|
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: 696.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLELNFSQTLGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGY 80
Cdd:PRK11144 1 MLELNFKQQLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 81 VFQDARLFPHYKVRGNLRYGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 161 IPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVMHPWLPKEQQSSILKVSVL 240
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 241 EHHPHYAMTALALGDQHLWVNKLEQPLQTALRIRIQASDVSLVLQPPQQTSIRNVLRAKVAQCYDDNGQVEVQLEVGGKT 320
Cdd:PRK11144 241 EHHPHYAMTALALGDQHLWVNKLDAPLGTALRIRIQASDVSLVLQPPQQSSIRNILRAKVVEIYDDNGQVEVKLEVGGKT 320
|
330 340 350
....*....|....*....|....*....|..
gi 1915297335 321 LWARISPWARDELGIKPGLWLYAQIKSVSITA 352
Cdd:PRK11144 321 LWARITPWARDELALKPGQWLYAQIKSVSITQ 352
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-351 |
0e+00 |
|
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: 525.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 2 LELNFSQTLGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYV 81
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 82 FQDARLFPHYKVRGNLRYGMAKSMAGQ----FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLA 157
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARPSErrisFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 158 SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVMhPWLPKEQQSSILKV 237
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL-PWLAREDQGSLIEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 238 SVLEHHPHYAMTALALGDQHLWVNKLEQPLQTALRIRIQASDVSLVLQPPQQTSIRNVLRAKVAQCYDDN-GQVEVQLEV 316
Cdd:TIGR02142 240 VVAEHDQHYGLTALRLGGGHLWVPENLGPTGARLRLRVPARDVSLALQKPEATSIRNILPARVVEIEDSDiGRVGVVLES 319
|
330 340 350
....*....|....*....|....*....|....*
gi 1915297335 317 GGKTLWARISPWARDELGIKPGLWLYAQIKSVSIT 351
Cdd:TIGR02142 320 GGKTLWARITRWARDELGIAPGTPVFAQIKAVALR 354
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-352 |
0e+00 |
|
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: 512.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLELNFSQTLGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGY 80
Cdd:COG4148 2 MLEVDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 81 VFQDARLFPHYKVRGNLRYGM----AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepl 156
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRkrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRAllssprlllmdepl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 157 ASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVMHPWLPKEQQSSILK 236
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 237 VSVLEHHPHYAMTALALGDQHLWVNKLEQPLQTALRIRIQASDVSLVLQPPQQTSIRNVLRAKVAQCY-DDNGQVEVQLE 315
Cdd:COG4148 242 ATVAAHDPDYGLTRLALGGGRLWVPRLDLPPGTRVRVRIRARDVSLALEPPEGSSILNILPGRVVEIEpADGGQVLVRLD 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 1915297335 316 VGGKTLWARISPWARDELGIKPGLWLYAQIKSVSITA 352
Cdd:COG4148 322 LGGQTLLARITRRSADELGLAPGQTVYAQIKSVALLR 358
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-211 |
2.87e-67 |
|
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: 210.61 E-value: 2.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLELNFSQTLGTHCLTLNETLPaSGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGY 80
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 81 VFQDARLFPHYKVRGNLRYGMAK----SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRkrnrEDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 157 ASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
29-350 |
8.74e-53 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 177.58 E-value: 8.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMA------ 102
Cdd:NF040840 31 ILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK---DITN---LPPEKRGIAYVYQNYMLFPHKTVFENIAFGLKlrkvpk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPM 182
Cdd:NF040840 105 EEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 183 LYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGssvmHPwlPKEQQSSILKV-SVLEHHPHYAMTALALGDQHLwvn 261
Cdd:NF040840 185 IHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFR----RP--KNEFVARFVGFeNIIEGVAEKGGEGTILDTGNI--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 262 KLEQPLQTA--LRIRIQASDVSLVLQpPQQTSIRNVLRAKVAQCYDDNGQVEVQLEVgGKTLWARISPWARDELGIKPGL 339
Cdd:NF040840 256 KIELPEEKKgkVRIGIRPEDITISTE-KVKTSARNEFKGKVEEIEDLGPLVKLTLDV-GIILVAFITRSSFLDLEINEGK 333
|
330
....*....|.
gi 1915297335 340 WLYAQIKSVSI 350
Cdd:NF040840 334 EVYASFKASAV 344
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-350 |
3.00e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.79 E-value: 3.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNdvengICLTPEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:COG1118 24 EIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRERRVGFVFQHYALFPHMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLAS-------------LD 160
Cdd:COG1118 99 GLrvrppsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA-------------LAVepevllldepfgaLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 161 IPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgssvMHP-------------WLP 227
Cdd:COG1118 166 AKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY----DRPatpfvarflgcvnVLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 228 KEQQSSILKVsvlehhphyamtalalGDQHLWVNKLEQPLQTALRIRiqASDVSLVLQPPQQtsirNVLRAKVAQCYDDN 307
Cdd:COG1118 242 GRVIGGQLEA----------------DGLTLPVAEPLPDGPAVAGVR--PHDIEVSREPEGE----NTFPATVARVSELG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1915297335 308 GQVEVQLEVGGKT---LWARISPWARDELGIKPGLWLYAQIKSVSI 350
Cdd:COG1118 300 PEVRVELKLEDGEgqpLEAEVTKEAWAELGLAPGDPVYLRPRPARV 345
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-211 |
3.06e-50 |
|
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: 166.93 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengiclTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPERRNIGMVFQDYALFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03259 93 IAFGLklrgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03259 173 LKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
27-334 |
8.40e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.86 E-value: 8.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRRVGYVFQDARLFPHYKVRGNLRYG--MAKS 104
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP------PKDRNIAMVFQSYALYPHMTVYENIAFPlkLRKV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 MAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldeplasldIPRKRELL----P------- 169
Cdd:COG3839 106 PKAEIDRRVreaaELLGLEDLLDRKPKQLSGGQRQRVALGRA------------------LVREPKVFlldePlsnldak 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 170 -------YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW------------GSSVMhpwlpkeq 230
Cdd:COG3839 168 lrvemraEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYdrpanlfvagfiGSPPM-------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 231 qsSILKVSVLEHHphyamtaLALGDQHLWVN-KLEQPLQTALRIRIQASDVSLVLQPPqqtsirNVLRAKVAQCYDDNGQ 309
Cdd:COG3839 240 --NLLPGTVEGGG-------VRLGGVRLPLPaALAAAAGGEVTLGIRPEHLRLADEGD------GGLEATVEVVEPLGSE 304
|
330 340
....*....|....*....|....*
gi 1915297335 310 VEVQLEVGGKTLWARISPWARDELG 334
Cdd:COG3839 305 TLVHVRLGGQELVARVPGDTRLRPG 329
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-216 |
6.80e-46 |
|
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: 156.34 E-value: 6.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMAK---- 103
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITN---LPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKrkvd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 104 --SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIP 181
Cdd:cd03299 103 kkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVT 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1915297335 182 MLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03299 183 VLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
26-338 |
2.42e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.94 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRRVGYVFQDARLFPHYKVRGNLRYG----- 100
Cdd:COG3842 33 FVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP------PEKRNVGMVFQDYALFPHLTVAENVAFGlrmrg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA-------------SLDIPRKRE 166
Cdd:COG3842 107 VPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA-------------LApeprvllldeplsALDAKLREE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSsvmhpwlPKEQ-------QSSILKVSV 239
Cdd:COG3842 174 MREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER-------PATRfvadfigEANLLPGTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 240 LEHHPhyamTALALGDQHLWVNKLEQ-PLQTALRIRIQASDVSLVLQPPqqtsiRNVLRAKVAQCYDDNGQVEVQLEVG- 317
Cdd:COG3842 247 LGDEG----GGVRTGGRTLEVPADAGlAAGGPVTVAIRPEDIRLSPEGP-----ENGLPGTVEDVVFLGSHVRYRVRLGd 317
|
330 340
....*....|....*....|.
gi 1915297335 318 GKTLWARISPwaRDELGIKPG 338
Cdd:COG3842 318 GQELVVRVPN--RAALPLEPG 336
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-215 |
7.17e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.36 E-value: 7.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLEL-NFSQTLGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRRVG 79
Cdd:COG3840 1 MLRLdDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------LPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 80 YVFQDARLFPHYKVRGNLRYGMAKSM---AGQFDKLVALL---GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLkltAEQRAQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 154 EPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLED 215
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-211 |
9.09e-39 |
|
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: 137.00 E-value: 9.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP------PKDRDIAMVFQNYALYPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYG--MAKSMAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03301 93 IAFGlkLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03301 173 LKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-217 |
2.34e-38 |
|
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: 136.70 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRRVGYVFQDARLFPHYKVRGNLRYG 100
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATD---VPVQERNVGFVFQHYALFRHMTVFDNVAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 M----------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03296 99 LrvkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:cd03296 179 LRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-211 |
4.65e-37 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 132.62 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 10 LGTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRRVGYVFQDARLFP 89
Cdd:cd03298 10 YGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTA---APPADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 90 HYKVRGNLRYGMAKSMA------GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKltaedrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 164 KRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-206 |
4.98e-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: 131.54 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngICLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE--DELPPLRRRIGMVFQDFALFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYgmaksmagqfdklvallgieplldrlpgGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAR 176
Cdd:cd03229 97 IAL----------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQA 148
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 177 EINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:cd03229 149 QLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-142 |
2.13e-35 |
|
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: 126.22 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengICLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD----DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 97 LRYG------MAKSMAGQFDKLVALLGIEPLLDRL----PGGLSGGEKQRVAIGRA 142
Cdd:pfam00005 80 LRLGlllkglSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARA 135
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-209 |
7.00e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.28 E-value: 7.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLndvengiclTPEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:COG1116 33 TVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV---------TGPGPDRGVVFQEPALLPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GM---------AKSMAgqfDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA------------- 157
Cdd:COG1116 104 GLelrgvpkaeRRERA---RELLELVGLAGFEDAYPHQLSGGMRQRVAIARA-------------LAndpevllmdepfg 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 158 SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLEN--GQVKA 209
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-216 |
2.78e-34 |
|
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: 126.13 E-value: 2.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGN 96
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-----RRQIGVLPDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRY-GMAKSMAGQ-----FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:COG4555 95 IRYfAELYGLFDEelkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 171 LQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4555 175 LRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-216 |
1.45e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.02 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGNLR- 98
Cdd:COG1131 22 TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-----RRRIGYVPQEPALYPDLTVRENLRf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 ----YGMAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:COG1131 97 farlYGLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1915297335 174 LAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1131 177 LAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-216 |
1.20e-32 |
|
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: 121.53 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL-SGKELRKARRRIGMIFQHFNLLSSRTVFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 -----GMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:cd03258 106 pleiaGVPKAeIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1915297335 174 LAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03258 186 INRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-216 |
6.75e-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: 119.36 E-value: 6.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDAR--LFpHYKVR--- 94
Cdd:COG1122 23 SIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN----LRELRRKVGLVFQNPDdqLF-APTVEedv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 --GNLRYGMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIgralltapelllldeplAS------------- 158
Cdd:COG1122 98 afGPENLGLPREeIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI-----------------AGvlamepevlvlde 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 159 ----LDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1122 161 ptagLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
28-217 |
9.89e-32 |
|
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: 119.26 E-value: 9.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRRVGYVFQDARLFPHYKVRGNLRYGM------ 101
Cdd:cd03300 30 TLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------LPPHKRPVNTVFQNYALFPHLTVFENIAFGLrlkklp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIP 181
Cdd:cd03300 104 KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGIT 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1915297335 182 MLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:cd03300 184 FVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
26-209 |
1.17e-31 |
|
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: 118.73 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltpekRRVGYVFQDARLFPHYKVRGNLRYGM-AKS 104
Cdd:cd03293 32 FVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---------PDRGYVFQQDALLPWLTVLDNVALGLeLQG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 MAG-----QFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREIN 179
Cdd:cd03293 103 VPKaeareRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETG 182
|
170 180 190
....*....|....*....|....*....|..
gi 1915297335 180 IPMLYVSHSLDEILHLADKVMVLEN--GQVKA 209
Cdd:cd03293 183 KTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-216 |
3.07e-31 |
|
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: 118.37 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicltPEKRRVGYVFQDAR--LFPHYKVRGNL 97
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----AFRRRVQMVFQDPYasLHPRHTVDRIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 R-----YGMAKSMAgQFDKLVALLGIEP-LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:COG1124 103 AeplriHGLPDREE-RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1915297335 172 QRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1124 182 KDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-207 |
5.91e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.99 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvlndvENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMA---KS 104
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNpglKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 MAGQFDKLVAL---LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIP 181
Cdd:PRK10771 103 NAAQREKLHAIarqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLT 182
|
170 180
....*....|....*....|....*.
gi 1915297335 182 MLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK10771 183 LLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
18-211 |
9.52e-31 |
|
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: 116.11 E-value: 9.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 18 NETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlndveNGICLTPEKRRVGYVFQDARLFPHYKVRGNL 97
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ------SHTGLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMAKSM---AGQFDKLVAL---LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:TIGR01277 92 GLGLHPGLklnAEQQEKVVDAaqqVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 172 QRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-207 |
4.13e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARLFPHyKVRGNL 97
Cdd:COG4619 22 TLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA------MPPPEwrRQVAYVPQEPALWGG-TVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGM-AKSMAGQFDKLVALL---GIEP-LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:COG4619 95 PFPFqLRERKFDRERALELLerlGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLR 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1915297335 173 RLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG4619 175 EYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-209 |
4.97e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 114.37 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKR------RVGYVFQDARLFPHYKV 93
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS------LSERELarlrrrHIGFVFQFFNLLPELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldeplASLDIPRKREL 167
Cdd:COG1136 104 LENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAlvnrpkliladeptGNLDSKTGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 168 LPYLQRLAREINIPMLYVSHSLdEILHLADKVMVLENGQVKA 209
Cdd:COG1136 184 LELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
26-207 |
2.33e-29 |
|
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: 112.20 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRV---LNDVEngicLTPEKRR-VGYVFQDARLFPHYKVRGNLRYGM 101
Cdd:cd03255 32 FVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKE----LAAFRRRhIGFVFQSFNLLPDLTALENVELPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 ------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLA 175
Cdd:cd03255 108 llagvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 1915297335 176 REINIPMLYVSHSlDEILHLADKVMVLENGQV 207
Cdd:cd03255 188 KEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-224 |
3.50e-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: 117.31 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQD--ARLFPHYKVRGNL 97
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL-SRRSLRELRRRVQMVFQDpySSLNPRMTVGDII 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGM-------AKSMAGQFDKLVALLGIEP-LLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA------------ 157
Cdd:COG1123 366 AEPLrlhgllsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARA-------------LAlepkllildept 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 158 -SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgSSVMHP 224
Cdd:COG1123 433 sALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF-ANPQHP 499
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
29-212 |
5.52e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.04 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengiclTPEKRRVGYVFQDARLFPHYKVRGNLRYG--MAKSMA 106
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV------PAENRHVNTVFQSYALFPHMTVFENVAFGlrMQKTPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 107 GQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPM 182
Cdd:PRK09452 119 AEITPRVmealRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITF 198
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 183 LYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:PRK09452 199 VFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-204 |
1.01e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLEL-NFSQTLGTHCLT--LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQ---SGRIVLNGRVLNDvengicLTPE 74
Cdd:COG4136 1 MLSLeNLTITLGGRPLLapLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA------LPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 75 KRRVGYVFQDARLFPHYKVRGNLRYGMAKSMAGQFDKLVAL-----LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPEL 149
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVEqaleeAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 150 LLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILhLADKVMVLEN 204
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGN 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-216 |
1.26e-28 |
|
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: 112.16 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENGICLTPEKRRVGYVFQdarlFPHYK-----VR-----G 95
Cdd:TIGR04521 33 FVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA-KKKKKLKDLRKKVGLVFQ----FPEHQlfeetVYkdiafG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYGMAKSMAGQ-FDKLVALLGI-EPLLDRLPGGLSGGEKQRVAIgralltapelllldeplAS--------------- 158
Cdd:TIGR04521 108 PKNLGLSEEEAEErVKEALELVGLdEEYLERSPFELSGGQMRRVAI-----------------AGvlamepevlildept 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 159 --LDiPR-KRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:TIGR04521 171 agLD-PKgRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-207 |
4.54e-28 |
|
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: 108.77 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDveNGICLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DKKNINELRQKVGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 L------RYGMAKSMAGQF-DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:cd03262 97 ItlapikVKGMSKAEAEERaLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 170 YLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03262 177 VMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-217 |
4.59e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.10 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:PRK10851 24 DIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSR---LHARDRKVGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GM----------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:PRK10851 98 GLtvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-216 |
5.40e-28 |
|
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: 109.75 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARLFPHYKVRGNL 97
Cdd:COG1120 23 SLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS------LSRRElaRRIAYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMA--KSMAGQF--------DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA---------- 157
Cdd:COG1120 97 ALGRYphLGLFGRPsaedreavEEALERTGLEHLADRPVDELSGGERQRVLIARA-------------LAqeppllllde 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 158 ---SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1120 164 ptsHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-206 |
9.62e-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: 107.94 E-value: 9.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARL-FPHYKVR---- 94
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELRRKVGLVFQNPDDqFFGPTVEeeva 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 -GNLRYGMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIgralltapelllldeplAS-------------- 158
Cdd:cd03225 99 fGLENLGLPEEeIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAI-----------------AGvlamdpdillldep 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 159 ---LDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:cd03225 162 tagLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-219 |
1.09e-27 |
|
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: 108.54 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLtpeKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ-DPVEL---RRKIGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 -------LRYGMAKSMAgQFDKLVALLGIEP--LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:cd03295 96 ialvpklLKWPKEKIRE-RADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 168 LPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGS 219
Cdd:cd03295 175 QEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
31-211 |
1.14e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.27 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRRVGYVFQDARLFPHYKVRGNLRYGM--AKSMAGQ 108
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP------PAERGVGMVFQSYALYPHLSVAENMSFGLklAGAKKEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 109 FDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLY 184
Cdd:PRK11000 110 INQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIY 189
|
170 180
....*....|....*....|....*..
gi 1915297335 185 VSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:PRK11000 190 VTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-226 |
2.70e-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: 107.20 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-SEAELYRLRRRMGMLFQSGALFDSLTVFEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 ----LRYGMAKSmAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:cd03261 98 vafpLREHTRLS-EEEIREIVleklEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSvmHPWL 226
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD--DPLV 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-207 |
3.39e-27 |
|
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: 106.82 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcLTPEKRRVGYVFQDAR--LFPHYKVRGNL 97
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL-RKIRRKEIQMVFQDPMssLNPRMTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 R-----YGMAKSMA----GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:cd03257 106 AeplriHGKLSKKEarkeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03257 186 DLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-216 |
1.79e-26 |
|
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: 109.61 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTqPQSGRIvlNGRVLNDVENGICLTPEKR--RVGYVFQD--ARLFPHyK 92
Cdd:COG1123 25 VSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRI--SGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQLNPV-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 93 VRGNLRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:COG1123 101 VGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1123 181 ILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-211 |
3.55e-26 |
|
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: 102.90 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQdarlfphykvr 94
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------LSPKElaRKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 gnlrygmaksmagqfdkLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:cd03214 81 -----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 175 AREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03214 144 ARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-216 |
4.02e-26 |
|
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: 103.67 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKR-R--VGYVFQDARLFPHYKVRGN 96
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR---DITG---LPPHERaRagIGYVPEGRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVA-LLGIEPLL----DRLPGGLSGGEKQRVAIGRALLTAPELLLldeplasLDIPRK------- 164
Cdd:cd03224 96 LLLGAYARRRAKRKARLErVYELFPRLkerrKQLAGTLSGGEQQMLAIARALMSRPKLLL-------LDEPSEglapkiv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 165 RELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03224 169 EEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-216 |
6.66e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 6.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRRVGYVFQDARLFPHYKVRGNLRYG-----MAK 103
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------PADRDIAMVFQNYALYPHMSVRENMAYGlkirgMPK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 104 smaGQFDKLVA----LLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldeplasldIPRK------RELLPYL-- 171
Cdd:PRK11650 109 ---AEIEERVAeaarILELEPLLDRKPRELSGGQRQRVAMGRA------------------IVREpavflfDEPLSNLda 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 172 ----------QRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK11650 168 klrvqmrleiQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-216 |
1.90e-25 |
|
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: 103.11 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGM---- 101
Cdd:cd03294 52 IFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLevqg 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 -------AKSMagqfdKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:cd03294 132 vpraereERAA-----EALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 175 AREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03294 207 QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-211 |
2.25e-25 |
|
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: 101.68 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNG-RVLNDvengicltPE--KRRVGYVFQDARLFPHYKVRGNLRY--- 99
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKE--------PAeaRRRLGFVSDSTGLYDRLTARENLEYfag 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 --GMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaR 176
Cdd:cd03266 105 lyGLKGDELtARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-R 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1915297335 177 EINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03266 184 ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-207 |
3.56e-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: 99.78 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV-----KRRIGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYgmaksmagqfdklvallgieplldrlpgglSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAR 176
Cdd:cd03230 94 LKL------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK 143
|
170 180 190
....*....|....*....|....*....|.
gi 1915297335 177 EiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03230 144 E-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-215 |
4.02e-25 |
|
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: 106.00 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPE--KRRVGYVFQDARLFpHYKVR 94
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD------LDPAswRRQIAWVPQNPYLF-AGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 GNLRygMAKSMAG--QFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRAlltapelllldeplASLDI 161
Cdd:COG4988 429 ENLR--LGRPDASdeELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARAllrdaplllldeptAHLDA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 162 PRKRELLPYLQRLAREINIpmLYVSHSLdEILHLADKVMVLENGQVKAFGSLED 215
Cdd:COG4988 507 ETEAEILQALRRLAKGRTV--ILITHRL-ALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-226 |
7.20e-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: 100.82 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRV---LNDVEngicLTPEKRRVGYVFQDARLFPHYKVRGN----LR 98
Cdd:COG1127 33 ILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKE----LYELRRRIGMLFQGGALFDSLTVFENvafpLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 Y--GMAKSMAgqfDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:COG1127 109 EhtDLSEAEI---RELVleklELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 173 RLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSvmHPWL 226
Cdd:COG1127 186 ELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD--DPWV 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-207 |
7.76e-25 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.90 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDARLFPHYKVRGNL-- 97
Cdd:COG3638 25 EIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL-RGRALRRLRRRIGMIFQQFNLVPRLSVLTNVla 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 ----RYGMAKSMAGQF---DKLVAL-----LGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldeplASLDIPRKR 165
Cdd:COG3638 104 grlgRTSTWRSLLGLFppeDRERALealerVGLADKAYQRADQLSGGQQQRVAIARAlvqepkliladepvASLDPKTAR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG3638 184 QVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
29-272 |
9.24e-25 |
|
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: 102.57 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengiclTPEKRRVGYVFQDARLFPHYKVRGNLRYG--MAKSMA 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV------PPHLRHINMVFQSYALFPHMTVEENVAFGlkMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 107 GQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPM 182
Cdd:TIGR01187 75 AEIKPRVlealRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 183 LYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVMHPWLPKEQQSSILKVSVLEHHPHYAMTALALG-----DQH 257
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGrrcdiYTD 234
|
250
....*....|....*
gi 1915297335 258 LWVNKlEQPLQTALR 272
Cdd:TIGR01187 235 VPVEK-DQPLHVVLR 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
1.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 18 NETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQ--DARLFPHYKVR- 94
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEETVEKd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 ---GNLRYGMAKSMAGQF-DKLVALLGI-EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-ELL 168
Cdd:PRK13634 107 icfGPMNFGVSEEDAKQKaREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKGRkEMM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13634 186 EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-216 |
1.36e-24 |
|
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: 100.20 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRR---VGYVFQDARLFPHYKVRGN 96
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE---DITG---LPPHEIArlgIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQF----------------DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:cd03219 96 VMVAAQARTGSGLllararreereareraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 161 IPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03219 176 PEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-207 |
4.11e-24 |
|
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: 98.79 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEnGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMA--- 102
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLK-GKALRQLRRQIGMIFQQFNLIERLSVLENVLSGRLgrr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 ---KSMAGQF---DKLVAL-----LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:cd03256 108 stwRSLFGLFpkeEKQRALaalerVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 1915297335 172 QRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03256 188 KRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| Mop |
TIGR00638 |
molybdenum-pterin binding domain; This model describes a multigene family of molybdenum-pterin ... |
288-352 |
5.68e-24 |
|
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: 93.19 E-value: 5.68e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 288 QQTSIRNVLRAKVAQCYDDNGQVEVQLEVGGKT-LWARISPWARDELGIKPGLWLYAQIKSVSITA 352
Cdd:TIGR00638 1 LQTSARNQLKGKVVAIEDGDVNAEVDLLLGGGTkLTAVITLESVAELGLKPGKEVYAVIKAPWVIL 66
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
26-207 |
1.03e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.76 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDveNGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGM---- 101
Cdd:COG1126 29 VVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD--SKKDINKLRRKVGMVFQQFNLFPHLTVLENVTLAPikvk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 ------AKSMAgqfDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA-------------SLDIP 162
Cdd:COG1126 107 kmskaeAEERA---MELLERVGLADKADAYPAQLSGGQQQRVAIARA-------------LAmepkvmlfdeptsALDPE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1915297335 163 RKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG1126 171 LVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-216 |
1.13e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDARLFPHYKVRGNLRY-----G 100
Cdd:COG1135 33 IFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAL-SERELRAARRKIGMIFQHFNLLSSRTVAENVALpleiaG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLAS-------------LDiPRK-R 165
Cdd:COG1135 112 VPKAeIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA-------------LANnpkvllcdeatsaLD-PETtR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 166 ELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1135 178 SILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-206 |
1.79e-23 |
|
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: 95.00 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQdarlfphykvrgnlry 99
Cdd:cd00267 21 TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP----LEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 gmaksmagqfdklvallgieplldrlpggLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREiN 179
Cdd:cd00267 81 -----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-G 130
|
170 180
....*....|....*....|....*..
gi 1915297335 180 IPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:cd00267 131 RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-216 |
3.96e-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: 96.65 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKR-RVGYV--FQDARLFPHYKVRGN 96
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG------LPPHRIaRLGIArtFQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQF---------------------DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEP 155
Cdd:COG0411 100 VLVAAHARLGRGLlaallrlprarreereareraEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 156 LASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-215 |
1.79e-22 |
|
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: 98.30 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARLFpHYKVRGNL 97
Cdd:COG4987 357 TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD------LDEDDlrRRIAVVPQRPHLF-DTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RygMAKSMAGQfDKLVALL---GIEPLLDRLPGGL-----------SGGEKQRVAIGRAlltapelllldeplASLDIPR 163
Cdd:COG4987 430 R--LARPDATD-EELWAALervGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARAllrdapillldeptEGLDAAT 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 164 KRELLPYLQRLAREINIpmLYVSHSLDEiLHLADKVMVLENGQVKAFGSLED 215
Cdd:COG4987 507 EQALLADLLEALAGRTV--LLITHRLAG-LERMDRILVLEDGRIVEQGTHEE 555
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-216 |
1.87e-22 |
|
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: 94.07 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNdvENGicltPEkRRVgyVFQDARLFPHYKVRGNL-------RYG 100
Cdd:TIGR01184 15 SLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--EPG----PD-RMV--VFQNYSLLPWLTVRENIalavdrvLPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQF-DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREIN 179
Cdd:TIGR01184 86 LSKSERRAIvEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHR 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 180 IPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:TIGR01184 166 VTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-216 |
1.94e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.39 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengicltpeKRRVGYVFQDA---RLFP------- 89
Cdd:COG1121 28 TIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---------RRRIGYVPQRAevdWDFPitvrdvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 90 ---HYKVRGNLRyGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:COG1121 99 lmgRYGRRGLFR-RPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLeNGQVKAFGSLEDV 216
Cdd:COG1121 178 LYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-212 |
4.50e-22 |
|
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: 92.95 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlNDVENgicLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTD---RKAARQSLGYCPQFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LR-YGMAKSMAGQFDKLVAL-----LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:cd03263 96 LRfYARLKGLPKSEIKEEVElllrvLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 171 LQRLAReiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:cd03263 176 ILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-231 |
5.61e-22 |
|
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: 97.21 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltPEKRR--VGYVFQDARLFpHYKVRGNL 97
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID------PASLRrqIGVVLQDVFLF-SGTIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RygMAKSMAGqFDKLVA---LLGIEPLLDRLPGG-----------LSGGEKQRVAIGRAlltapelllldeplASLDIPR 163
Cdd:COG2274 570 T--LGDPDAT-DEEIIEaarLAGLHDFIEALPMGydtvvgeggsnLSGGQRQRLAIARAllrnprilildeatSALDAET 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 164 KRELLPYLQRLAReiNIPMLYVSHSLdEILHLADKVMVLENGQVKAFGSLEDVWGSSVMHPWLPKEQQ 231
Cdd:COG2274 647 EAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-216 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.19 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvLNDVENGICLTPEKRRVGYVFQdarlFPHYK-----VRGNLRYG-- 100
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSDIRKKVGLVFQ----YPEYQlfeetIEKDIAFGpi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 ------------MAKSMagqfdKLVAlLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-EL 167
Cdd:PRK13637 111 nlglseeeienrVKRAM-----NIVG-LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD-PKGRdEI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1915297335 168 LPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
31-142 |
1.14e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK-----RRVGYVFQDARLFPHYKVRGNLRYGM---- 101
Cdd:COG2884 35 GPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR------LKRREipylrRRIGVVFQDFRLLPDRTVYENVALPLrvtg 108
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1915297335 102 --AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:COG2884 109 ksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
25-207 |
1.36e-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: 91.98 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 25 GITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMA-- 102
Cdd:TIGR02315 29 EFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK-LRGKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRLgy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 ----KSMAGQF---DKLVAL-----LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:TIGR02315 108 kptwRSLLGRFseeDKERALsalerVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDY 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:TIGR02315 188 LKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-211 |
1.40e-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: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPAsGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03264 19 VSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-----RRRIGYLPQEFGVYPNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRY-----GMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP---RKREL 167
Cdd:cd03264 93 LDYiawlkGIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEeriRFRNL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1915297335 168 lpyLQRLAREINIpmLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03264 173 ---LSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-212 |
7.48e-21 |
|
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: 89.55 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGL-----TQPQSGRIVLNGRVLNDVENGICLTpeKRRVGYVFQDARLFPhYKVRG 95
Cdd:cd03260 23 IPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLEL--RRRVGMVFQKPNPFP-GSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYG---MAKSMAGQFDKLV--ALLGI---EPLLDRL-PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:cd03260 100 NVAYGlrlHGIKLKEELDERVeeALRKAalwDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 167 LLPYLQRLAREINIPMlyVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:cd03260 180 IEELIAELKKEYTIVI--VTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-207 |
7.82e-21 |
|
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: 89.60 E-value: 7.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFpHYKVRGN 96
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT----LDSLRRAIGVVPQDTVLF-NDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:cd03253 95 IRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQV 207
Cdd:cd03253 175 EIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
29-258 |
1.35e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.02 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGV---SGAGKTSLINAISGLTQPQSGRIVLNGR---VLNDVEngicLTPEKRRVGYVFQDARLFPHYKVRGNLRY--- 99
Cdd:PRK11153 33 IFGVigaSGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKE----LRKARRQIGMIFQHFNLLSSRTVFDNVALple 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 --GMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLAS-------------LDIPR 163
Cdd:PRK11153 109 laGTPKAeIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA-------------LASnpkvllcdeatsaLDPAT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 164 KRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgssvMHPWLPKEQQ--SSILKVSVLE 241
Cdd:PRK11153 176 TRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF----SHPKHPLTREfiQSTLHLDLPE 251
|
250
....*....|....*..
gi 1915297335 242 HHPHYAMTALALGDQHL 258
Cdd:PRK11153 252 DYLARLQAEPTTGSGPL 268
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-217 |
1.44e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENgicLTPEKRRVGYVFQ--DARLFPHyKVR 94
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-EN---IREVRKFVGLVFQnpDDQIFSP-TVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 GNLRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:PRK13652 98 QDIAFGPinlgldEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-216 |
1.47e-20 |
|
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: 88.89 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND------VENGICLTPEKRRVgyvfqdarlFPHYKV 93
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphriARLGIGYVPEGRRI---------FPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLRYGM-----AKSMAGQFDKLVAL---LgiEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLldeplasLDIPRK- 164
Cdd:COG0410 96 EENLLLGAyarrdRAEVRADLERVYELfprL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL-------LDEPSLg 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 165 ------RELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG0410 167 laplivEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-217 |
1.67e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 2 LEL-NFSQTLGTHCL--TLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDV-ENGIcltpEKRR 77
Cdd:PRK11432 7 VVLkNITKRFGSNTVidNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVtHRSI----QQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 78 VGYVFQDARLFPHYKVRGNLRYGMakSMAGQFD-----------KLVALLGIEpllDRLPGGLSGGEKQRVAIGRALLTA 146
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGL--KMLGVPKeerkqrvkealELVDLAGFE---DRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 147 PELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-211 |
1.70e-20 |
|
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: 88.36 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicltpEKRRVGYVFQDA---RLFPhYKV 93
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRsidRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 R-----GNLRYGMAKSMAGQFDK---LVAL--LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:cd03235 88 RdvvlmGLYGHKGLFRRLSKADKakvDEALerVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 164 KRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLeNGQVKAFG 211
Cdd:cd03235 168 QEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-216 |
4.44e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.53 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN-----DVengicltpeKRRVGYVFQDA-RLFPHYKVRGNLRYGM 101
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwDV---------RRQVGMVFQNPdNQFVGATVQDDVAFGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKS------MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKR-ELLPYLQRL 174
Cdd:PRK13635 108 ENIgvpreeMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD-PRGRrEVLETVRQL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 175 AREINIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13635 187 KEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-216 |
6.00e-20 |
|
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: 87.87 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENgicLTPEKRRVGYVFQD------ARLfphykVRGNLRYG 100
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN---LWEIRKKVGMVFQNpdnqfvGAT-----VEDDVAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 M------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIgralltapelllldeplAS---------------- 158
Cdd:TIGR04520 103 LenlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI-----------------AGvlamrpdiiildeats 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 159 -LDiPR-KRELLPYLQRLAREINIPMLYVSHSLDEILhLADKVMVLENGQVKAFGSLEDV 216
Cdd:TIGR04520 166 mLD-PKgRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-206 |
8.61e-20 |
|
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: 85.13 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRR--VGYVFQDARLFpHYKVR 94
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD------LDLESLRknIAYVPQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 GNLrygmaksmagqfdklvallgieplldrlpggLSGGEKQRVAIGRAlltapelllldeplASLDIPRKRELLPYLQRL 174
Cdd:cd03228 94 ENI-------------------------------LSGGQRQRIAIARAllrdppilildeatSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 1915297335 175 AREINIpmLYVSHSLDEILHlADKVMVLENGQ 206
Cdd:cd03228 143 AKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-208 |
1.06e-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: 85.77 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 4 LNFSQTLGTHCL-TLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengICLTPEKRRVGYVF 82
Cdd:cd03226 5 ISFSYKKGTEILdDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-------IKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 83 QDAR--LFPHyKVRGNLRYGMAKSMAGQFD--KLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:cd03226 78 QDVDyqLFTD-SVREELLLGLKELDAGNEQaeTVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 159 LDIPRKRELLPYLQRLAREINIpMLYVSHSLDEILHLADKVMVLENGQVK 208
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-212 |
1.46e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.84 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARLFpHYKVRGNL 97
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD------LTLESlrRQIGVVPQDTFLF-SGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMAK-SMAgQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRAlltapelllldeplASLDIPRKR 165
Cdd:COG1132 435 RYGRPDaTDE-EVEEAAKAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIARAllkdppilildeatSALDTETEA 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 166 ELLPYLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQVKAFGS 212
Cdd:COG1132 514 LIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.75e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 3 ELNFSQTLGTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicLTPEKRRVGYV 81
Cdd:PRK13636 10 ELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG--LMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 82 FQ--DARLFPHyKVRGNLRYGMA------KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:PRK13636 88 FQdpDNQLFSA-SVYQDVSFGAVnlklpeDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 154 EPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVM 222
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-212 |
2.49e-19 |
|
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: 85.35 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 4 LNFSQTLGTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengicltPEK---RRVG 79
Cdd:cd03254 8 VNFSYDEKKPVLKdINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-------SRKslrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 80 YVFQDARLFPHyKVRGNLRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPE 148
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 149 LLLLDEPLASLDiPRKRELlpyLQRLAREI--NIPMLYVSHSLDEILHlADKVMVLENGQVKAFGS 212
Cdd:cd03254 160 ILILDEATSNID-TETEKL---IQEALEKLmkGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-217 |
6.99e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengiclTPEKRRVGYVFQDARLFPHYKVRGNLRYGMAK-- 103
Cdd:PRK11607 47 IFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV------PPYQRPINMMFQSYALFPHMTVEQNIAFGLKQdk 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 104 ----SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP-RKRELLPYLQRLAReI 178
Cdd:PRK11607 121 lpkaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILER-V 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 179 NIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK11607 200 GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-215 |
7.73e-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: 83.96 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGR-VLNDVENgicltpEKRRVGYVFQDARLFPHYKVRG 95
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPRE------VRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLR-----YGMAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:cd03265 93 NLYiharlYGVPGAERRErIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLED 215
Cdd:cd03265 173 YIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-207 |
8.28e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN-----DVENGICLtpeKRRVGYVFQDARLFPHY 91
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpSDKAIREL---RRNVGMVFQQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNL------RYGMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:PRK11124 98 TVQQNLieapcrVLGLSKDQAlARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1915297335 165 RELLPYLQRLArEINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11124 178 AQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-202 |
8.80e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNdvengiclTPEKRRvGYVFQDARLFPHYKVRGN 96
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--------GPGADR-GVVFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMakSMAG--------QFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD-IPRKR-- 165
Cdd:COG4525 97 VAFGL--RLRGvpkaerraRAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDaLTREQmq 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 166 ELlpyLQRLAREINIPMLYVSHSLDEILHLADKVMVL 202
Cdd:COG4525 175 EL---LLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-215 |
9.97e-19 |
|
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: 83.82 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFpHYKVRGN 96
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT----LASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:cd03251 96 IAYGRPGATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 166 ELLPYLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLED 215
Cdd:cd03251 176 LVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-209 |
1.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENgiclTPEKRR-VGYVFQDA-RLFPHYKVRGNLRYGMA--- 102
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-EN----VWDIRHkIGMVFQNPdNQFVGATVEDDVAFGLEnkg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 ---KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREIN 179
Cdd:PRK13650 112 iphEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQ 191
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 180 IPMLYVSHSLDEILhLADKVMVLENGQVKA 209
Cdd:PRK13650 192 MTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-206 |
1.06e-18 |
|
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: 83.45 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLEL-NFSQTLGTHCLTLNE---TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDV-ENGICLTpeK 75
Cdd:TIGR02673 1 MIEFhNVSKAYPGGVAALHDvslHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrGRQLPLL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 76 RRVGYVFQDARLFPHYKVRGN------LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPEL 149
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENvalpleVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 150 LLLDEPLASLDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-214 |
3.41e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN-----DVENGICLtpeKRRVGYVFQDARLFPHY 91
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpSEKAIRLL---RQKVGMVFQQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNLR------YGMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:COG4161 98 TVMENLIeapckvLGLSKEQArEKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 165 RELLPYLQRLArEINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLE 214
Cdd:COG4161 178 AQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-216 |
3.83e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMakSM 105
Cdd:PRK10070 56 IFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGM--EL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 106 AG------QFDKLVAL--LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK10070 134 AGinaeerREKALDALrqVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK10070 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-211 |
4.14e-18 |
|
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: 81.87 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNG---RVLNDVEngicltpEKRRVGYVFQDARLFpHYKVRGNLRYGMAKS 104
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPAD-------LRRNIGYVPQDVTLF-YGTLRDNITLGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 MAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:cd03245 106 DDERILRAAELAGVTDFVNKHPNGldlqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQ 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 174 LAREINipMLYVSHSLdEILHLADKVMVLENGQVKAFG 211
Cdd:cd03245 186 LLGDKT--LIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-202 |
5.20e-18 |
|
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: 85.03 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFPHyKVRGN 96
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:TIGR02857 416 IRLARPDASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 166 ELLPYLQRLAReiNIPMLYVSHSLdEILHLADKVMVL 202
Cdd:TIGR02857 496 EVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-207 |
5.65e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLtpekrrvgyVFQDARLFPHYKVRGNLRYG 100
Cdd:PRK11247 35 IPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL---------MFQDARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINI 180
Cdd:PRK11247 106 LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGF 185
|
170 180
....*....|....*....|....*..
gi 1915297335 181 PMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11247 186 TVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-216 |
7.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENgicLTPEKRRVGYVFQDA-RLFPHYKVRGNLRYGMA--- 102
Cdd:PRK13632 38 VAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-EN---LKEIRKKIGIIFQNPdNQFIGATVEDDIAFGLEnkk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 ---KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREIN 179
Cdd:PRK13632 114 vppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRK 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 180 IPMLYVSHSLDEILhLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13632 194 KTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-207 |
1.31e-17 |
|
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: 79.01 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNdvengiCLTP---EKRRVGYVFQdarlfphykvrgnlrygma 102
Cdd:cd03216 28 VHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------FASPrdaRRAGIAMVYQ------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 ksmagqfdklvallgieplldrlpggLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREiNIPM 182
Cdd:cd03216 83 --------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAV 135
|
170 180
....*....|....*....|....*
gi 1915297335 183 LYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03216 136 IFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-142 |
1.49e-17 |
|
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: 80.14 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicLTPEKRR-VGYVFQDARLFPHYKVRG 95
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR--AIPYLRRkIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 96 NLRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:cd03292 98 NVAFALevtgvpPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-216 |
1.72e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.52 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 5 NFSQTLGTHCLTLNetLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTpeKRRVGYVFQD 84
Cdd:PRK09493 10 HFGPTQVLHNIDLN--IDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI--RQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 ARLFPHYKVRGNLRYG------MAKSMAGQFDK-LVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLA 157
Cdd:PRK09493 86 FYLFPHLTALENVMFGplrvrgASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 158 SLDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-217 |
1.81e-17 |
|
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: 80.28 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvlNDVENgicLTPEKRR---VGYVFQDARLFPHYKVRGNLR---Y 99
Cdd:cd03218 28 IVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITK---LPMHKRArlgIGYLPQEASIFRKLTVEENILavlE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKSMAGQFDKLVALL---GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQRLAR 176
Cdd:cd03218 102 IRGLSKKEREEKLEELLeefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD-PIAVQDIQKIIKILK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 177 EINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:cd03218 181 DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
17-202 |
2.13e-17 |
|
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: 79.58 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:TIGR03608 17 LNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETVEEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDK----LVAL--LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:TIGR03608 97 LDLGLKYKKLSKKEKrekkKEALekVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDL 176
|
170 180 190
....*....|....*....|....*....|..
gi 1915297335 171 LQRLAREiNIPMLYVSHSLdEILHLADKVMVL 202
Cdd:TIGR03608 177 LLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-207 |
2.29e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.97 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTqPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFpHYKVRGN 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD----PESWRKHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLP-----------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAREINIPMlyVSHSLDEiLHLADKVMVLENGQV 207
Cdd:PRK11174 523 LVMQALNAASRRQTTLM--VTHQLED-LAQWDQIWVMQDGQI 561
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-207 |
4.16e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.79 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIvlngRVLN-DVENGICLTPEKRR-------VGYVFQDARLFPHYKVRGNL 97
Cdd:PRK11264 31 VVAIIGPSGSGKTTLLRCINLLEQPEAGTI----RVGDiTIDTARSLSQQKGLirqlrqhVGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYG------MAKSMAGQFDK-LVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:PRK11264 107 IEGpvivkgEPKEEATARAReLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915297335 171 LQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11264 187 IRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-215 |
4.53e-17 |
|
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: 82.07 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 22 PASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengICLTPEKRRVGYVFQDARLFPHyKVRGNLRYG- 100
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD----YTLASLRRQVALVSQDVVLFND-TIANNIAYGr 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:TIGR02203 431 TEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 170 YLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLED 215
Cdd:TIGR02203 511 ALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-211 |
9.34e-17 |
|
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: 77.59 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQ--SGRIVLNGRVLNDVEngicltpEKRRVGYVFQDARLFPHYKVRGNLRYgmak 103
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS-------FRKIIGYVPQDDILHPTLTVRETLMF---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 104 smagqfdklVALLgieplldRlpgGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREiNIPML 183
Cdd:cd03213 106 ---------AAKL-------R---GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTII 165
|
170 180
....*....|....*....|....*....
gi 1915297335 184 YVSHSL-DEILHLADKVMVLENGQVKAFG 211
Cdd:cd03213 166 CSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-202 |
1.37e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRR--VGYVFQDARLFPHyKVRGNL 97
Cdd:PRK10247 29 SLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST------LKPEIYRqqVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RY-----GMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:PRK10247 102 IFpwqirNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIH 181
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 173 RLAREINIPMLYVSHSLDEILHlADKVMVL 202
Cdd:PRK10247 182 RYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-207 |
1.64e-16 |
|
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: 76.10 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFPHyKVRGN 96
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD----PNELGDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LrygmaksmagqfdklvallgieplldrlpggLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaR 176
Cdd:cd03246 96 I-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-K 143
|
170 180 190
....*....|....*....|....*....|.
gi 1915297335 177 EINIPMLYVSHSLdEILHLADKVMVLENGQV 207
Cdd:cd03246 144 AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-228 |
2.07e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLNETLPAsgITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicLTPEKRRVGYVFQDARLFPHYK-- 92
Cdd:PRK13638 20 LNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRG--LLALRQQVATVFQDPEQQIFYTdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 93 ---VRGNLR-YGMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK13638 96 dsdIAFSLRnLGVPEAeITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 168 LPYLQRLAREINiPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWG-------SSVMHPWLPK 228
Cdd:PRK13638 176 IAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFActeameqAGLTQPWLVK 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-224 |
2.21e-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: 78.56 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLN--ETLpasgitAIFGVSGAGKTSLINAISGLTQPQ---SGRIVLNGRVLNDvengicLTPEK------RRVGYVFQ 83
Cdd:COG0444 26 FDVRrgETL------GLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLK------LSEKElrkirgREIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 84 D--ARLFPHYKVrGN-----LRYGMAKSMAGQFDKLVALL---GIEP---LLDRLPGGLSGGEKQRVAIGRAlltapell 150
Cdd:COG0444 94 DpmTSLNPVMTV-GDqiaepLRIHGGLSKAEARERAIELLervGLPDperRLDRYPHELSGGMRQRVMIARA-------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 151 lldepLAS-------------LDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:COG0444 165 -----LALepklliadepttaLDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
....*..
gi 1915297335 218 GSSvMHP 224
Cdd:COG0444 240 ENP-RHP 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-207 |
2.88e-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: 77.54 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRR-----VGYVFQDA------RLFPHYKVRGN 96
Cdd:TIGR02769 41 GLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ------LDRKQRRafrrdVQLVFQDSpsavnpRMTVRQIIGEP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALL---GIEP-LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:TIGR02769 115 LRHLTSLDESEQKARIAELLdmvGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLR 194
|
170 180 190
....*....|....*....|....*....|....*
gi 1915297335 173 RLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:TIGR02769 195 KLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-177 |
2.98e-16 |
|
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: 76.36 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGN 96
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-----RRRLAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LR-----YGMAKSMAgQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRAlltapelllldepLASLDIPRKRELLPYL 171
Cdd:COG4133 96 LRfwaalYGLRADRE-AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLllspaplwlldepFTALDAAGVALLAELI 174
|
....*.
gi 1915297335 172 QRLARE 177
Cdd:COG4133 175 AAHLAR 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
28-142 |
3.14e-16 |
|
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: 76.70 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKR------RVGYVFQDARLFPHYKVRGN----- 96
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA------LDEDARarlrarHVGFVFQSFQLLPTLTALENvmlpl 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 -LRygmakSMAGQFDKLVALL---GIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:COG4181 116 eLA-----GRRDARARARALLervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-207 |
3.99e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDA--RLFPHYKVRG----NLRYGM 101
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL-NRAQRKAFRRDIQMVFQDSisAVNPRKTVREiirePLRHLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKSMAGQFDKLVALL---GIEP-LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK10419 121 SLDKAERLARASEMLravDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQ 200
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK10419 201 FGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-224 |
4.89e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARL-FPhYKVRGN 96
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD------WSPAElaRRRAVLPQHSSLsFP-FTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMA--KSMAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEP------LASLDIPRK 164
Cdd:PRK13548 97 VAMGRAphGLSRAEDDALVaaalAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPPRWllldepTSALDLAHQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 165 RELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGS---------LEDVWGSSV---MHP 224
Cdd:PRK13548 177 HHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpaevltpetLRRVYGADVlvqPHP 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-205 |
6.00e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicltPEKRRvGYVFQDARLFPHYKVRGN 96
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--------PGAER-GVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMA---------KSMAGQFDKLVALLGIEpllDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK11248 91 VAFGLQlagvekmqrLEIAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 168 LPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENG 205
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-207 |
6.04e-16 |
|
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: 74.78 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND------VENGICLTPEKRRvgyvfqDARLFPHYKVRGNLRy 99
Cdd:cd03215 28 IVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrsprdaIRAGIAYVPEDRK------REGLVLDLSVAENIA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 gmaksmagqfdklvallgieplldrLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREiN 179
Cdd:cd03215 101 -------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-G 154
|
170 180
....*....|....*....|....*...
gi 1915297335 180 IPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03215 155 KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-216 |
7.78e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.31 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQDARL-FPhYKVR-- 94
Cdd:COG4559 23 TLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA------WSPWElaRRRAVLPQHSSLaFP-FTVEev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 ---GNLRYGmakSMAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEP-------LASLD 160
Cdd:COG4559 96 valGRAPHG---SSAAQDRQIVrealALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGPRwlfldepTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 161 IPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4559 173 LAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-216 |
7.86e-16 |
|
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: 75.89 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSG-RIVLNGRVLNDVEngiclTPE-KRRVGYVfqDARLfpHYKVRGNLR------ 98
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED-----VWElRKRIGLV--SPAL--QLRFPRDETvldvvl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 ---YGMA-------KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:COG1119 103 sgfFDSIglyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1119 183 ALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-207 |
8.14e-16 |
|
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: 75.39 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQ---SGRIVLNGRVLNdvengicltPE--KRRVGYVFQDARLFPHY 91
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---------PDqfQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNLRY-----GMAKSMAGQFDKLVA-----LLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:cd03234 97 TVRETLTYtailrLPRKSSDAIRKKRVEdvllrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 162 PRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-231 |
8.16e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 23 ASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDV--ENGICLTPEKR-------RVGYVFQDARLFPHYKV 93
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdKDGQLKVADKNqlrllrtRLTMVFQHFNLWSHMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLR------YGMAKSMAGQ-FDKLVALLGI-EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK10619 110 LENVMeapiqvLGLSKQEARErAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 166 ELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSsvmhPWLPKEQQ 231
Cdd:PRK10619 190 EVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN----PQSPRLQQ 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-212 |
1.35e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.43 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRI----VLNGRVLNDVENGICLTPEK--------RRVGYVFQdarlFPHYKV 93
Cdd:PRK13631 54 IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKiknfkelrRRVSMVFQ----FPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 R----------GNLRYGMAKSMAGQFDKL-VALLGI-EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13631 130 FkdtiekdimfGPVALGVKKSEAKKLAKFyLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 162 PRKRELLPyLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:PRK13631 210 KGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-207 |
1.37e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVL-----ND-VENGIcltpekrrvGYVFQDARLFPHYKVRGNLRY 99
Cdd:COG3845 33 IHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRDaIALGI---------GMVHQHFMLVPNLTVAENIVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKSMAGQFD------KLVAL-----LGIEPllDRLPGGLSGGEKQRVAIGRAlltapelllldeplasL----DI--- 161
Cdd:COG3845 104 GLEPTKGGRLDrkaaraRIRELserygLDVDP--DAKVEDLSVGEQQRVEILKA----------------LyrgaRIlil 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 162 --------PR-KRELLPYLQRLARE---InipmLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG3845 166 deptavltPQeADELFEILRRLAAEgksI----IFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-211 |
2.03e-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: 74.24 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengicltpEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:cd03269 22 SVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--------ARNRIGYLPEERGLYPKMKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 -----GMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR 173
Cdd:cd03269 94 laqlkGLKKEEArRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD-PVNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 174 LAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03269 173 ELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-142 |
2.50e-15 |
|
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: 77.02 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENgiclTPEKRRVGYVFQDARLFpHYKVRGNLRY 99
Cdd:TIGR02868 357 DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ----DEVRRRVSVCAQDAHLF-DTTVRENLRL 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 100 GMAKSMAGQFDKLVALLGIEPLLDRLPGGL-----------SGGEKQRVAIGRA 142
Cdd:TIGR02868 432 ARPDATDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARA 485
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-217 |
3.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLNE---TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENgicLTPEKRRVGYVFQDA-RLFPH 90
Cdd:PRK13648 23 FTLKDvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DN---FEKLRKHIGIVFQNPdNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMAKSMAgQFDKLV-----ALLGIEpLLDRL---PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:PRK13648 99 SIVKYDVAFGLENHAV-PYDEMHrrvseALKQVD-MLERAdyePNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 163 RKRELLPYLQRLAREINIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-207 |
3.50e-15 |
|
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: 73.91 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVF-QDARLFPHYKVRG 95
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-----LRRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLR-----YGMAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:cd03267 115 SFYllaaiYDLPPARFKKrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
26-219 |
5.01e-15 |
|
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: 73.46 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlndvenGICLTPEKRR----VGYVFQDARLFPHYKVRGNL---- 97
Cdd:TIGR04406 29 IVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ-------DITHLPMHERarlgIGYLPQEASIFRKLTVEENImavl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 --RYGMAKsmAGQFDKLVALL---GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQ 172
Cdd:TIGR04406 102 eiRKDLDR--AEREERLEALLeefQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD-PIAVGDIKKII 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 173 RLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGS 219
Cdd:TIGR04406 179 KHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-216 |
5.31e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTP---EKRRVGYVFQDARLFPHYKVRGNL----- 97
Cdd:COG1129 32 VHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF------RSPrdaQAAGIAIIHQELNLVPNLSVAENIflgre 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 --RYGM--AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTapelllldePLASLDIPRKRELLPYLQR 173
Cdd:COG1129 106 prRGGLidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRdarvlildePTASLTEREVERLFRIIRR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1915297335 174 LAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1129 186 LKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
5.81e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK-RRVG--YVFQDARLFPHYKVRGN 96
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR------LTPAKaHQLGiyLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQ--FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK15439 107 ILFGLPKRQASMqkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 175 aREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLED 215
Cdd:PRK15439 187 -LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-216 |
5.84e-15 |
|
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: 75.61 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRivLNGRVLNDVENGICLTPE-----KRRVGYVFQDARLFPHYKVRGNLRYG 100
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGE--VNVRVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYPHRTVLDNLTEA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQFDKLVALLGI----------EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:TIGR03269 390 IGLELPDELARMKAVITLkmvgfdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:TIGR03269 470 ILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-217 |
7.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQ--DARLFPHYKVR----GNLRYG 100
Cdd:PRK13643 35 TALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEETVLKdvafGPQNFG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQF--DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaREI 178
Cdd:PRK13643 115 IPKEKAEKIaaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQS 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 179 NIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13643 194 GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-217 |
7.81e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQ--DARLFPHYKVR----GNLRYG 100
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEETVLKdvafGPQNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQF--DKLvALLGI-EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLaRE 177
Cdd:PRK13649 116 VSQEEAEALarEKL-ALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13649 194 SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-216 |
9.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.48 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 11 GTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENgicLTPEKRRVGYVFQDARL-F 88
Cdd:PRK13644 14 GTPALEnINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK---LQGIRKLVGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 89 PHYKVRGNLRYGMAK------SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:PRK13644 91 VGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 163 RKRELLPYLQRLAREiNIPMLYVSHSLDEiLHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-230 |
1.04e-14 |
|
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: 72.52 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFpHYKVRGNL---RYGM- 101
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD----PAWLRRQVGVVLQENVLF-NRSIRDNIalaDPGMs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 ------AKSMAGQFDKLVAL-LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:cd03252 105 mervieAAKLAGAHDFISELpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 175 AReiNIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDVWGSSVMHPWLPKEQ 230
Cdd:cd03252 185 CA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-216 |
1.06e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMAKSM 105
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---DVEA-LSARAASRRVASVPQDTSLSFEFDVRQVVEMGRTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 106 aGQFDKL-----------VALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK09536 107 -SRFDTWtetdraaveraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 175 AREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK09536 186 VDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-212 |
1.70e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGR-IVLNGRVLNDVENGICLTPEKRRVGYVFQdarlFPHYK-----V 93
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANLKKIKEVKRLRKEIGLVFQ----FPEYQlfqetI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLRYG---MAKSMAGQFDKLVALLGI----EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK13645 109 EKDIAFGpvnLGENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 167 LLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-216 |
1.95e-14 |
|
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: 74.01 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEK--RRVGYVFQDARLFPHyKVRGNL 97
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQ---WDREElgRHIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 -RYGMAKSmagqfDKLVA---LLGIEPLLDRLPGG-----------LSGGEKQRVAIGRAlltapelllldeplASLDIP 162
Cdd:COG4618 427 aRFGDADP-----EKVVAaakLAGVHEMILRLPDGydtrigeggarLSGGQRQRIGLARAlygdprlvvldepnSNLDDE 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 163 RKRELLPYLQRLaREINIPMLYVSHSLdEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4618 502 GEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-207 |
6.10e-14 |
|
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: 70.19 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpeKRRVGYVFQDARLFPHyKVRGNLRY 99
Cdd:cd03248 36 TLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMA------------KSMAGQFDKLVALlGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:cd03248 111 GLQscsfecvkeaaqKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 168 LPYLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQV 207
Cdd:cd03248 190 QQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
9.43e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVL---NDVENgICLTPEKRRVGYVFQDARLFPHYKVRGNL 97
Cdd:PRK14246 33 IPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQ-IDAIKLRKEVGMVFQQPNPFPHLSIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMA-------KSMAGQFDKLVALLGI-EPLLDRL---PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK14246 112 AYPLKshgikekREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 167 LLPYLQRLAREINIpmLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGS 219
Cdd:PRK14246 192 IEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-228 |
1.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQ--DARLFPHYKVR----GNLRYGM 101
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFENTVLKdvefGPKNFGF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 ----AKSMAGQFDKLVALlgIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK13641 117 sedeAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 178 INIPMLyVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSvmhPWLPK 228
Cdd:PRK13641 195 GHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK---EWLKK 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-222 |
1.41e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 13 HCLTLneTLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpeKRRVGYVFQDARLFPHYK 92
Cdd:PRK10575 28 HPLSL--TFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 93 VR-----------GNL-RYGMAKSMagQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK10575 102 VRelvaigrypwhGALgRFGAADRE--KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 161 IPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVM 222
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-224 |
1.91e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.15 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 19 ETLpasgitAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQD--ARLFPHYKVRGN 96
Cdd:COG4608 45 ETL------GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL-SGRELRPLRRRMQMVFQDpyASLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMA----KSMAGQFDKLVALL---GIEP-LLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA----------- 157
Cdd:COG4608 118 IAEPLRihglASKAERRERVAELLelvGLRPeHADRYPHEFSGGQRQRIGIARA-------------LAlnpklivcdep 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 158 --SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSvMHP 224
Cdd:COG4608 185 vsALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP-LHP 252
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-207 |
4.11e-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: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlNDVENGICLtpekRRVGYVFQDARLFPHYKVRGN 96
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEAL----RRIGALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LR-----YGMAKSMAgqfDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:cd03268 93 LRllarlLGIRKKRI---DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1915297335 172 QRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:cd03268 170 LSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-199 |
4.12e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGN-----LRYGMA 102
Cdd:PRK11629 39 AIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENvamplLIGKKK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 KSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIP 181
Cdd:PRK11629 119 PAEINSrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTA 198
|
170
....*....|....*...
gi 1915297335 182 MLYVSHSldeiLHLADKV 199
Cdd:PRK11629 199 FLVVTHD----LQLAKRM 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-209 |
4.28e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN-----D-VENGICLTPEKRRVGYVFQD---------ARLfPH 90
Cdd:COG1129 280 ILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDaIRAGIAYVPEDRKGEGLVLDlsirenitlASL-DR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMAKSMAgqfDKLVALLGIE-PLLDRLPGGLSGGEKQRVAIGRALLTAPELLLldeplasLDIP-R----- 163
Cdd:COG1129 359 LSRGGLLDRRRERALA---EEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI-------LDEPtRgidvg 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 164 -KRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKA 209
Cdd:COG1129 429 aKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-212 |
4.47e-13 |
|
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: 70.15 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 3 ELNFSQTLGTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpeKRRVGYV 81
Cdd:TIGR01193 478 DVSYSYGYGSNILSdISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 82 FQDARLFPHyKVRGNLRYGmAKSMAGQ--FDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPE 148
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLG-AKENVSQdeIWAACEIAEIKDDIENMPLGyqtelseegssISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 149 LLLLDEPLASLDIPRKRELLPYLQRLAREINIpmlYVSHSLdEILHLADKVMVLENGQVKAFGS 212
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRL-SVAKQSDKIIVLDHGKIIEQGS 691
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-142 |
1.74e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 22 PASGItAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGN----- 96
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENvelpa 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1915297335 97 -LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:PRK10584 114 lLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
|
| TOBE |
pfam03459 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
292-350 |
1.83e-12 |
|
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: 61.53 E-value: 1.83e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 292 IRNVLRAKVAQCYDDNGQVEVQLEV-GGKTLWARISPWARDELGIKPGLWLYAQIKSVSI 350
Cdd:pfam03459 1 ARNQLPGTVTVIEPLGSEVEVRVDLgGGLTLTARITRDSAEELGLAPGDEVWALIKATKV 60
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-219 |
2.01e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpEKRRVGYVFQDA--RLFPHYKVRG-- 95
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY----RSQRIRMIFQDPstSLNPRQRISQil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 --NLRYGMAKSMAGQFDKLVALLGIEPLL----DRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:PRK15112 111 dfPLRLNTDLEPEQREKQIIETLRQVGLLpdhaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGS 219
Cdd:PRK15112 191 LMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-222 |
2.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSgrivlNGRVLNDVEnGICLTPE-----KRRVGYVFQDA-RLFPH 90
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKITVD-GITLTAKtvwdiREKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMA------KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:PRK13640 100 ATVGDDVAFGLEnravprPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 165 RELLPYLQRLAREINIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDVWGSSVM 222
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
2.97e-12 |
|
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: 67.40 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLN--ETLpasgitAIFGVSGAGKTSLINAISGLtQPQSGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQD--ARLFPH 90
Cdd:COG4172 307 LTLRrgETL------GLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGL-SRRALRPLRRRMQVVFQDpfGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMA-----KSMAGQFDKLVALL---GIEP-LLDRLPGGLSGGEKQRVAIGRAlltapelllldepLA---- 157
Cdd:COG4172 379 MTVGQIIAEGLRvhgpgLSAAERRARVAEALeevGLDPaARHRYPHEFSGGQRQRIAIARA-------------LIlepk 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 158 ---------SLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4172 446 llvldeptsALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-216 |
4.17e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.49 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgiclTPEK---RRVGYVFQD----ARL----- 87
Cdd:COG4604 23 TIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL---DVAT----TPSRelaKRLAILRQEnhinSRLtvrel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 -----FPHYKvrGNL----RYGMAKSMAgqfdklvaLLGIEPLLDRLPGGLSGGEKQRVAIgralltapelllldeplAS 158
Cdd:COG4604 96 vafgrFPYSK--GRLtaedREIIDEAIA--------YLDLEDLADRYLDELSGGQRQRAFIamvlaqdtdyvlldeplNN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 159 LDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4604 166 LDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-207 |
4.44e-12 |
|
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: 64.87 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengICLTPEKRRVGYVFQDARLFPHyKVRGN 96
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD----LNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:cd03249 97 IRYGKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAREINIpmLYVSHSLDEILHlADKVMVLENGQV 207
Cdd:cd03249 177 LVQEALDRAMKGRTT--IVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-207 |
5.00e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQ--DARLFPHYKVR----GNLRYGM 101
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVEReiifGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 ----AKSMAgqFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK13646 117 nldeVKNYA--HRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTD 194
|
170 180 190
....*....|....*....|....*....|
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK13646 195 ENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-215 |
5.05e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.91 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvlNDVeNGICLTPEKRRVGYVFQDARLFpHYKVRGNLRYGmaKSMAG 107
Cdd:PRK13657 365 AIVGPTGAGKSTLINLLQRVFDPQSGRILIDG---TDI-RTVTRASLRRNIAVVFQDAGLF-NRSIEDNIRVG--RPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 108 QFDKLVALLGIEPL--LDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK13657 438 DEEMRAAAERAQAHdfIERKPDGydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 175 AReiNIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLED 215
Cdd:PRK13657 518 MK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-211 |
5.15e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 3 ELNFSQTLGTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvENGICLtpeKRRVGYV 81
Cdd:PRK13647 9 DLHFRYKDGTKALKgLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWV---RSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 82 FQDarlfPHYKVR----------GNLRYGMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELL 150
Cdd:PRK13647 85 FQD----PDDQVFsstvwddvafGPVNMGLDKDeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 151 LLDEPLASLDIPRKRELLPYLQRLAREINIPMLyVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIV-ATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-207 |
6.48e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRV-----GYVFQDAR--LFPHYKVRGNL--- 97
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlrtewGFVHQHPRdgLRMQVSAGGNIger 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 -------RYGMAKSMAGQFDKLVAllgIEPL-LDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:PRK11701 116 lmavgarHYGDIRATAGDWLERVE---IDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11701 193 LLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-216 |
6.52e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRV---LNdvengicltpekrrVGYVFQdarlfPHYKVRGNLR-----Y 99
Cdd:COG1134 56 GIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalLE--------------LGAGFH-----PELTGRENIYlngrlL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKS-MAGQFDKLVALLGIEPLLDrLP-GGLSGGEKQRVAIGRAlltapelllldeplASL--------------DIPR 163
Cdd:COG1134 117 GLSRKeIDEKFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVA--------------TAVdpdillvdevlavgDAAF 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 164 KRELLPYLQRLAREINIpMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1134 182 QKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
28-211 |
7.85e-12 |
|
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: 63.10 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPhykvrgnlrygmaksmag 107
Cdd:cd03247 32 ALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-----SSLISVLNQRPYLFD------------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 108 qfdklvallgiEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIpmLYVSH 187
Cdd:cd03247 89 -----------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITH 155
|
170 180
....*....|....*....|....
gi 1915297335 188 SLDEILHlADKVMVLENGQVKAFG 211
Cdd:cd03247 156 HLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-207 |
1.02e-11 |
|
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: 66.00 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengiclTPE--KRRVGYVFQDARLFpHYKVRGNL 97
Cdd:COG5265 380 EVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV------TQAslRAAIGIVPQDTVLF-NDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMAKsmAGQfDKLVA---LLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:COG5265 453 AYGRPD--ASE-EEVEAaarAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1915297335 164 KRELLPYLQRLAReiNIPMLYVSHSLDEILHlADKVMVLENGQV 207
Cdd:COG5265 530 ERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-207 |
1.07e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLNEtlpasG--ITAIfGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKR--RVGYVFQDARL--F 88
Cdd:COG1101 27 LTIEE-----GdfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTK---LPEYKRakYIGRVFQDPMMgtA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 89 PHYKV---------RG---NLRYGMAKSMAGQFDKLVALLGIEpLLDRLP---GGLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:COG1101 95 PSMTIeenlalayrRGkrrGLRRGLTKKRRELFRELLATLGLG-LENRLDtkvGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 154 EPLASLDiPRKRELLPYL-QRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG1101 174 EHTAALD-PKTAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-215 |
1.23e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQS--GRIVLNGRVLNdvengiclTPEKRRVGYVFQDARLFPHYKVRGNLRY---- 99
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--------KQILKRTGFVTQDDILYPHLTVRETLVFcsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKSMAGQ-----FDKLVALLGIEPLLDRLPG-----GLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:PLN03211 168 RLPKSLTKQekilvAESVISELGLTKCENTIIGnsfirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLED 215
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-140 |
1.33e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQP---QSGRIVLNGRVLNDVEngicltpEKRRVGYVFQDARLFPHYKVRGNLRYGMAKS 104
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE-------MRAISAYVQQDDLFIPTLTVREHLMFQAHLR 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 105 MAGQFDKLVALLGIEPLLDRL------------PG---GLSGGEKQRVAIG 140
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQALglrkcantrigvPGrvkGLSGGERKRLAFA 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-216 |
1.34e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNgrvlndvENGICLTP----EKRRVGYVFQDARLFPHYKVRGNLRYGM 101
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-------DEDISLLPlharARRGIGYLPQEASIFRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 -------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRL 174
Cdd:PRK10895 104 qirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 175 aREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK10895 184 -RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-207 |
1.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND-----------VENGICLTPEK---------RRVGYVFQdarl 87
Cdd:PRK13651 37 AIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvlEKLVIQKTRFKkikkikeirRRVGVVFQ---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 FPHYK----------VRGNLRYGM----AKSMAGQFDKLVALlgIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:PRK13651 113 FAEYQlfeqtiekdiIFGPVSMGVskeeAKKRAAKYIELVGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFD 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 154 EPLASLDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK13651 191 EPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-225 |
1.60e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 19 ETLpasgitAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEKRR-----VGYVFQD--ARL---- 87
Cdd:PRK15079 48 ETL------GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG------MKDDEWRavrsdIQMIFQDplASLnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 -------------FPHYK---VRGNLRYGMAKsmagqfdklVALLgiEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLL 151
Cdd:PRK15079 116 tigeiiaeplrtyHPKLSrqeVKDRVKAMMLK---------VGLL--PNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 152 LDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgSSVMHPW 225
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY-HNPLHPY 257
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-207 |
1.71e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND------VENGICLTPEKRRVgyvfqdarlFPHYKVRGNLry 99
Cdd:PRK11614 33 IVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIVPEGRRV---------FSRMTVEENL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 gmakSMAGQF-DKLVALLGIEPLLDRLP----------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:PRK11614 102 ----AMGGFFaERDQFQERIKWVYELFPrlherriqraGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 169 PYLQRLaREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11614 178 DTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-216 |
2.09e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK--RRVGYVFQdARLFPH-YKV 93
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM------LSSRQlaRRLALLPQ-HHLTPEgITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLRYGMAK------SMAGQFDKLV----ALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPR 163
Cdd:PRK11231 94 RELVAYGRSPwlslwgRLSAEDNARVnqamEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 164 KRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK11231 174 QVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-216 |
3.80e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISG-LTQPQ-------SGRIVLNGRVLN--DVENGICLT---PEKRRVGYVFQDARL----- 87
Cdd:PRK13547 29 VTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAaiDAPRLARLRavlPQAAQPAFAFSAREIvllgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 FPHYKVRGNLrygmAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEP---------LAS 158
Cdd:PRK13547 109 YPHARRAGAL----THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPPHDAAQPpryllldepTAA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 159 LDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK13547 185 LDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-228 |
4.21e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLnDVENGICLTPEKRRVGYVFQD--ARLFPH----YKVRGNLR-YG 100
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLQALRRDIQFIFQDpyASLDPRqtvgDSIMEPLRvHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 M--AKSMAGQFDKLVALLGIEPLLD-RLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK10261 433 LlpGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgSSVMHPWLPK 228
Cdd:PRK10261 513 FGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF-ENPQHPYTRK 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-229 |
4.78e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRV------LNDVENGICLTPEKRRvgyvfqDARLFPHYKVRGN------LR 98
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspLDAVKKGMAYITESRR------DNGFFPNFSIAQNmaisrsLK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 YGMAKSMAGQFD---------KLVALLGIE-PLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELL 168
Cdd:PRK09700 370 DGGYKGAMGLFHevdeqrtaeNQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 169 PYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKA-FGSLEDVWGSSVMHPWLPKE 229
Cdd:PRK09700 450 KVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNRDDMSEEEIMAWALPQE 510
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-216 |
5.18e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDV------ENGIcltpekrrvGYVFQDARLFPHYKVRGNLRY 99
Cdd:PRK09700 33 IHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhklaaQLGI---------GIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMA-------------KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK09700 104 GRHltkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDY 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK09700 184 LFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-216 |
5.23e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicLTPEK-RRVGYV--FQDARLF------------PH 90
Cdd:PRK11300 33 IVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG------LPGHQiARMGVVrtFQHVRLFremtvienllvaQH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMAKSMAGQFDKLVAL---------LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK11300 107 QQLKTGLFSGLLKTPAFRRAESEALdraatwlerVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 162 PRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK11300 187 KETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
11-216 |
5.44e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 11 GTHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTqPQSGRIVLNGRVLNDVEngicLTPEKRRVGY---------- 80
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWS----AAELARHRAYlsqqqtppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 81 --VFQDARLFPHYKVRgnlrygmAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRV-------AIGRALLTAPELLL 151
Cdd:PRK03695 84 mpVFQYLTLHQPDKTR-------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 152 LDEPLASLDIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-216 |
6.00e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENgiclTPEKRRVGYVFQDARL--------- 87
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQNATTpgditvqel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 -----FPHYKVRGNLRygmaKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:PRK10253 102 vargrYPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 163 RKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-209 |
6.28e-11 |
|
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: 63.31 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQ-SGRIVLNGRVLN------DVENGICLTPEKR-RVGYVfqdarlfPHYKVRGNL 97
Cdd:TIGR02633 288 ILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaqAIRAGIAMVPEDRkRHGIV-------PILGVGKNI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 RYGMAKSMA--GQFDKLVALLGIEPLLDRLP----------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:TIGR02633 361 TLSVLKSFCfkMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1915297335 166 ELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKA 209
Cdd:TIGR02633 441 EIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-207 |
7.21e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENgicLTPEKRR---VGYVFQDaRL--------------- 87
Cdd:COG3845 286 ILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE---DITG---LSPRERRrlgVAYIPED-RLgrglvpdmsvaenli 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 -----FPHYKVRGNLRYGMAKSMAgqfDKLVALLGIE-PLLDRLPGGLSGGEKQRVAIGRAlltapelllldeplasldI 161
Cdd:COG3845 359 lgryrRPPFSRGGFLDRKAIRAFA---EELIEEFDVRtPGPDTPARSLSGGNQQKVILARE------------------L 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 162 PRKRELL----P----------YL-QRL--AREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:COG3845 418 SRDPKLLiaaqPtrgldvgaieFIhQRLleLRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
28-225 |
1.14e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVengicLTPEK-------RRVGYVFQD--ARLFPHYKVRGNLR 98
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQ---DL-----LKADPeaqkllrQKIQIVFQNpyGSLNPRKKVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 YGM-------AKSMAGQFDKLVALLGIEP-LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPY 170
Cdd:PRK11308 117 EPLlintslsAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 171 LQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSvMHPW 225
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP-RHPY 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-220 |
1.19e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNdVENGICLtpeKRRVGYVFQDA-RLFPHYKVRGNLRYGMA---- 102
Cdd:PRK13642 37 SIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT-AENVWNL---RRKIGMVFQNPdNQFVGATVEDDVAFGMEnqgi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 --KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINI 180
Cdd:PRK13642 113 prEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 181 PMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDVWGSS 220
Cdd:PRK13642 193 TVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-142 |
1.24e-10 |
|
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: 60.18 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrrvGYVFQDARLFPHyKVRGN 96
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI-----------------AYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 97 LRYGMaksmagQFD--------KLVALlgiEPLLDRLPGG-----------LSGGEKQRVAIGRA 142
Cdd:cd03250 86 ILFGK------PFDeeryekviKACAL---EPDLEILPDGdlteigekginLSGGQKQRISLARA 141
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-207 |
2.33e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLT------PEKRRVGYVFQDARLfpHYKVRGNLRY 99
Cdd:PRK15439 291 ILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvylPEDRQSSGLYLDAPL--AWNVCALTHN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMA-----KSMAGQFDKLVALLGIE-PLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK15439 369 RRGfwikpARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS 448
|
170 180 190
....*....|....*....|....*....|....
gi 1915297335 174 LAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK15439 449 IAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-225 |
3.00e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQpQSGRI----VLNGR-VLNdvengiclTPEKR-------RVGYVFQD 84
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGReILN--------LPEKElnklraeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 --ARLFPHYKVRGNL------RYGMAKSMAgqFDKLVALLG---IEPLLDRL---PGGLSGGEKQRVAIGRALLTAPELL 150
Cdd:PRK09473 106 pmTSLNPYMRVGEQLmevlmlHKGMSKAEA--FEESVRMLDavkMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 151 LLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGSSVmHPW 225
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS-HPY 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-216 |
3.15e-10 |
|
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: 61.36 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLNEtlpaSGITAIFGVSGAGKTSLINAISGLTQ--PQSGRIVLN-------GRVLNDVENG----IC---LTPE---- 74
Cdd:TIGR03269 21 FTIEE----GEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcGYVERPSKVGepcpVCggtLEPEevdf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 75 -----------KRRVGYVFQdaRLFPHY---KVRGNLRYGM------AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEK 134
Cdd:TIGR03269 97 wnlsdklrrriRKRIAIMLQ--RTFALYgddTVLDNVLEALeeigyeGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 135 QRVAIGRALLTAPELLLLDEPLASLDiPRKRELL-PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSL 213
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTP 253
|
...
gi 1915297335 214 EDV 216
Cdd:TIGR03269 254 DEV 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-207 |
4.68e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicLTPEKRR-VGYVFQDARLFPHYKVRGNLRYGMAKSMAGQF 109
Cdd:PRK10908 35 GHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR--EVPFLRRqIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 110 D---KLVALLGIEPLLDR---LPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAReINIPML 183
Cdd:PRK10908 113 DirrRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVL 191
|
170 180
....*....|....*....|....
gi 1915297335 184 YVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK10908 192 MATHDIGLISRRSYRMLTLSDGHL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-207 |
5.33e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN------DVENGICLTPEKRRvgyvfQDArLFPHYKVRGN--- 96
Cdd:PRK11288 281 IVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGIMLCPEDRK-----AEG-IIPVHSVADNini 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 ------LRYGM---AKSMAGQFDKLVALLGIE-PLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK11288 355 sarrhhLRAGClinNRWEAENADRFIRSLNIKtPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 167 LLPYLQRLArEINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK11288 435 IYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| MopI |
COG3585 |
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism]; |
275-350 |
7.51e-10 |
|
Molybdopterin-binding protein MopI [Coenzyme transport and metabolism];
Pssm-ID: 442804 [Multi-domain] Cd Length: 141 Bit Score: 56.62 E-value: 7.51e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 275 IQASDVSLVLQPPQQTSIRNVLRAKVAQCYDDNGQVEVQLEVG-GKTLWARISPWARDELGIKPGLWLYAQIKSVSI 350
Cdd:COG3585 59 KKASVVILATDDAMKLSARNQLKGTVTRIERGAVNSEVVLDLGgGTTLTAVITNESVEELGLKEGDEVTALFKASSV 135
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-142 |
9.68e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:PRK10535 30 DIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNVEV 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1915297335 100 -----GMAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:PRK10535 110 pavyaGLERKQRLLrAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-160 |
1.12e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENGICLTpeKRRVGYVFQDARLFPHYKVRGNLRYG 100
Cdd:PRK13540 24 LPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTY--QKQLCFVGHRSGINPYLTLRENCLYD 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 101 M-AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:PRK13540 99 IhFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-217 |
1.15e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQ-----SGRIVLNGR-VLNDVENGICLtpeKRRVGYVFQDARLFPH 90
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRnIYSPDVDPIEV---RREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYG-----MAKSmAGQFDKLV-------ALLgiEPLLDRL---PGGLSGGEKQRVAIGRALLTAPELLLLDEP 155
Cdd:PRK14267 100 LTIYDNVAIGvklngLVKS-KKELDERVewalkkaALW--DEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 156 LASLDIPRKRELLPYLQRLAREINIpmLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-216 |
1.32e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTqPQSGRIVLNGRVLNDvengiCLTPEKRRV-GYVFQDARLFP-----H 90
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSD-----WSAAELARHrAYLSQQQSPPFampvfQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEP-------LASLDIPR 163
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQlllldepMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 164 KRELLPYLQRLARE-INIPMlyVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4138 169 QAALDRLLRELCQQgITVVM--SSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-212 |
1.36e-09 |
|
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: 57.42 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVeNGICLTPEKRRVGYVFQDARLFPHyKVRGNL-RYGMAKSmag 107
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGI---DI-STIPLEDLRSSLTIIPQDPTLFSG-TIRSNLdPFDEYSD--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 108 qfDKLVALLGIEPlldrlpGG--LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREllpyLQRLAREI--NIPML 183
Cdd:cd03369 111 --EEIYGALRVSE------GGlnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL----IQKTIREEftNSTIL 178
|
170 180
....*....|....*....|....*....
gi 1915297335 184 YVSHSLDEILHLaDKVMVLENGQVKAFGS 212
Cdd:cd03369 179 TIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-214 |
1.59e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDV--ENGICLTPEKRRVGYVF----QDARLFPHYKV 93
Cdd:PRK15056 29 TVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqKNLVAYVPQSEEVDWSFpvlvEDVVMMGRYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 RGNLRYGMAKSMAgQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK15056 109 MGWLRRAKKRDRQ-IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 174 LaREINIPMLYVSHSLDEILHLAD-KVMVleNGQVKAFGSLE 214
Cdd:PRK15056 188 L-RDEGKTMLVSTHNLGSVTEFCDyTVMV--KGTVLASGPTE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-207 |
1.66e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.72 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 2 LELNFSQTLGTHCLTLNetLPASGITAIFGVSGAGKTSLINAISGL----TQPQS-----GRIV-LNGRVLNDVENgicl 71
Cdd:PRK09984 10 LAKTFNQHQALHAVDLN--IHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGShiellGRTVqREGRLARDIRK---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 72 tpEKRRVGYVFQDARLFPHYKVRGNLRYGMAKSMA---------GQFDKLVAL-----LGIEPLLDRLPGGLSGGEKQRV 137
Cdd:PRK09984 84 --SRANTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfswfTREQKQRALqaltrVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 138 AIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-217 |
1.81e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQ--PQ---SGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFPHY 91
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMD----VIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNLRYG-----MAKSMAGQFDKLVALLGIEPL-------LDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK14247 98 SIFENVALGlklnrLVKSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 160 DIPRKRELLPYLQRLAREINIPMlyVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVL--VTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-212 |
2.32e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLndvengicltPE-----KRRVGYVFQDARLFPHYKVRGNLR----- 98
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------PSrarhaRQRVGVVPQFDNLDPDFTVRENLLvfgry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 YGMAksmAGQFDKLVALL----GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR- 173
Cdd:PRK13537 108 FGLS---AAAARALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD-PQARHLMWERLRs 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 174 -LAREINIpmLYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:PRK13537 184 lLARGKTI--LLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-216 |
2.33e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN------DVENGICLtpekrrvgyVFQDARLFPHYKVRGNLRYGM 101
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAGVAI---------IYQELHLVPEMTVAENLYLGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKSMAGQFDKLVALLGIEPLLDRL-----P----GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQ 172
Cdd:PRK11288 105 LPHKGGIVNRRLLNYEAREQLEHLgvdidPdtplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1915297335 173 RLAREINIpMLYVSHSLDEILHLADKVMVLENGQ-VKAFGSLEDV 216
Cdd:PRK11288 185 ELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRyVATFDDMAQV 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-142 |
2.78e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQS-GRIVLNGRVlndvengicltpekrrvGYVFQDARLFpHYKVRG 95
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTV-----------------AYVPQVSWIF-NATVRD 697
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 96 NLRYGmAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRA 142
Cdd:PLN03130 698 NILFG-SPFDPERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARA 754
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
2.84e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.43 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 1 MLEL-NFSQTLGTHcLTLNE---TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengicltPEKR 76
Cdd:COG4152 1 MLELkGLTKRFGDK-TAVDDvsfTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP--------EDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 77 RVGYVFQDARLFPHYKVRGNLRY-----GMAKSMA-GQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGralltapell 150
Cdd:COG4152 72 RIGYLPEERGLYPKMKVGEQLVYlarlkGLSKAEAkRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 151 lldeplAS---------LDIP-----------RKRELLpylqRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKAF 210
Cdd:COG4152 142 ------AAllhdpelliLDEPfsgldpvnvelLKDVIR----ELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
....*.
gi 1915297335 211 GSLEDV 216
Cdd:COG4152 211 GSVDEI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-211 |
2.86e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpeKRRVGYVFQDARLFPHyKVRGN 96
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1915297335 166 ELLPYLQRLAReiniPMLYVSHSLdEILHLADKVMVLENGQVKAFG 211
Cdd:TIGR00958 655 LLQESRSRASR----TVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-212 |
5.66e-09 |
|
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: 55.58 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDvengICLTPEKRRVGYVFQDARLFphykvRGNLRY-------- 99
Cdd:cd03244 34 GIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK----IGLHDLRSRISIIPQDPVLF-----SGTIRSnldpfgey 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 ---------------GMAKSMAGQFDKLVALLGieplldrlpGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIprk 164
Cdd:cd03244 105 sdeelwqalervglkEFVESLPGGLDTVVEEGG---------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDP--- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 165 rELLPYLQRLAREI--NIPMLYVSHSLDEILHlADKVMVLENGQVKAFGS 212
Cdd:cd03244 173 -ETDALIQKTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-216 |
5.87e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR-LYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAK--SMAGQFDKLVALLGIEPLLDR-----LPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP 169
Cdd:PRK11831 105 VAYPLREhtQLPAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 170 YLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
17-208 |
9.40e-09 |
|
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: 55.10 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGR--VLNDVENgicltpekrrVGYVFQDARLFPHYKVR 94
Cdd:TIGR03740 19 ISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHpwTRKDLHK----------IGSLIESPPLYENLTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 95 GNLRY-----GMAKSmagQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD---IPRKRE 166
Cdd:TIGR03740 89 ENLKVhttllGLPDS---RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpigIQELRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 167 LLpylqRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVK 208
Cdd:TIGR03740 166 LI----RSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-221 |
9.47e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 24 SGITAIFGVSGAGKTSLINAISGLTQPQsGRIVLNGRV----LNDVENGICLTPEKRRVGYVFQDARLFPhYKVRGNLRY 99
Cdd:PRK14258 33 SKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnQNIYERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMakSMAG-----QFDKLV-ALLGIEPLLDRLPGG-------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE 166
Cdd:PRK14258 111 GV--KIVGwrpklEIDDIVeSALKDADLWDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLEN-----GQVKAFGSLEDVWGSSV 221
Cdd:PRK14258 189 VESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-142 |
1.16e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 22 PASGITAIFGVSGAGKTSLINAISGL--TQPQ---SGRIVLNGRVLNDveNGICLTPEKRRVGYVFQDARLFPH--YKvr 94
Cdd:COG1117 35 PENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYD--PDVDVVELRRRVGMVFQKPNPFPKsiYD-- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 95 gNLRYGM----AKSmAGQFDKLVallgiEPLL----------DRL--PG-GLSGGEKQRVAIGRA 142
Cdd:COG1117 111 -NVAYGLrlhgIKS-KSELDEIV-----EESLrkaalwdevkDRLkkSAlGLSGGQQQRLCIARA 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-142 |
1.19e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.23 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrRVGYVFQDARLFPHYKVRGNLRYGMAKSMA---- 106
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------------RIGYLPQEPPLDDDLTVLDTVLDGDAELRAleae 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 107 ----------------------GQFD------------KLVALLGI-EPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:COG0488 96 leeleaklaepdedlerlaelqEEFEalggweaearaeEILSGLGFpEEDLDRPVSELSGGWRRRVALARA 166
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-217 |
1.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.08 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGicLTPEKRRVGYVFQ--DARLF-PHYK---VRGNLRY 99
Cdd:PRK13639 30 MVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS--LLEVRKTVGIVFQnpDDQLFaPTVEedvAFGPLNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAK-SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREi 178
Cdd:PRK13639 108 GLSKeEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE- 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 179 NIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13639 187 GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
1.66e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.10 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAISGLTQP-----QSGRIVLNGRVLNDVENgicLTPEKRRVGYVFQDARLFPhYKVRG 95
Cdd:PRK14271 44 FPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRD---VLEFRRRVGMLFQRPNPFP-MSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYGMA-------KSMAGQFDKLVALLGI-EPLLDRL---PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:PRK14271 120 NVLAGVRahklvprKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 165 RELLPYLQRLAREINIpmLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWGS 219
Cdd:PRK14271 200 EKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-217 |
1.67e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQsGRIVLNGRVLNDVeNGICLTPEKRRVGYVFQDA------RLFPHYKVRGNLRYGMAKS 104
Cdd:PRK15134 319 GESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNL-NRRQLLPVRHRIQVVFQDPnsslnpRLNVLQIIEEGLRVHQPTL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 MAGQFDKLVALLGIEPLLD-----RLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREIN 179
Cdd:PRK15134 397 SAAQREQQVIAVMEEVGLDpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQ 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 180 IPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVF 514
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-217 |
2.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 25 GITAIFGVSGAGKTSLINAIS--GLTQPQ---SGRIVLNGrvlNDVENGICLTPEKRR-VGYVFQDARLFPhYKVRGNLR 98
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNG---HNIYSPRTDTVDLRKeIGMVFQQPNPFP-MSIYENVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 YGMakSMAGQFDKLVALLGIEPLL----------DRLPG---GLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK14239 108 YGL--RLKGIKDKQVLDEAVEKSLkgasiwdevkDRLHDsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAREINipMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK14239 186 KIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-215 |
2.59e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrRVGYVFQD-ARLFPHYKVRG 95
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------------KIGYFDQHqEELDPDKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYGM-------AKSMAGQF-------DKLVallgieplldrlpGGLSGGEKQRVAIGRAlltapelllldepLAS--- 158
Cdd:COG0488 399 ELRDGApggteqeVRGYLGRFlfsgddaFKPV-------------GVLSGGEKARLALAKL-------------LLSppn 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 159 ----------LDIPRKRELLPYLQrlareiNIP--MLYVSHS---LDEIlhlADKVMVLENGQVKAF-GSLED 215
Cdd:COG0488 453 vllldeptnhLDIETLEALEEALD------DFPgtVLLVSHDryfLDRV---ATRILEFEDGGVREYpGGYDD 516
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-215 |
2.62e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFpHYKVRGN 96
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT----LASLRNQVALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGM-----------AKSMAgqfdklVALLGIEPL---LDRLPG----GLSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:PRK11176 437 IAYARteqysreqieeAARMA------YAMDFINKMdngLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 159 LDIPRKRELLPYLQRLAReiNIPMLYVSHSLDEIlHLADKVMVLENGQVKAFGSLED 215
Cdd:PRK11176 511 LDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVEDGEIVERGTHAE 564
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-202 |
2.63e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.39 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRivlngrvlndvengiCLTPEKRRVGYVFQDARL--------- 87
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVpdslpltvr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 88 -------FPHykvRGNLRYGMAKSMAGQFDKLVALlGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:NF040873 76 dlvamgrWAR---RGLWRRLTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 161 IPRKRELLPYLQRLAREiNIPMLYVSHSLDEILhLADKVMVL 202
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-224 |
2.77e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVlngrvlndvengiclTPEKRRVGYVFQDARLFPHYKVRGNlRY 99
Cdd:PRK09544 26 ELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYVPQKLYLDTTLPLTVN-RF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKSMAGQFDKLVALLGIEP--LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:PRK09544 90 LRLRPGTKKEDILPALKRVQAghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLeNGQVKAFGSLEDVwgssVMHP 224
Cdd:PRK09544 170 LDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVV----SLHP 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-205 |
2.85e-08 |
|
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: 53.49 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 6 FSQTLGTHCLT-LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICLTPEKRRVGYVFQD 84
Cdd:cd03290 8 FSWGSGLATLSnINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 ARLFpHYKVRGNLRYGmAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLD 153
Cdd:cd03290 88 PWLL-NATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 154 EPLASLDIPRKRELLPY-LQRLAREINIPMLYVSHSLDEILHlADKVMVLENG 205
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
117-207 |
3.04e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 117 GIEPLLDRL---PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEIL 193
Cdd:PRK15134 142 GIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVR 221
|
90
....*....|....
gi 1915297335 194 HLADKVMVLENGQV 207
Cdd:PRK15134 222 KLADRVAVMQNGRC 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-212 |
3.98e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.83 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND-----VENGICLTPEkrRVgYVFQDArlfphy 91
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaaLRQAISVVSQ--RV-HLFSAT------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 kVRGNLRygMAKSMAGQfDKLVALL---GIEPLLDRLP--------GG--LSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:PRK11160 430 -LRDNLL--LAAPNASD-EALIEVLqqvGLEKLLEDDKglnawlgeGGrqLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 159 LDIPRKRELLPYLQRLAReiNIPMLYVSHSLDEILHLaDKVMVLENGQVKAFGS 212
Cdd:PRK11160 506 LDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-217 |
4.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENgicLTPEKRRVGYVFQDarlfPHYKVrgnlrygmaksMAG 107
Cdd:PRK13633 40 VILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN---LWDIRNKAGMVFQN----PDNQI-----------VAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 108 QFDKLVAL----LGIEPLLDRL------------------PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK13633 102 IVEEDVAFgpenLGIPPEEIRErvdeslkkvgmyeyrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLQRLAREINIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDVW 217
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
26-216 |
4.23e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVengicltPEKRR----VGYVFQDARLFPHYKVRGNLrygM 101
Cdd:COG1137 31 IVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-------PMHKRarlgIGYLPQEASIFRKLTVEDNI---L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 A------KSMAGQFDKLVALL---GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD------IprkRE 166
Cdd:COG1137 101 AvlelrkLSKKEREERLEELLeefGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavadI---QK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 167 LLPYLqrlaREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG1137 178 IIRHL----KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-216 |
6.07e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvlNDVENgICLTPEKRRVGYVFQDARLFPHyKVRGNLRYGMAKSMAGQ 108
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAK-FGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 109 FDKLvALLGIEPLLDRLPGGL-----------SGGEKQRVAIGRALLTAPELLLLDEPLASLDIpRKRELlpyLQRLARE 177
Cdd:PLN03232 1342 WEAL-ERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDV-RTDSL---IQRTIRE 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915297335 178 --INIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLEDV 216
Cdd:PLN03232 1417 efKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-222 |
9.10e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 5 NFSQTLGTHCLTL---NETLPASGITAIFGVSGAGKTSLINAISG-LTQPQSGRIVLNGRVlndvengicltpekrrvGY 80
Cdd:PLN03232 621 YFSWDSKTSKPTLsdiNLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSV-----------------AY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 81 VFQDARLFpHYKVRGNLRYGmAKSMAGQFDKLVALLGIEPLLDRLPG-----------GLSGGEKQRVAIGRALLTAPEL 149
Cdd:PLN03232 684 VPQVSWIF-NATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 150 LLLDEPLASLDIPRKRELLPYLQRLAREINIPMLyVSHSLdEILHLADKVMVLENGQVKAFGSLEDVWGSSVM 222
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVL-VTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-142 |
1.24e-07 |
|
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: 53.25 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 22 PASG-ITAIFGVSGAGKTSLINAISGLTQPqsgrivlNgrvLNDVENGicltPEKRRVGYVFQDARLFPHYK--VRGNLR 98
Cdd:COG1245 96 PKKGkVTGILGPNGIGKSTALKILSGELKP-------N---LGDYDEE----PSWDEVLKRFRGTELQDYFKklANGEIK 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297335 99 ------Y---------GMAKSM------AGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRA 142
Cdd:COG1245 162 vahkpqYvdlipkvfkGTVRELlekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAA 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-214 |
1.24e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.99 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLT--QPQSGRIVLNGRVLNDvengicLTPEKR-RVG--YVFQDARLFPHY 91
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILE------LSPDERaRAGifLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNLRYGM-----AKSMAGQFDKLV----ALLGIEP-LLDR-LPGGLSGGEKQR------------VAI------Gra 142
Cdd:COG0396 93 SVSNFLRTALnarrgEELSAREFLKLLkekmKELGLDEdFLDRyVNEGFSGGEKKRneilqmlllepkLAIldetdsG-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 143 lltapelllldeplasLDIPRkrellpyLQRLAREIN------IPMLYVSHS---LDEIlhLADKVMVLENGQVKAFGSL 213
Cdd:COG0396 171 ----------------LDIDA-------LRIVAEGVNklrspdRGILIITHYqriLDYI--KPDFVHVLVDGRIVKSGGK 225
|
.
gi 1915297335 214 E 214
Cdd:COG0396 226 E 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-211 |
1.25e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.53 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRI-VLNGRVLNDVENGicltpeKRRVGYVFQDARLFPHYKVRGNL----RY-GM- 101
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLA------RARIGVVPQFDNLDLEFTVRENLlvfgRYfGMs 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELLPYLQR--LAREIN 179
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHLIWERLRslLARGKT 224
|
170 180 190
....*....|....*....|....*....|..
gi 1915297335 180 IpmLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:PRK13536 225 I--LLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-198 |
1.60e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLI---NAISGLTQP--QSGRIVLNGRVLNDveNGICLTPEKRRVGYVFQDARLFPHyKVRG 95
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLYA--PDVDPVEVRRRIGMVFQKPNPFPK-SIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYGM-AKSMAGQFDKLV------ALLGIEpLLDRLPG---GLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK14243 110 NIAYGArINGYKGDMDELVerslrqAALWDE-VKDKLKQsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTL 188
|
170 180 190
....*....|....*....|....*....|...
gi 1915297335 166 ELLPYLQRLAREINIpmLYVSHSLDEILHLADK 198
Cdd:PRK14243 189 RIEELMHELKEQYTI--IIVTHNMQQAARVSDM 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-202 |
1.96e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRI--------VLN---GRVLND-----VENGIcltpekrRVGYVFQDARLFP 89
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGTELQNyfkklYNGEI-------KVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 90 HYkVRGNLRYGMAKS-MAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGralltapelllldeplASL----DIPRK 164
Cdd:PRK13409 174 KV-FKGKVRELLKKVdERGKLDEVVERLGLENILDRDISELSGGELQRVAIA----------------AALlrdaDFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1915297335 165 RELLPYL---QRL--AREI-----NIPMLYVSHSLdEIL-HLADKVMVL 202
Cdd:PRK13409 237 DEPTSYLdirQRLnvARLIrelaeGKYVLVVEHDL-AVLdYLADNVHIA 284
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-203 |
2.97e-07 |
|
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: 50.87 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 7 SQTLGTHCLTLNE-TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvengicltpEKRRVGYVfqda 85
Cdd:cd03237 7 KKTLGEFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI----------------ELDTVSYK---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 86 rlfPHY---KVRGNLRYGMAKSMAG-----QFDKLVAL-LGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:cd03237 67 ---PQYikaDYEGTVRDLLSSITKDfythpYFKTEIAKpLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 157 ASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLE 203
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-160 |
3.82e-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: 50.18 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGIcltpeKRRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:cd03231 22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 100 GMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLD 160
Cdd:cd03231 97 WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-211 |
4.77e-07 |
|
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: 50.44 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 22 PASG-ITAIFGVSGAGKTSLINAISGLTQPQSGRI--------VLN---GRVLND-----VENGICLTpekRRVGYVFQD 84
Cdd:cd03236 23 PREGqVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNyftklLEGDVKVI---VKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 ARLFPHyKVRGNLRygmAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRK 164
Cdd:cd03236 100 PKAVKG-KVGELLK---KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 165 RELLPYLQRLAREINiPMLYVSHSLDEILHLADKVMVLEnGQVKAFG 211
Cdd:cd03236 176 LNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-GEPGAYG 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-244 |
5.17e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 50.67 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 15 LTLNEtlpaSGITAIFGVSGAGKTSLINAISGLTQPQ----SGRIVLNGRVLndvengICLTPEKRR------VGYVFQD 84
Cdd:COG4170 28 LTLNE----GEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDL------LKLSPRERRkiigreIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 AR--LFPHYKVRGNLRYGM-AKSMAGQF--------DKLVALL---GI---EPLLDRLPGGLSGGEKQRVAIGRALLTAP 147
Cdd:COG4170 98 PSscLDPSAKIGDQLIEAIpSWTFKGKWwqrfkwrkKRAIELLhrvGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 148 ELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgSSVMHP--- 224
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL-KSPHHPytk 256
|
250 260 270
....*....|....*....|....*....|...
gi 1915297335 225 -----------WLPKEQQSSILKVSV--LEHHP 244
Cdd:COG4170 257 allrsmpdfrqPLPHKSRLNTLPGSIppLQHLP 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-216 |
5.44e-07 |
|
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: 51.22 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 19 ETLpasgitAIFGVSGAGK--TSLinAISGLTQPQ----SGRIVLNGRVLNDVengicltPEK-------RRVGYVFQD- 84
Cdd:COG4172 37 ETL------ALVGESGSGKsvTAL--SILRLLPDPaahpSGSILFDGQDLLGL-------SERelrrirgNRIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 85 -ARLFPHYKVrGN-------LRYGMAKSMAGQfdKLVALL---GI---EPLLDRLPGGLSGGEKQRVAIGRAlltapell 150
Cdd:COG4172 102 mTSLNPLHTI-GKqiaevlrLHRGLSGAAARA--RALELLervGIpdpERRLDAYPHQLSGGQRQRVMIAMA-------- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 151 lldepLAS-------------LDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:COG4172 171 -----LANepdlliadepttaLDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-219 |
6.69e-07 |
|
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: 51.17 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENGicLTPEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK---DIETN--LDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 -LRYGMAKSMAGQFDKL--VALL---GIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRE---- 166
Cdd:TIGR01257 1024 iLFYAQLKGRSWEEAQLemEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSiwdl 1103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915297335 167 LLPYlqRLAREInipmLYVSHSLDEILHLADKVMVLENGQVKAFGS---LEDVWGS 219
Cdd:TIGR01257 1104 LLKY--RSGRTI----IMSTHHMDEADLLGDRIAIISQGRLYCSGTplfLKNCFGT 1153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-209 |
8.77e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQS-GRIVLNGRVLN------DVENGICLTPEKR-RVGYVfqdarlfPHYKVRGNL 97
Cdd:PRK13549 290 ILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKirnpqqAIAQGIAMVPEDRkRDGIV-------PVMGVGKNI 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 ------RYgmakSMAGQFDKLVALLGIEPLLDRLP----------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13549 363 tlaaldRF----TGGSRIDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 162 PRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKA 209
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-206 |
1.39e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN------DVENGIcltpekrrvGYVFQDARLFPHYKVRGNL---- 97
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpksSQEAGI---------GIIHQELNLIPQLTIAENIflgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 98 ----RYGMA--KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYL 171
Cdd:PRK10762 105 efvnRFGRIdwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVI 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1915297335 172 QRLaREINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:PRK10762 185 REL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-140 |
1.69e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQP---QSGRIVLNGRVLNdvengiclTPEKRRVGYVFQDARLFPHYKVRGNLRYG-- 100
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD--------SSFQRSIGYVQQQDLHLPTSTVRESLRFSay 862
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 101 ------MAKSMAGQF-DKLVALLGIEPLLDRLPG----GLSGGEKQRVAIG 140
Cdd:TIGR00956 863 lrqpksVSKSEKMEYvEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIG 913
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-211 |
1.91e-06 |
|
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: 48.30 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltpekrrVGYVFQdarlfPHYKVRGNLR-----YGM- 101
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----------LGGGFN-----PELTGRENIYlngrlLGLs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 102 AKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPelllldeplaslDIprkrellpYL---------- 171
Cdd:cd03220 116 RKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEP------------DI--------LLidevlavgda 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1915297335 172 -------QRLAREINIP--MLYVSHSLDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03220 176 afqekcqRRLRELLKQGktVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-207 |
2.32e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLND------VENGICLTPEKRRVGYVFqdarlfphykvrGNLRY 99
Cdd:PRK10982 276 ILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINHGFALVTEERRSTGIY------------AYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMaKSMAGQFDKLVALLG--------------IEPLLDRLP------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:PRK10982 344 GF-NSLISNIRNYKNKVGlldnsrmksdtqwvIDSMRVKTPghrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1915297335 160 DIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQV 207
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-211 |
2.72e-06 |
|
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: 47.64 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTqpqSGRIVLNGRVL-NDVENGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYgmAKSMAGqf 109
Cdd:cd03233 40 GRPGSGCSTLLKALANRT---EGNVSVEGDIHyNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDF--ALRCKG-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 110 dklvallgiepllDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIP-MLYVSHS 188
Cdd:cd03233 113 -------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQA 179
|
170 180
....*....|....*....|...
gi 1915297335 189 LDEILHLADKVMVLENGQVKAFG 211
Cdd:cd03233 180 SDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
119-225 |
2.72e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 119 EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADK 198
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
90 100
....*....|....*....|....*..
gi 1915297335 199 VMVLENGQVKAFGSLEDVWGSSvMHPW 225
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAP-QHPY 264
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-225 |
3.64e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLT----QPQSGRIVLNGRVLNDvengicLTPEKRR------VGYVFQDA--RLFPHYKV 93
Cdd:PRK11022 35 VVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQR------ISEKERRnlvgaeVAMIFQDPmtSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 R------------GNLRYGMAKSMagqfdKLVALLGI---EPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLAS 158
Cdd:PRK11022 109 GfqimeaikvhqgGNKKTRRQRAI-----DLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 159 LDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDVWgSSVMHPW 225
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF-RAPRHPY 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-209 |
3.93e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSG---AGKTSLINAISGLTQPQSGRIVLNGRVLNDV------ENGICLTPEKR-RVGYVFQDA----------RLF 88
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglANGIVYISEDRkRDGLVLGMSvkenmsltalRYF 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 89 PHYKvrGNLRYGMAKSMAGQFdklVALLGIE-PLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK10762 360 SRAG--GSLKHADEQQAVSDF---IRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 168 LPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQVKA 209
Cdd:PRK10762 435 YQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-216 |
5.00e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPqsGRIVLNGRVLNDvenGICLTPEK---RRVGYVFQDAR--LFPHYKVRGNLR-Y 99
Cdd:PRK10418 31 VLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLD---GKPVAPCAlrgRKIATIMQNPRsaFNPLHTMHTHAReT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 100 GMAKSMAGQFDKLVALL---GIEP---LLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQR 173
Cdd:PRK10418 106 CLALGKPADDATLTAALeavGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1915297335 174 LAREINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:PRK10418 186 IVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-142 |
6.40e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.88 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvengicltPEKRRVGYVFQDARLFPhykvrGNLR----YGmakS 104
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------------PAGARVLFLPQRPYLPL-----GTLReallYP---A 450
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1915297335 105 MAGQFD--KLVALL---GIEPLLDRL------PGGLSGGEKQRVAIGRA 142
Cdd:COG4178 451 TAEAFSdaELREALeavGLGHLAERLdeeadwDQVLSLGEQQRLAFARL 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-206 |
1.04e-05 |
|
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: 47.13 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 14 CLTLNetlpASGITAIFGVSGAGKTSLINAISGLtQPQ---SGRIVLNGRVLndVENGICLTpEKRRVGYVFQDARLFPH 90
Cdd:TIGR02633 21 DLEVR----PGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPL--KASNIRDT-ERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 YKVRGNLRYG---------MA-KSMAGQFDKLVALLGIEPLLDRLP-GGLSGGEKQRVAIGRALLTAPELLLLDEPLASL 159
Cdd:TIGR02633 93 LSVAENIFLGneitlpggrMAyNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915297335 160 DIPRKRELLPYLQRLAREiNIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2-141 |
1.40e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 2 LELNFSQTlgtHCLTLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpekrrvGYV 81
Cdd:PRK13541 7 LQFNIEQK---NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 82 FQDARLFPHYKVRGNLRY-GMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGR 141
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIAR 136
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-141 |
1.50e-05 |
|
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: 46.85 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvENGIcltpekrRVGYVFQDARLFPHYKVRGNLRYGMAK----- 103
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGI-------KVGYLPQEPQLDPTKTVRENVEEGVAEikdal 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 104 ------SMA-----GQFDKLVALLG-IEPLLD------------------RLPGG------LSGGEKQRVAIGR 141
Cdd:TIGR03719 101 drfneiSAKyaepdADFDKLAAEQAeLQEIIDaadawdldsqleiamdalRCPPWdadvtkLSGGERRRVALCR 174
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-206 |
1.63e-05 |
|
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: 45.50 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQSGRIVLN--GRVLNdvengICLTPE-------KRRVGYVFQDARLFPhyKV---- 93
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD-----LAQASPreilalrRRTIGYVSQFLRVIP--RVsald 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 ---RGNLRYGMAKSMA-GQFDKLVALLGIEPLLDRL-PGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDiPRKRELL 168
Cdd:COG4778 113 vvaEPLLERGVDREEArARARELLARLNLPERLWDLpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD-AANRAVV 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 1915297335 169 PYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:COG4778 192 VELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-161 |
1.85e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.86 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRvlnDVENGICLTpekrRVGYV-FQDArLFPHYKVRG 95
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAE----ACHYLgHRNA-MKPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915297335 96 NLR-----YGMAKSMAgqfDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13539 93 NLEfwaafLGGEELDI---AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-57 |
3.39e-05 |
|
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: 45.70 E-value: 3.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVL 57
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-215 |
4.05e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRV--LNDVENgicltpeKRRVGYVF-QDARLFPHYKVRGNLR---- 98
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfKRRKEF-------ARRIGVVFgQRSQLWWDLPAIDSFRllka 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 99 -YGMAKSMAGQ-FDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAR 176
Cdd:COG4586 123 iYRIPDAEYKKrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNR 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 177 EINIPMLYVSHSLDEILHLADKVMVLENGQVKAFGSLED 215
Cdd:COG4586 203 ERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-214 |
4.27e-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: 45.77 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVL----NDVENGICLTPEKRRVGYVFQDARlfpHYKVRGNLRYGMAK 103
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSDVHQNMGYCPQFDAIDDLLTGRE---HLYLYARLRGVPAE 2045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 104 SMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPML 183
Cdd:TIGR01257 2046 EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
170 180 190
....*....|....*....|....*....|.
gi 1915297335 184 yVSHSLDEILHLADKVMVLENGQVKAFGSLE 214
Cdd:TIGR01257 2126 -TSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-218 |
4.77e-05 |
|
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: 45.29 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 5 NFSqTLGTHCL-TLNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrrvGYVFQ 83
Cdd:TIGR01271 433 NFS-LYVTPVLkNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-----------------SFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 84 DARLFPHyKVRGNLRYGMAKS--------MAGQFDKLVALLgiePLLDRLP---GG--LSGGEKQRVAIGRALLTAPELL 150
Cdd:TIGR01271 495 TSWIMPG-TIKDNIIFGLSYDeyrytsviKACQLEEDIALF---PEKDKTVlgeGGitLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 151 LLDEPLASLDIPRKRELLPY-LQRLAreINIPMLYVSHSLdEILHLADKVMVLENGQVKAFGSLEDVWG 218
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFEScLCKLM--SNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQA 636
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-57 |
4.88e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 4.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVL 57
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-206 |
5.04e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLTQpQSGRIVLNGRVLNDVENgICLTPEKRR------VGYVFQDAR--LFPH- 90
Cdd:PRK15093 29 TLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDL-LRLSPRERRklvghnVSMIFQEPQscLDPSe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 91 --------------YKVRGNLRYGMAKSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:PRK15093 107 rvgrqlmqnipgwtYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPT 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915297335 157 ASLDIPRKRELLPYLQRLAREINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:PRK15093 187 NAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-206 |
6.52e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 18 NETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLN------DVENGICLtpekrrvgyVFQDARLFPHY 91
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskeALENGISM---------VHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNL---RYGMA------KSMAGQFDKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIP 162
Cdd:PRK10982 89 SVMDNMwlgRYPTKgmfvdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1915297335 163 RKRELLPYLQRLaREINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:PRK10982 169 EVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-139 |
6.73e-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: 44.78 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 26 ITAIFGVSGAGKTSLINAISGLTQPQSGRIvlngrvlndvengicltPEKRRVGYVFQdaRLFPHYK--VRGNLRYGMAK 103
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------------DEDLKISYKPQ--YISPDYDgtVEEFLRSANTD 428
|
90 100 110
....*....|....*....|....*....|....*...
gi 1915297335 104 SMAGQFDK--LVALLGIEPLLDRLPGGLSGGEKQRVAI 139
Cdd:COG1245 429 DFGSSYYKteIIKPLGLEKLLDKNVKDLSGGELQRVAI 466
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-139 |
7.74e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvengicltpeKRRVGYVFQdaRLFPHYK--VRGNLRygmakSMA 106
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------------ELKISYKPQ--YIKPDYDgtVEDLLR-----SIT 425
|
90 100 110
....*....|....*....|....*....|....*....
gi 1915297335 107 GQFD------KLVALLGIEPLLDRLPGGLSGGEKQRVAI 139
Cdd:PRK13409 426 DDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAI 464
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-214 |
9.01e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 43.40 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISG--LTQPQSGRIVLNGRVLNDVEngicltPEKR-RVGYV--FQDARLFPHY 91
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELE------PDERaRAGLFlaFQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 92 KVRGNLR---------YGMAKSMAGQFDKLV----ALLGI-EPLLDR-LPGGLSGGEKQRVAIGRALLTAPELLLLDEPL 156
Cdd:TIGR01978 93 SNLEFLRsalnarrsaRGEEPLDLLDFEKLLkeklALLDMdEEFLNRsVNEGFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297335 157 ASLDIPRKRELLPYLQRLaREINIPMLYVSHSLDEILHLA-DKVMVLENGQVKAFGSLE 214
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRL-REPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-142 |
1.13e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 42.14 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvengicltPEKRRVGYVFQDArlfphYKVRGNLRygmaksmagq 108
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQRP-----YLPLGTLR---------- 81
|
90 100 110
....*....|....*....|....*....|....
gi 1915297335 109 fDKLvallgIEPLLDRlpggLSGGEKQRVAIGRA 142
Cdd:cd03223 82 -EQL-----IYPWDDV----LSGGEQQRLAFARL 105
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-142 |
1.18e-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: 44.17 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 16 TLNE---TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrrvGYVFQDARLfPHYK 92
Cdd:TIGR00957 653 TLNGitfSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------------AYVPQQAWI-QNDS 714
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 93 VRGNLRYGMA--KSMAGQFDKLVALLgiePLLDRLPGG-----------LSGGEKQRVAIGRA 142
Cdd:TIGR00957 715 LRENILFGKAlnEKYYQQVLEACALL---PDLEILPSGdrteigekgvnLSGGQKQRVSLARA 774
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-216 |
1.21e-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: 43.31 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 28 AIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVlndvengicltpekrrvGYVFQDARLFPHyKVRGNLRYGMA----- 102
Cdd:cd03291 67 AITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------------SFSSQFSWIMPG-TIKENIIFGVSydeyr 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 103 -KSM--AGQFDKLVALLgiePLLDRLP---GG--LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLP--YLQ 172
Cdd:cd03291 129 yKSVvkACQLEEDITKF---PEKDNTVlgeGGitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCK 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1915297335 173 RLAREINIpmlYVSHSLdEILHLADKVMVLENGQVKAFGSLEDV 216
Cdd:cd03291 206 LMANKTRI---LVTSKM-EHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-206 |
1.49e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 20 TLPASGITAIFGVSGAGKTSLINAISGLtQPQ---SGRIVLNGRVLndVENGICLTpEKRRVGYVFQDARLFPHYKVRGN 96
Cdd:PRK13549 27 KVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL--QASNIRDT-ERAGIAIIHQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLP---------GGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKREL 167
Cdd:PRK13549 103 IFLGNEITPGGIMDYDAMYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915297335 168 LPYLQRLaREINIPMLYVSHSLDEILHLADKVMVLENGQ 206
Cdd:PRK13549 183 LDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-207 |
1.83e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVENGICltpeKRRVGYVFQDARLFPHyKVRGN 96
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYGMAKSMAGQFDKLvALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PRK10790 435 VTLGRDISEEQVWQAL-ETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1915297335 166 ELLPYLqRLAREiNIPMLYVSHSLDEILHlADKVMVLENGQV 207
Cdd:PRK10790 514 AIQQAL-AAVRE-HTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-141 |
1.99e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVE-------------NGI--CLTPEKrrvgyv 81
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhqdllylghqPGIktELTALE------ 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297335 82 fqdarlfphykvrgNLRYGMAKS-MAGQFDKLVAL--LGIEPLLDRLPGGLSGGEKQRVAIGR 141
Cdd:PRK13538 94 --------------NLRFYQRLHgPGDDEALWEALaqVGLAGFEDVPVRQLSAGQQRRVALAR 142
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
24-125 |
2.67e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.33 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 24 SGITAIFGVSGAGKTSLINAIS-GLTQ--PQSGRIVLNGRVLNDVENGICLTPEK-RRVGYVFQDARLFPHYKVRGNLRY 99
Cdd:pfam13476 18 KGLTLITGPNGSGKTTILDAIKlALYGktSRLKRKSGGGFVKGDIRIGLEGKGKAyVEITFENNDGRYTYAIERSRELSK 97
|
90 100
....*....|....*....|....*.
gi 1915297335 100 GMAKSMAGQFDKLVALLGIEPLLDRL 125
Cdd:pfam13476 98 KKGKTKKKEILEILEIDELQQFISEL 123
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-211 |
3.10e-04 |
|
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: 41.07 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 27 TAIFGVSGAGKTSLINAISGLTQPQ--SGRIVLNGRvlndvENGICLTpekRRVGYVFQDARLFPHYKVRGNLRYGmaks 104
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR-----PLDKNFQ---RSTGYVEQQDVHSPNLTVREALRFS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 105 magqfdklvALLgieplldRlpgGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE------- 177
Cdd:cd03232 104 ---------ALL-------R---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgqailct 164
|
170 180 190
....*....|....*....|....*....|....
gi 1915297335 178 INIPMLYVSHSLDEILHLAdkvmvlENGQVKAFG 211
Cdd:cd03232 165 IHQPSASIFEKFDRLLLLK------RGGKTVYFG 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-141 |
3.25e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLngrvlndvENGIcltpekrRVGYVFQDARLFPHYKVRGNLRYGMAKSMA-- 106
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGI-------KVGYLPQEPQLDPEKTVRENVEEGVAEVKAal 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915297335 107 --------------GQFDKLVALLG-IEPLLD------------------RLPGG------LSGGEKQRVAIGR 141
Cdd:PRK11819 103 drfneiyaayaepdADFDALAAEQGeLQEIIDaadawdldsqleiamdalRCPPWdakvtkLSGGERRRVALCR 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-212 |
5.51e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 23 ASGITAIFGVSGAGKTSLINAISGLTQ----PQSGRIVLNGRVLNDVEngicltPEKR-RVGYVFQDARLFPHYKV---- 93
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIK------KHYRgDVVYNAETDVHFPHLTVgetl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 94 -----------RGNL--RYGMAKSMAgqfDKLVALLGIEPLLDRLPG-----GLSGGEKQRVAIGRALLTAPELLLLDEP 155
Cdd:TIGR00956 160 dfaarcktpqnRPDGvsREEYAKHIA---DVYMATYGLSHTRNTKVGndfvrGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 156 LASLDIPRKRELLPYLQRLAREIN-IPMLYVSHSLDEILHLADKVMVLENGQVKAFGS 212
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-44 |
5.86e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 5.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1915297335 2 LEL-NFSQTLGTHCLTLNetlpaSGITAIFGVSGAGKTSLINAI 44
Cdd:COG0419 5 LRLeNFRSYRDTETIDFD-----DGLNLIVGPNGAGKSTILEAI 43
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-221 |
1.29e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVlngrvlndvengicltpEKRRVGYVFQDARLFpHYKVRGN 96
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------------AERSIAYVPQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 97 LRYgMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKR 165
Cdd:PTZ00243 741 ILF-FDEEDAARLADAVRVSQLEADLAQLGGGleteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297335 166 ELLP--YLQRLAREINIPMLYVSHsldeILHLADKVMVLENGQVKAFGSLEDVWGSSV 221
Cdd:PTZ00243 820 RVVEecFLGALAGKTRVLATHQVH----VVPRADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-139 |
1.77e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 39.05 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGL--TQPQSGRIVLNGRVLNDvengicLTPEKR-RVG--YVFQDARLFPHY 91
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITD------LPPEERaRLGifLAFQYPPEIPGV 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1915297335 92 KVRGNLRYgmaksmagqfdklvallgieplldrLPGGLSGGEKQRVAI 139
Cdd:cd03217 93 KNADFLRY-------------------------VNEGFSGGEKKRNEI 115
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-57 |
3.32e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|...
gi 1915297335 25 GITAIFGVSGAGKTSLINAISGLTQPQSGRIVL 57
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-161 |
4.85e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 37.91 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 31 GVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicltpEKRRVGYVFQDARLFPHYKVRGNLRY--GM----AKS 104
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLENLHFlcGLhgrrAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 105 MAGQFDKLVALLGIEPLLDRlpgGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDI 161
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-142 |
5.41e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.54 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNGRVLNDVEngicLTPEKRRVGYVFQDARLFPHyKVRGN 96
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ----LDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915297335 97 LRYGMAKSMAGQFDKLVALLGIEPLLDRLPGG-----------LSGGEKQRVAIGRA 142
Cdd:PRK10789 409 IALGRPDATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARA 465
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
101-211 |
5.42e-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: 37.55 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 101 MAKSMAGQF---DKLVALLGIEPLLDRLPGGLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLARE 177
Cdd:cd03222 41 AVKILAGQLipnGDNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
90 100 110
....*....|....*....|....*....|....
gi 1915297335 178 INIPMLYVSHSLDEILHLADKVMVLEnGQVKAFG 211
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYG 153
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-59 |
5.49e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 5.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 3 ELNFSQTLGTHCLTLNE---TLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLNG 59
Cdd:PRK13545 26 DLFFRSKDGEYHYALNNisfEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
21-139 |
5.88e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.63 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 21 LPASGITAIFGVSGAGKTSLINAIS----GLTqPQSGRIVLNGRVLNDVENgicltpeKRRVGYVFQdarlfphykvRGN 96
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAITyalyGKT-PRYGRQENLRSVFAPGED-------TAEVSFTFQ----------LGG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1915297335 97 LRYGMAKSM---AGQFDKLVALL--GIEPLLDRLPGGLSGGEKQRVAI 139
Cdd:cd03279 87 KKYRVERSRgldYDQFTRIVLLPqgEFDRFLARPVSTLSGGETFLASL 134
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-214 |
6.07e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.57 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 29 IFGVSGAGKTSLINAISGLTQPQSGRIVLNGrvlNDVENgICLTPEKRRVGYVFQDARLFPHyKVRGNLRYGMAKSMAGQ 108
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDG---CDISK-FGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDADL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 109 FDKLV-ALLgiEPLLDRLPGGL-----------SGGEKQRVAIGRALLTAPELLLLDEPLASLDIpRKRELlpyLQRLAR 176
Cdd:PLN03130 1345 WESLErAHL--KDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDV-RTDAL---IQKTIR 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915297335 177 E--INIPMLYVSHSLDEILHlADKVMVLENGQVKAFGSLE 214
Cdd:PLN03130 1419 EefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPE 1457
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-46 |
8.03e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 8.03e-03
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
28-46 |
9.05e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 36.45 E-value: 9.05e-03
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-204 |
9.25e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 17 LNETLPASGITAIFGVSGAGKTSLINAISGLTQPQSGRIVLN-GRVLNDVEngicLTPEKRRVGYVFQDARLFPHyKVRG 95
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDIN----LKWWRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 96 NLRYGM------------------------------AKSMAGQFDKLVALLGIEPLL----------------------- 122
Cdd:PTZ00265 479 NIKYSLyslkdlealsnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIemrknyqtikdsevvdvskkvli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297335 123 -----------DRLPGG----LSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLAREINIPMLYVSH 187
Cdd:PTZ00265 559 hdfvsalpdkyETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250
....*....|....*..
gi 1915297335 188 SLDEILHlADKVMVLEN 204
Cdd:PTZ00265 639 RLSTIRY-ANTIFVLSN 654
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
28-60 |
9.39e-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: 9.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1915297335 28 AIFGVSGAGKTSLINAIS----------GLTQ-PQSGRIVLNGR 60
Cdd:pfam01926 3 ALVGRPNVGKSTLINALTgakaivsdypGTTRdPNEGRLELKGK 46
|
|
| |
