHSlDEIQHLADRVLVLEAGKV 207
Cdd:PRK10535 182 EVMAILHQLRDRGHT-VIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-207 |
7.07e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 19 ETLpasgitAVFGVSGAGKTsfINAISGL----TRP---QAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQD--ARLFP 89
Cdd:PRK15134 36 ETL------ALVGESGSGKS--VTALSILrllpSPPvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 90 HYKVRG------NLQYGMAKSMV-SQFDKLVDLLGIAPLLDRL---PGRLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK15134 108 LHTLEKqlyevlSLHRGMRREAArGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984369 160 DIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK15134 188 DVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-218 |
8.75e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.78 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQRICLAPEQRRIGYVFQ--DARLFPHYkVRGNLQYG----- 100
Cdd:PRK13633 40 VILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL---DTSDEENLWDIRNKAGMVFQnpDNQIVATI-VEEDVAFGpenlg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 -MAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:PRK13633 116 iPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYG 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984369 180 IPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13633 196 ITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-225 |
8.83e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 15 LQIRETLpasGITavfGVSGAGKTSFINAISGLTRPQaGRI----VLNGR-VLN-DTAQRICLAPEQrrIGYVFQD--AR 86
Cdd:PRK09473 39 LRAGETL---GIV---GESGSGKSQTAFALMGLLAAN-GRIggsaTFNGReILNlPEKELNKLRAEQ--ISMIFQDpmTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 87 LFPHYKVRGNL------QYGMAKSmvSQFD---KLVDLLGIAPLLDRL---PGRLSGGEKQRVAIGRALLTAPELLLLDE 154
Cdd:PRK09473 110 LNPYMRVGEQLmevlmlHKGMSKA--EAFEesvRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 155 PLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSVmHPW 225
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS-HPY 257
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-216 |
1.14e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEqrrIGYVFQDARLFPHYKVRGNLQYG------- 100
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG---VAIIYQELHLVPEMTVAENLYLGqlphkgg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 ------MAKSMVSQFDKL-VDLLGIAPLldrlpGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK11288 111 ivnrrlLNYEAREQLEHLgVDIDPDTPL-----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 174 LAQEIHIpMLYVSHSLDEIQHLADRVLVLEAG-KVKAFGPLEEV 216
Cdd:PRK11288 186 LRAEGRV-ILYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQV 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-160 |
1.16e-07 |
|
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: 51.34 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03231 22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 100 GMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:cd03231 97 WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-142 |
1.30e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVlndtaqriclapeqrRIGYVFQDARLFPHYKVRGNLQYGMA--KSMVSQ 108
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------------RIGYLPQEPPLDDDLTVLDTVLDGDAelRALEAE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 109 FDKLVDL------------------------------------LGIAP-LLDRLPGRLSGGEKQRVAIGRA 142
Cdd:COG0488 96 LEELEAKlaepdedlerlaelqeefealggweaearaeeilsgLGFPEeDLDRPVSELSGGWRRRVALARA 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-142 |
1.40e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQA-GRIVLNGRVlndtaqriclapeqrriGYVFQDARLFpHYKVRGNLQY 99
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTV-----------------AYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488984369 100 GmAKSMVSQFDKLVDLLGIAPLLDRLPGR-----------LSGGEKQRVAIGRA 142
Cdd:PLN03130 702 G-SPFDPERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARA 754
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-217 |
1.78e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.70 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 25 GITAVFGVSGAGKTSFINAIS--GLTRPQ---AGRIVLNGRvlNDTAQRICLAPEQRRIGYVFQDARLFPhYKVRGNLQY 99
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGH--NIYSPRTDTVDLRKEIGMVFQQPNPFP-MSIYENVVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMV---SQFDKLVD--LLGiAPLLDRLPGRL-------SGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK14239 109 GLRLKGIkdkQVLDEAVEksLKG-ASIWDEVKDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984369 168 LPYLQRLAQEihIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVW 217
Cdd:PRK14239 188 EETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-216 |
2.13e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 51.65 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclapeqrRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:COG4152 23 TVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR--------RIGYLPEERGLYPKMKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 -----GMAKSMV-SQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELlpylqr 173
Cdd:COG4152 95 larlkGLSKAEAkRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVEL------ 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984369 174 LAQEIH------IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:COG4152 168 LKDVIRelaakgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
26-152 |
2.14e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.18 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGK-TSFiNAISGLTRPQAGRIVLNGRVLNDtaqriclAPEQRR----IGYVFQDARLFPHYKVRGNLqyg 100
Cdd:COG1137 31 IVGLLGPNGAGKtTTF-YMIVGLVKPDSGRIFLDGEDITH-------LPMHKRarlgIGYLPQEASIFRKLTVEDNI--- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984369 101 MA------KSMVSQFDKLVDLL---GIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLL 152
Cdd:COG1137 100 LAvlelrkLSKKEREERLEELLeefGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-142 |
2.37e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 22 PASGITAVFGVSGAGKTSFINAISGL--TRPQA---GRIVLNGRVLNDTaqRICLAPEQRRIGYVFQDARLFPH--YKvr 94
Cdd:COG1117 35 PENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDP--DVDVVELRRRVGMVFQKPNPFPKsiYD-- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 95 gNLQYGMAKSMV---SQFDKLV-DLLGIAPL-------LDRLPGRLSGGEKQRVAIGRA 142
Cdd:COG1117 111 -NVAYGLRLHGIkskSELDEIVeESLRKAALwdevkdrLKKSALGLSGGQQQRLCIARA 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-218 |
3.16e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRicLAPEQRRIGYVFQ--DARLF-PHYK---VRGNLQY 99
Cdd:PRK13639 30 MVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS--LLEVRKTVGIVFQnpDDQLFaPTVEedvAFGPLNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAK----SMVSQFDKLVDLLGIApllDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:PRK13639 108 GLSKeeveKRVKEALKAVGMEGFE---NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984369 176 QEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK13639 185 KE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-215 |
3.76e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.65 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeQRRIGYVFQDARLFPHyKVRGNLQY 99
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 G---------MAKSMVSQFDKLVDLL--GIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRell 168
Cdd:TIGR00958 578 GltdtpdeeiMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ--- 654
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984369 169 pYLQRLAQEIHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEE 215
Cdd:TIGR00958 655 -LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ 699
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
31-205 |
4.10e-07 |
|
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: 50.13 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVL---NGRVlnDTAQ---RICLAPEQRRIGYVFQDARLFPhykvRgnlqygmaks 104
Cdd:COG4778 44 GPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWV--DLAQaspREILALRRRTIGYVSQFLRVIP----R---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 mVSQFD----KLVDLlGIAP---------LLDRL--PGRL--------SGGEKQRVAIGRALLTAPELLLLDEPLASLDi 161
Cdd:COG4778 108 -VSALDvvaePLLER-GVDReeararareLLARLnlPERLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLD- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984369 162 PRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAG 205
Cdd:COG4778 185 AANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
121-228 |
5.32e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 121 LLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVL 200
Cdd:PRK10261 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
90 100
....*....|....*....|....*...
gi 488984369 201 VLEAGKVKAFGPLEEVWSSSvMHPWLPA 228
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAP-QHPYTRA 267
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-197 |
6.08e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLT------RPQaGRIVLNGRVLNDtaQRICLAPEQRRIGYVFQDARLFPHyKVR 94
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVE-GKVTFHGKNLYA--PDVDPVEVRRRIGMVFQKPNPFPK-SIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 GNLQYGM-AKSMVSQFDKLVDL-LGIAPLLDRLPGRL-------SGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK14243 109 DNIAYGArINGYKGDMDELVERsLRQAALWDEVKDKLkqsglslSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTL 188
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 166 ELLPYLQRLAQEIHIpmLYVSHSLDEIQHLAD 197
Cdd:PRK14243 189 RIEELMHELKEQYTI--IIVTHNMQQAARVSD 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-222 |
6.69e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 17 IRETLPASGITAVFGVSGAGKTSFINAISG-LTRPQAGRIVLNGRVlndtaqriclapeqrriGYVFQDARLFpHYKVRG 95
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSV-----------------AYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGmAKSMVSQFDKLVDLLGIAPLLDRLPGR-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:PLN03232 698 NILFG-SDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 165 RELLPYLQRLAQEIHIPMLyVSHSLDEIQhLADRVLVLEAGKVKAFGPLEEVWSSSVM 222
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVL-VTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-215 |
8.38e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLNGRVlnDTAQRICLApeqRRIGYVF-QDARLFPHYKVRGNLQ-----YGMAKS 104
Cdd:COG4586 55 GPNGAGKSTTIKMLTGILVPTSGEVRVLGYV--PFKRRKEFA---RRIGVVFgQRSQLWWDLPAIDSFRllkaiYRIPDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 105 mvsQF----DKLVDLLGIAPLLDRlPGR-LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIH 179
Cdd:COG4586 130 ---EYkkrlDELVELLDLGELLDT-PVRqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 180 IPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEE 215
Cdd:COG4586 206 TTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-211 |
1.71e-06 |
|
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: 48.18 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAqRICLAPEQRRIGYVFQDARLFPhykvrgnlqyGMAKSMVSQ 108
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGI---DIS-TIPLEDLRSSLTIIPQDPTLFS----------GTIRSNLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 109 FDKLVDLLGIAPLLDRLPG-RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREllpyLQRLAQEI--HIPMLYV 185
Cdd:cd03369 105 FDEYSDEEIYGALRVSEGGlNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL----IQKTIREEftNSTILTI 180
|
170 180
....*....|....*....|....*.
gi 488984369 186 SHSLDEIQHLaDRVLVLEAGKVKAFG 211
Cdd:cd03369 181 AHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
108-211 |
1.85e-06 |
|
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: 48.52 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHiPMLYVSH 187
Cdd:cd03236 119 KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEH 197
|
90 100
....*....|....*....|....
gi 488984369 188 SLDEIQHLADRVLVLeAGKVKAFG 211
Cdd:cd03236 198 DLAVLDYLSDYIHCL-YGEPGAYG 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-142 |
2.37e-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: 49.40 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 22 PASG-ITAVFGVSGAGKTSFINAISGLTRPQAGRI--------VLN---GRVLNDTAQRicLAPEQRRIGYVFQDARLFP 89
Cdd:COG1245 96 PKKGkVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKK--LANGEIKVAHKPQYVDLIP 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 90 HY---KVRGNL----QYGMAksmvsqfDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:COG1245 174 KVfkgTVRELLekvdERGKL-------DELAEKLGLENILDRDISELSGGELQRVAIAAA 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-225 |
2.61e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQ----AGRIVLNGRVLndtaqrICLAPEQRR------IGYVFQDAR--L 87
Cdd:COG4170 29 TLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDL------LKLSPRERRkiigreIAMIFQEPSscL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 88 FPHYKVRGNLQYGMAKSMVS------------QFDKLVDLLGI---APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLL 152
Cdd:COG4170 103 DPSAKIGDQLIEAIPSWTFKgkwwqrfkwrkkRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984369 153 DEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPW 225
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP-HHPY 254
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-202 |
4.94e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVlngrvlndtaqriclAPEQRRIGYVFQDARLFPHYKVRGNlQY 99
Cdd:PRK09544 26 ELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYVPQKLYLDTTLPLTVN-RF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMVSQFDKLVDL--LGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQE 177
Cdd:PRK09544 90 LRLRPGTKKEDILPALkrVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170 180
....*....|....*....|....*
gi 488984369 178 IHIPMLYVSHSLDEIQHLADRVLVL 202
Cdd:PRK09544 170 LDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-215 |
5.20e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVlndtaqriclapeqrRIGYVFQD-ARLFPHYKVRGNLQ 98
Cdd:COG0488 337 RIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------------KIGYFDQHqEELDPDKTVLDELR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGM-------AKSMVSQF-------DKLVdllgiaplldrlpGRLSGGEKQRVAIGRAlltapelllldepLAS------ 158
Cdd:COG0488 402 DGApggteqeVRGYLGRFlfsgddaFKPV-------------GVLSGGEKARLALAKL-------------LLSppnvll 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 159 -------LDIPRKRELLPYLQrlaqeiHIP--MLYVSHslDE--IQHLADRVLVLEAGKVKAF-GPLEE 215
Cdd:COG0488 456 ldeptnhLDIETLEALEEALD------DFPgtVLLVSH--DRyfLDRVATRILEFEDGGVREYpGGYDD 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-207 |
5.23e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQR------ICLAPEQRRigyvfQDArLFPHYKVRGN--- 96
Cdd:PRK11288 281 IVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagIMLCPEDRK-----AEG-IIPVHSVADNini 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 ------LQYGM---AKSMVSQFDKLVDLLGI-APLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK11288 355 sarrhhLRAGClinNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 167 LLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK11288 435 IYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-140 |
5.61e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGltRPQAGRI-----VLNGRVLNDTAqriclapeQRRIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAE--RVTTGVItggdrLVNGRPLDSSF--------QRSIGYVQQQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 101 MA---------KSMVSQFDKLVDLLGIAPLLDRL---PGR-LSGGEKQRVAIG 140
Cdd:TIGR00956 861 AYlrqpksvskSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIG 913
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-205 |
6.41e-06 |
|
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: 46.56 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 21 LPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLAPEQRRIGYVFQDARLFpHYKVRGNLQYG 100
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 maksmvSQFDK-----LVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:cd03290 103 ------SPFNKqrykaVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 165 RELLPY-LQRLAQEIHIPMLYVSHSLDEIQHlADRVLVLEAG 205
Cdd:cd03290 177 DHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-142 |
7.80e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRI--------VLN---GRVLNDTAQRicLAPEQRRIGYVFQDARLFPHYkVR 94
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGTELQNYFKK--LYNGEIKVVHKPQYVDLIPKV-FK 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 95 GNlqygmaksmVSQ----------FDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRA 142
Cdd:PRK13409 178 GK---------VREllkkvdergkLDEVVERLGLENILDRDISELSGGELQRVAIAAA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-206 |
1.47e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGNLQYGMA----- 102
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK---SSQEAGIGIIHQELNLIPQLTIAENIFLGREfvnrf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 -----KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL-AQ 176
Cdd:PRK10762 111 gridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELkSQ 190
|
170 180 190
....*....|....*....|....*....|
gi 488984369 177 EIHIpmLYVSHSLDEIQHLADRVLVLEAGK 206
Cdd:PRK10762 191 GRGI--VYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-161 |
1.65e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtAQRICLAPEQrrIGYV-FQDArLFPHYKVRGNLQ 98
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-----DIDDPDVAEA--CHYLgHRNA-MKPALTVAENLE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 99 -----YGMAKSMVsqfDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13539 96 fwaafLGGEELDI---AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-135 |
1.69e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRI-VLNGRvLNDTAQRICLAPeqrRIGYVFQ--DARLFPHYKVRGN 96
Cdd:NF033858 23 DIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD-MADARHRRAVCP---RIAYMPQglGKNLYPTLSVFEN 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488984369 97 LQ-----YGMAKSMVSQ-FDKLVDLLGIAPLLDRLPGRLSGGEKQ 135
Cdd:NF033858 99 LDffgrlFGQDAAERRRrIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-99 |
1.70e-05 |
|
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: 44.93 E-value: 1.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 27 TAVFGVSGAGKTSFINAISGltRPQA----GRIVLNGRVLNDTAqriclapeQRRIGYVFQDARLFPHYKVRGNLQY 99
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLDKNF--------QRSTGYVEQQDVHSPNLTVREALRF 102
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-139 |
2.84e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 5 DFTQTLGSHCL-----QIREtlpaSGITAVFGVSGAGKTSFINAISGLTRPQAGRIvlngrvlnDTAQRICLAPEqrrig 79
Cdd:PRK13409 345 DLTKKLGDFSLeveggEIYE----GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKISYKPQ----- 407
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984369 80 YVFQDarlfPHYKVRGNLqygmaKSMVSQFD------KLVDLLGIAPLLDRLPGRLSGGEKQRVAI 139
Cdd:PRK13409 408 YIKPD----YDGTVEDLL-----RSITDDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAI 464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-211 |
2.91e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.78 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAqricLAPEQRRIGYVFQDARLFpHYKVRGNLQY 99
Cdd:PRK11176 365 KIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT----LASLRNQVALVSQNVHLF-NDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 G---------------MAKSM--VSQFDKLVDLL----GIAplldrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:PRK11176 440 ArteqysreqieeaarMAYAMdfINKMDNGLDTVigenGVL---------LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984369 159 LDIPRKRELLPYLQRLAQEIHIpmLYVSHSLDEIQHlADRVLVLEAGKVKAFG 211
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-212 |
3.69e-05 |
|
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: 44.41 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlnDTAQrICLAPEQRRIGYVFQDARLFPHyKVRGNL----QYGMA- 102
Cdd:cd03244 34 GIVGRTGSGKSSLLLALFRLVELSSGSILIDGV---DISK-IGLHDLRSRISIIPQDPVLFSG-TIRSNLdpfgEYSDEe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 ----------KSMVSQFDKLVDLlgiapLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIprkrELLPYLQ 172
Cdd:cd03244 109 lwqalervglKEFVESLPGGLDT-----VVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP----ETDALIQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984369 173 RLAQEI--HIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGP 212
Cdd:cd03244 180 KTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-202 |
4.19e-05 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 43.76 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRivlngrVLNDTAQRICLAPEQRRIgyvfqdARLFPhYKVRGNLQY 99
Cdd:NF040873 14 TIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------VRRAGGARVAYVPQRSEV------PDSLP-LTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 G----------MAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:NF040873 81 GrwarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|...
gi 488984369 170 YLQRLAQEiHIPMLYVSHSLDEIQhLADRVLVL 202
Cdd:NF040873 161 LLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-213 |
6.72e-05 |
|
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: 45.00 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIclapeQRRIGYVFQDARLFPHYKVRGN-LQ 98
Cdd:TIGR01257 952 TFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCPQHNILFHHLTVAEHiLF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 99 YGMAKSMVS-----QFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:TIGR01257 1027 YAQLKGRSWeeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 174 LAQEIHIPMlyVSHSLDEIQHLADRVLVLEAGKVKAFG-PL 213
Cdd:TIGR01257 1107 YRSGRTIIM--STHHMDEADLLGDRIAIISQGRLYCSGtPL 1145
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-216 |
7.90e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 8 QTLGSHCLQIREtLPASGITAV---------FGVSG---AGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRICLApeq 75
Cdd:PRK10762 251 KAPGEVRLKVDN-LSGPGVNDVsftlrkgeiLGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLA--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 76 RRIGYVFQDAR------------------LFPHYKVRGNLQYGMAKSMVSQFdklVDLLGI-APLLDRLPGRLSGGEKQR 136
Cdd:PRK10762 327 NGIVYISEDRKrdglvlgmsvkenmsltaLRYFSRAGGSLKHADEQQAVSDF---IRLFNIkTPSMEQAIGLLSGGNQQK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 137 VAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEV 216
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-209 |
8.14e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQ-AGRIVLNGRVLN------DTAQRICLAPEQR-RIGYVfqdarlfPHYKVRGNl 97
Cdd:PRK13549 290 ILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKirnpqqAIAQGIAMVPEDRkRDGIV-------PVMGVGKN- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 98 qygMAKSMVSQF------DKLVDLLGIAPLLDRLP----------GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13549 362 ---ITLAALDRFtggsriDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984369 162 PRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKVKA 209
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-218 |
8.21e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.53 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPqaGRIVLNGRVLNDTaqrICLAPEQ---RRIGYVFQDAR-------LFPHYKVRG 95
Cdd:PRK10418 31 VLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDG---KPVAPCAlrgRKIATIMQNPRsafnplhTMHTHARET 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 96 NLQYGMAKSMVSQFDKL--VDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK10418 106 CLALGKPADDATLTAALeaVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984369 174 LAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:PRK10418 186 IVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-139 |
9.82e-05 |
|
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: 44.00 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 5 DFTQTLGSHCLQIRE-TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIvlngrvlnDTAQRICLAPEqrrigYVFQ 83
Cdd:COG1245 346 DLTKSYGGFSLEVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISYKPQ-----YISP 412
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984369 84 DArlfpHYKVRGNLQYGMAKSMVSQFDK--LVDLLGIAPLLDRLPGRLSGGEKQRVAI 139
Cdd:COG1245 413 DY----DGTVEEFLRSANTDDFGSSYYKteIIKPLGLEKLLDKNVKDLSGGELQRVAI 466
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-215 |
9.95e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.05 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAisgLTR---PQAGRIVLNGRVLNDTA-----QRICLAPeQRRigYVFQDArlfphy 91
Cdd:PRK11160 362 QIKAGEKVALLGRTGCGKSTLLQL---LTRawdPQQGEILLNGQPIADYSeaalrQAISVVS-QRV--HLFSAT------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 92 kVRGNLQygMAKSMVSQfDKLVDLL---GIAPLLDRLPG----------RLSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:PRK11160 430 -LRDNLL--LAAPNASD-EALIEVLqqvGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 159 LDIPRKRELLPYLQRLAQeiHIPMLYVSHSLDEIQHLaDRVLVLEAGKVKAFGPLEE 215
Cdd:PRK11160 506 LDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-218 |
1.21e-04 |
|
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: 44.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVL----NDTAQRICLAPEQRRIGYVFQD-ARLFPHYKVRGNlqygMA 102
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSDVHQNMGYCPQFDAIDDLLTGrEHLYLYARLRGV----PA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 103 KSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPM 182
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984369 183 LyVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWS 218
Cdd:TIGR01257 2125 L-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-214 |
2.20e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 41.98 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGltRPQ----AGRIVLNGRVLNDtaqricLAPEQR-R--IGYVFQDARLFPHYKVR---- 94
Cdd:COG0396 28 VHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILE------LSPDERaRagIFLAFQYPVEIPGVSVSnflr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 95 --GNLQYGMAKSMVsQFDKLV----DLLGIAP-LLDR-LPGRLSGGEKQR------------VAI------Gralltape 148
Cdd:COG0396 100 taLNARRGEELSAR-EFLKLLkekmKELGLDEdFLDRyVNEGFSGGEKKRneilqmlllepkLAIldetdsG-------- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 149 lllldeplasLDIPRkrellpyLQRLAQ---EIHIP---MLYVSHS---LDEIQhlADRVLVLEAGKVKAFGPLE 214
Cdd:COG0396 171 ----------LDIDA-------LRIVAEgvnKLRSPdrgILIITHYqriLDYIK--PDFVHVLVDGRIVKSGGKE 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-239 |
2.77e-04 |
|
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: 42.15 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVlNDTAQRICLAPEQRRIGYVFQDArlFPHYKVRGNLQYGMAKSMVS 107
Cdd:cd03291 67 AITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-SFSSQFSWIMPGTIKENIIFGVS--YDEYRYKSVVKACQLEEDIT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 108 QF-DKLVDLLGIAPLLdrlpgrLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP--YLQRLAQEIHIpmLY 184
Cdd:cd03291 144 KFpEKDNTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANKTRI--LV 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984369 185 VShsldEIQHL--ADRVLVLEAGKVKAFGPLEEV------WSSSVM----HPWLPAEQQSTILSATV 239
Cdd:cd03291 216 TS----KMEHLkkADKILILHEGSSYFYGTFSELqslrpdFSSKLMgydtFDQFSAERRNSILTETL 278
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
31-142 |
3.78e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.10 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 31 GVSGAGKTSFINAISGLTRPQAGRIVLngrvlndtaqriclaPEQRRIGYVFQDARLfPHYKVRGNLQYGMAKSMVSQfD 110
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIAR---------------PAGARVLFLPQRPYL-PLGTLREALLYPATAEAFSD-A 458
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488984369 111 KLVDLL---GIAPLLDRL------PGRLSGGEKQRVAIGRA 142
Cdd:COG4178 459 ELREALeavGLGHLAERLdeeadwDQVLSLGEQQRLAFARL 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-231 |
4.95e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGrvlNDTAqRICLAPEQRRIGYVFQDARLFPHyKVRGNLQyGMAKSMVSQ 108
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVA-KFGLTDLRRVLSIIPQSPVLFSG-TVRFNID-PFSEHNDAD 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 109 FDKLVDLLGIAPLLDRLPGRL-----------SGGEKQRVAIGRALLTAPELLLLDEPLASLDIpRKRELlpyLQRLAQE 177
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDV-RTDSL---IQRTIRE 1416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 178 --IHIPMLYVSHSLDEIQHlADRVLVLEAGKVKAFGPLEEVWS------SSVMHPWLPAEQQ 231
Cdd:PLN03232 1417 efKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSrdtsafFRMVHSTGPANAQ 1477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-231 |
6.57e-04 |
|
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: 41.85 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVlndtaqriCLAPEQRRIgyvfQDARLfphykvRGNLQY 99
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--------AYVPQQAWI----QNDSL------RENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMAKSMvSQFDKLVDLLGIAPLLDRLPG-----------RLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:TIGR00957 722 GKALNE-KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984369 169 PYL----QRLAQEIHIpmlYVSHSLDEIQHLaDRVLVLEAGKVKAFGPLEEVWS-----SSVMHPWLPAEQQ 231
Cdd:TIGR00957 801 EHVigpeGVLKNKTRI---LVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQrdgafAEFLRTYAPDEQQ 868
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
129-203 |
1.03e-03 |
|
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: 39.48 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 129 LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLE 203
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
182-211 |
1.17e-03 |
|
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: 39.82 E-value: 1.17e-03
10 20 30
....*....|....*....|....*....|
gi 488984369 182 MLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03220 195 VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-141 |
1.46e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVLNDTAQRIClapeqrriGYVFQDARLFPHYKVRGNLQY 99
Cdd:PRK13541 22 TFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488984369 100 -GMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGR 141
Cdd:PRK13541 94 wSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIAR 136
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-206 |
1.50e-03 |
|
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: 40.19 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLtRPQA---GRIVLNGRVLNDTAQRiclAPEQRRIGYVFQDARLFPHYKVRGN 96
Cdd:TIGR02633 23 EVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIR---DTERAGIVIIHQELTLVPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 97 LQYG---------MA-KSMVSQFDKLVDLLGIAPLLDRLP-GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:TIGR02633 99 IFLGneitlpggrMAyNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984369 166 ELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGK 206
Cdd:TIGR02633 179 ILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-228 |
1.81e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPqagrivlNGRVlndTAQR--------ICLAPEQRR------IGYVFQDA 85
Cdd:PRK15093 29 TLTEGEIRGLVGESGSGKSLIAKAICGVTKD-------NWRV---TADRmrfddidlLRLSPRERRklvghnVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 86 R--LFPH---------------YKVRGNLQYGMAKSMVSQFDKLVDLLGIAPLLDRLPGRLSGGEKQRVAIGRALLTAPE 148
Cdd:PRK15093 99 QscLDPServgrqlmqnipgwtYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 149 LLLLDEPLASLDIPRKRELLPYLQRLAQEIHIPMLYVSHSLDEIQHLADRVLVLEAGKVKAFGPLEEVWSSSvMHPWLPA 228
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP-HHPYTQA 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-57 |
1.91e-03 |
|
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: 39.92 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488984369 20 TLPASGITAVFGVSGAGKTSFINAISGLTRPQAGRIVL 57
Cdd:TIGR03719 344 KLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-200 |
2.06e-03 |
|
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: 38.46 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 13 HCLQIRE-TLPASGITAVFGVSGAGKTSFINAisGLTRPQAGRIVlngrvlndtaqriclapeqrrigyvfQDARLFPHY 91
Cdd:cd03238 9 HNLQNLDvSIPLNVLVVVTGVSGSGKSTLVNE--GLYASGKARLI--------------------------SFLPKFSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 92 KVrgnlqygmakSMVSQFDKLVDL-LGIAPLlDRLPGRLSGGEKQRVAIGR--ALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:cd03238 61 KL----------IFIDQLQFLIDVgLGYLTL-GQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLL 129
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 169 PYLQRLAQEIHiPMLYVSHSLDEIQhLADRVL 200
Cdd:cd03238 130 EVIKGLIDLGN-TVILIEHNLDVLS-SADWII 159
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-161 |
2.25e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.06 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVlNDTAQRiclapeQRRIGYVFQDARLFPHYKVRGNLQY--GM----A 102
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDR------SRFMAYLGHLPGLKADLSTLENLHFlcGLhgrrA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984369 103 KSMVSQFDKLVDLLGIAPLLDRlpgRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13543 115 KQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-238 |
3.26e-03 |
|
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: 39.51 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 28 AVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRvlndtaqriclapeqrrIGYVFQDARLFPHyKVRGNLQYGMAK---- 103
Cdd:TIGR01271 456 AVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-TIKDNIIFGLSYdeyr 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 104 -SMVSQFDKLVDLLGIAPLLDRLP-----GRLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP--YLQRLA 175
Cdd:TIGR01271 518 yTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMS 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984369 176 QEIHIpmLYVShsldEIQHL--ADRVLVLEAGKVKAFGPLEEV------WSSSVM----HPWLPAEQQSTILSAT 238
Cdd:TIGR01271 598 NKTRI--LVTS----KLEHLkkADKILLLHEGVCYFYGTFSELqakrpdFSSLLLgleaFDNFSAERRNSILTET 666
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-207 |
3.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTRPQAGRIVLNGRVL-NDTAQR-----ICLAPEQRRIGYVFqdarlfphykvrGNLQY 99
Cdd:PRK10982 276 ILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEainhgFALVTEERRSTGIY------------AYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 100 GMaKSMVSQFDKLVDLLGiapLLD-----------------RLP------GRLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:PRK10982 344 GF-NSLISNIRNYKNKVG---LLDnsrmksdtqwvidsmrvKTPghrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984369 157 ASLDIPRKRELLPYLQRLAQEiHIPMLYVSHSLDEIQHLADRVLVLEAGKV 207
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-141 |
4.08e-03 |
|
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: 39.15 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 29 VFGVSGAGKTSFINAISGLTRPQAGRIVLNgrvlndtaqriclapEQRRIGYVFQDARLFPHYKVRGNLQYGMA--KSMV 106
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------------PGIKVGYLPQEPQLDPTKTVRENVEEGVAeiKDAL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984369 107 SQFD---------------------KLVDLLGIAPLLD------------RLP------GRLSGGEKQRVAIGR 141
Cdd:TIGR03719 101 DRFNeisakyaepdadfdklaaeqaELQEIIDAADAWDldsqleiamdalRCPpwdadvTKLSGGERRRVALCR 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-211 |
9.10e-03 |
|
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: 36.86 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 26 ITAVFGVSGAGKTSFINAISGLTrpqAGRIVLNGRVL-----NDTAQRIClapeQRRIGYVFQDARLFPHYKVRGNLQYG 100
Cdd:cd03233 35 MVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHyngipYKEFAEKY----PGEIIYVSEEDVHFPTLTVRETLDFA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984369 101 mAKSMVSQFdklvdLLGIaplldrlpgrlSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAQEIHI 180
Cdd:cd03233 108 -LRCKGNEF-----VRGI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKT 170
|
170 180 190
....*....|....*....|....*....|..
gi 488984369 181 P-MLYVSHSLDEIQHLADRVLVLEAGKVKAFG 211
Cdd:cd03233 171 TtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
28-66 |
9.21e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.67 E-value: 9.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488984369 28 AVFGVSGAGKTSFINAIS----------GLTR-PQAGRIVLNGR--VLNDTA 66
Cdd:pfam01926 3 ALVGRPNVGKSTLINALTgakaivsdypGTTRdPNEGRLELKGKqiILVDTP 54
|
|
| |
