|
Name |
Accession |
Description |
Interval |
E-value |
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-268 |
2.66e-178 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 491.12 E-value: 2.66e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAHGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRV 160
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKL 240
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250 260
....*....|....*....|....*...
gi 16131352 241 TFSSDAGRVLQNAVLPAFPVRRRTTEKV 268
Cdd:PRK10419 241 TFSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-266 |
1.86e-161 |
|
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: 448.49 E-value: 1.86e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVC 161
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLT 241
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250 260
....*....|....*....|....*
gi 16131352 242 FSSDAGRVLQNAVLPAFPVRRRTTE 266
Cdd:TIGR02769 241 FKHPAGRNLQSAVLPEHPVRRSITT 265
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-261 |
2.64e-114 |
|
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: 328.30 E-value: 2.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGgfngkHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnRA 82
Cdd:COG1124 1 MLEVRNLSVSYGQG-----GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLlslKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCL 162
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKL-T 241
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLaG 229
|
250 260
....*....|....*....|
gi 16131352 242 FSSDAGRVLQNAVlPAFPVR 261
Cdd:COG1124 230 PKHPYTRELLAAS-LAFERA 248
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-233 |
2.21e-109 |
|
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: 315.21 E-value: 2.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGGFngkhqHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRA 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-----SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARAS-EMLKAVDLDDSVLDKRPPQLSGGQLQRVC 161
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-233 |
1.47e-103 |
|
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: 310.30 E-value: 1.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGGFNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGGVR----AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVC 161
Cdd:COG1123 335 RSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-232 |
2.02e-94 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 280.85 E-value: 2.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGG--FNGKHQH-QAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKL 79
Cdd:COG4608 7 LLEVRDLKKHFPVRGglFGRTVGVvKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQR 159
Cdd:COG4608 86 SGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-233 |
2.22e-94 |
|
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: 280.40 E-value: 2.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGgfngKHQHQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESP---AQGNISWRGEPLAKL 79
Cdd:COG0444 1 LLEVRNLKVYFPTR----RGVVKAV-DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 NRAQRKAFR-RDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDD--SVLDKRPPQLSGGQ 156
Cdd:COG0444 76 SEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-232 |
4.37e-86 |
|
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: 266.17 E-value: 4.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYA--HGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLEsPAQGNISWRGEPLAKL 79
Cdd:COG4172 274 PLLEARDLKVWFPikRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMR-HLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQ 158
Cdd:COG4172 353 SRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRvHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-239 |
3.37e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 219.07 E-value: 3.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHY--AHGGFNGKHQHQAvLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAK 78
Cdd:PRK11308 3 QPLLQAIDLKKHYpvKRGLFKPERLVKA-LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQ 158
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqvvGE 238
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK---GT 238
|
.
gi 16131352 239 K 239
Cdd:PRK11308 239 K 239
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-232 |
9.52e-68 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 213.03 E-value: 9.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNP 104
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVREILREPMR-HLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK15079 114 RMTIGEIIAEPLRtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-229 |
6.97e-66 |
|
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: 202.80 E-value: 6.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHggfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaQ 83
Cdd:cd03229 1 LELKNVSKRYGQ---------KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED-E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSisAVNPRKTVREILREPmrhllslkkseqlarasemlkavdlddsvldkrppqLSGGQLQRVCLA 163
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFPHLTVLENIALG------------------------------------LSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
1.78e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 205.33 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLn 80
Cdd:COG3842 3 MPALELENVSKRY--GDV-------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 raqrKAFRRDIQMVFQDSisAVNPRKTVRE-I---LRepMRHLlslKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQ 156
Cdd:COG3842 73 ----PPEKRNVGMVFQDY--ALFPHLTVAEnVafgLR--MRGV---PKAEIRARVAELLELVGLEG-LADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD----LRLverfCQRVMVMDNGQIV 231
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIE 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
2.19e-64 |
|
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: 209.93 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHyahggFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLA----RLLVGLESPAQGNISWRGEPL 76
Cdd:COG4172 4 MPLLSVEDLSVA-----FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 77 AKLNRAQRKAFR-RDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDD--SVLDKRPPQLS 153
Cdd:COG4172 79 LGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDpeRRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-232 |
2.19e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 200.65 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGGfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:COG1136 3 PLLELRNLTKSYGTGE-----GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRD-IQMVFQDSisavN--PRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQ 158
Cdd:COG1136 78 RELARLRRRhIGFVFQFF----NllPELTALENVALPLL-LAGVSRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-232 |
1.00e-63 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 200.45 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYA-HGGFNGKHQHQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKL 79
Cdd:COG4167 2 SALLEVRNLSKTFKyRTGLFRRQQFEAV-KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 NRAQRKafrRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQR 159
Cdd:COG4167 81 DYKYRC---KHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
2.93e-63 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 197.94 E-value: 2.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGgfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraq 83
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQdsisavNPR-----KTVREilrE----PMRhlLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSG 154
Cdd:COG1122 70 LRELRRKVGLVFQ------NPDdqlfaPTVEE---DvafgPEN--LGLPREEIRERVEEALELVGLEH-LADRPPHELSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-241 |
9.96e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 205.14 E-value: 9.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MT-LLNISGLSHHYAHGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPA---QGNISWRGEPL 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGGDV-------PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 77 AKLNRAQRkafRRDIQMVFQDSISAVNPRkTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQ 156
Cdd:COG1123 74 LELSEALR---GRRIGMVFQDPMTQLNPV-TVGDQIAEALE-NLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVV 236
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
....*
gi 16131352 237 GEKLT 241
Cdd:COG1123 228 EEILA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-233 |
1.76e-61 |
|
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: 192.73 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHggfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraq 83
Cdd:cd03259 1 LELKGLSKTYGS---------VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rKAFRRDIQMVFQDSisAVNPRKTVREILREPMRHLLsLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLA 163
Cdd:cd03259 68 -PPERRNIGMVFQDY--ALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-230 |
3.46e-61 |
|
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: 192.32 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:cd03255 1 IELKNLSKTYGGGG-----EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRD-IQMVFQDSisavN--PRKTVREILREPMrHLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRV 160
Cdd:cd03255 76 LAAFRRRhIGFVFQSF----NllPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-232 |
1.06e-60 |
|
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: 191.73 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
Cdd:COG1127 14 SFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 -----DSIsavnprkTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPK 171
Cdd:COG1127 90 ggalfDSL-------TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG-AADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-229 |
3.58e-60 |
|
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: 189.60 E-value: 3.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAHGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrk 85
Cdd:cd03225 2 LKNLSFSYPDGA-------RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 aFRRDIQMVFQdsisavNPR-----KTVREILREPMRHlLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:cd03225 73 -LRRKVGLVFQ------NPDdqffgPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-238 |
3.64e-60 |
|
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: 190.10 E-value: 3.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQD 97
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 sisaVN--PRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:cd03258 91 ----FNllSSRTVFENVALPLE-IAGVPKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
1.20e-58 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 187.22 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAHGGfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLn 80
Cdd:COG1116 5 APALELRGVSKRFPTGG-----GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 raqrkafRRDIQMVFQDsiSAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:COG1116 79 -------GPDRGVVFQE--PALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAG-FEDAYPHQLSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 161 CLARALAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTACLFITHDLRlvE--RFCQRVMVMDN--GQIVE 232
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDaltrERLQ----DELLRLWQETGKTVLFVTHDVD--EavFLADRVVVLSArpGRIVE 221
|
....
gi 16131352 233 TQVV 236
Cdd:COG1116 222 EIDV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-230 |
9.75e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.09 E-value: 9.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQ 96
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DSisaVNPRKTVREILREPMRHLlslKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:COG4619 82 EP---ALWGGTVRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
25-238 |
4.04e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 182.17 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDS--Isav 102
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDFrlL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 nPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:COG2884 92 -PDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:COG2884 169 DPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-233 |
5.62e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.28 E-value: 5.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAHGGfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRK 85
Cdd:COG1135 4 LENLSKTFPTKG--GPVT---ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRDIQMVFQDSisavN--PRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLA 163
Cdd:COG1135 79 AARRKIGMIFQHF----NllSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-232 |
1.25e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 181.35 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAkLNRA 82
Cdd:COG1126 1 MIEIENLHKSF------GDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFRRDIQMVFQDsisaVN--PRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRV 160
Cdd:COG1126 71 DINKLRRKVGMVFQQ----FNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-233 |
2.76e-56 |
|
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: 179.98 E-value: 2.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGFNGKhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaq 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVT-----ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkafrrDIQMVFQDSisAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLA 163
Cdd:cd03293 74 ------DRGYVFQQD--ALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLSGF-ENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVET 233
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-235 |
4.92e-56 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 183.35 E-value: 4.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:COG3839 1 MASLELENVSKSY------GGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAqrkafRRDIQMVFQDsiSAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:COG3839 72 PK-----DRNIAMVFQS--YALYPHMTVYENIAFPLK-LRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlrLVE--RFCQRVMVMDNGQIVetQV 235
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD--QVEamTLADRIAVMNDGRIQ--QV 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
1.42e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.10 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGgfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:COG3638 1 PMLELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRDIQMVFQDSisAVNPRKTVRE-IL------REPMRHLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSG 154
Cdd:COG3638 73 RALRRLRRRIGMIFQQF--NLVPRLSVLTnVLagrlgrTSTWRSLLGLFPPEDRERALEALERVGLAD-KAYQRADQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-232 |
1.18e-54 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 184.14 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHY--AHGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKST----LARLLvglesPAQGNISWRGEP 75
Cdd:PRK15134 274 PLLDVEQLQVAFpiRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 76 LAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMR-HLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSG 154
Cdd:PRK15134 349 LHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-231 |
2.20e-54 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 176.00 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRa 82
Cdd:COG1120 1 MLEAENLSVGY---------GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 qrKAFRRDIQMVFQDSISAVNprKTVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDDsvLDKRP-PQLSGGQLQ 158
Cdd:COG1120 71 --RELARRIAYVPQEPPAPFG--LTVRELValgRYPHLGLFGRPSAEDREAVEEALERTGLEH--LADRPvDELSGGERQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
2.24e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 2.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQ 83
Cdd:COG1131 1 IEVRGLTKRY------GDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSisAVNPRKTVREILREpMRHLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLA 163
Cdd:COG1131 68 PAEVRRRIGYVPQEP--ALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-251 |
3.56e-54 |
|
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: 175.00 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
Cdd:cd03261 9 SFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DsiSAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:cd03261 85 S--GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEklTFSSDAGRVLQ 251
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE--LRASDDPLVRQ 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-232 |
4.15e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.02 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEpLAKLNRAQ 83
Cdd:COG1118 3 IEVRNISKRF--GSF-------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-DLFTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKafrRDIQMVFQDSisAVNPRKTVREILREPMRHLlSLKKSEQLARASEMLKAVDLDDsvLDKR-PPQLSGGQLQRVCL 162
Cdd:COG1118 73 RE---RRVGFVFQHY--ALFPHMTVAENIAFGLRVR-PPSKAEIRARVEELLELVQLEG--LADRyPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-178 |
8.96e-51 |
|
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: 163.59 E-value: 8.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPlakLNRAQRKAFRRDIQMVFQDsiSAVNPRKT 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQD--PQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 108 VREILREP--MRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:pfam00005 76 VRENLRLGllLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
1.25e-50 |
|
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: 166.20 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:cd03256 1 IEVENLSKTYPNGK--------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSisAVNPRKTVRE-IL------REPMRHLLSLKKSEQLARASEMLKAVDLDDSVLdKRPPQLSGGQ 156
Cdd:cd03256 73 LRQLRRQIGMIFQQF--NLIERLSVLEnVLsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAY-QRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-232 |
1.66e-50 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 175.04 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVR 109
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 EILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
Cdd:PRK10261 422 DSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131352 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
4.71e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.88 E-value: 4.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:COG1121 4 MPAIELENLTVSY---------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RA-----QRKAFRRDIQMvfqdsisavnprkTVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDDsvLDKRP-PQ 151
Cdd:COG1121 75 RRigyvpQRAEVDWDFPI-------------TVRDVVlmgRYGRRGLFRRPSRADREAVDEALERVGLED--LADRPiGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
2.01e-49 |
|
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: 162.60 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGGfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:COG4181 7 PIIELRGLTKTVGTGA-----GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRD-IQMVFQDS--IsavnPRKTVREILREPmrhlLSLK-KSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQL 157
Cdd:COG4181 82 DARARLRARhVGFVFQSFqlL----PTLTALENVMLP----LELAgRRDARARARALLERVGLGHR-LDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQ 234
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-238 |
2.05e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 166.13 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAhggfNGKHQHQAvLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRK 85
Cdd:PRK11153 4 LKNISKVFP----QGGRTIHA-LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRDIQMVFQ--DSISAvnprKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLA 163
Cdd:PRK11153 79 KARRQIGMIFQhfNLLSS----RTVFDNVALPLE-LAGTPKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-232 |
8.64e-49 |
|
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: 161.25 E-value: 8.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraqrKAFRRDIQMVFQDSisAVN 103
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPVNTVFQNY--ALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:cd03300 85 PHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-238 |
1.22e-47 |
|
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: 158.48 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnra 82
Cdd:COG4555 1 MIEVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFRRDIQMVFQDSIsaVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCL 162
Cdd:COG4555 68 EPREARRQIGVLPDERG--LYDRLTVRENIRYFAE-LYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-232 |
1.24e-47 |
|
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: 158.11 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLE-----SPAQGNISWRGEPLAK 78
Cdd:cd03260 1 IELRDLNVYY------GDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNrAQRKAFRRDIQMVFQDSisavNP-RKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPP-QLSGGQ 156
Cdd:cd03260 72 LD-VDVLELRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
27-233 |
2.44e-47 |
|
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: 156.65 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraqrKAFRRDIQMVFQDSisAVNPRK 106
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-----PPKDRDIAMVFQNY--ALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:cd03301 88 TVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131352 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:cd03301 166 RVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-231 |
1.31e-46 |
|
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: 156.44 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAHggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGepLAKLNRAQRK 85
Cdd:TIGR04520 3 VENVSFSYPE-------SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRDIQMVFQdsisavNP-----RKTVRE----------ILREPMRHllslkkseqlaRASEMLKAVDLDDsvLDKRPP 150
Cdd:TIGR04520 74 EIRKKVGMVFQ------NPdnqfvGATVEDdvafglenlgVPREEMRK-----------RVDEALKLVGMED--FRDREP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 151 Q-LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQ 229
Cdd:TIGR04520 135 HlLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGK 213
|
..
gi 16131352 230 IV 231
Cdd:TIGR04520 214 IV 215
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-233 |
1.34e-46 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 156.51 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGGFNGKhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRG-----EPLA 77
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVV-----ACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDrdggpRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 78 KLNRAQRKAFRR-DIQMVFQdsisavNPRKTVReilrepMRHLLSLKKSEQL------------ARASEMLKAVDLDDSV 144
Cdd:COG4107 83 ALSEAERRRLRRtDWGMVYQ------NPRDGLR------MDVSAGGNIAERLmaagerhygdirARALEWLERVEIPLER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 145 LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
Cdd:COG4107 151 IDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMV 230
|
....*....
gi 16131352 225 MDNGQIVET 233
Cdd:COG4107 231 MKNGRVVES 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-232 |
3.81e-46 |
|
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: 163.85 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAq 83
Cdd:COG2274 474 IELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkAFRRDIQMVFQDS----------ISAVNPRKTVREILrepmrhllslkkseqlarasEMLKAVDLDDsVLDKRP---- 149
Cdd:COG2274 546 --SLRRQIGVVLQDVflfsgtirenITLGDPDATDEEII--------------------EAARLAGLHD-FIEALPmgyd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 150 -------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRV 222
Cdd:COG2274 603 tvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRI 679
|
250
....*....|
gi 16131352 223 MVMDNGQIVE 232
Cdd:COG2274 680 IVLDKGRIVE 689
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-229 |
6.81e-46 |
|
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: 151.77 E-value: 6.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQD 97
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 SI--SAvnprkTVREILrepmrhllslkkseqlarasemlkavdlddsvldkrppqLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:cd03228 85 PFlfSG-----TIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQ 229
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-230 |
1.50e-45 |
|
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: 152.30 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlNRAQ 83
Cdd:cd03262 1 IEIKNLHKSF------GDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDsisaVN--PRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVC 161
Cdd:cd03262 71 INELRQKVGMVFQQ----FNlfPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-229 |
3.11e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 149.32 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkafRRDIQMVFQdsis 100
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 avnprktvreilrepmrhllslkkseqlarasemlkavdlddsvldkrppqLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-230 |
7.71e-45 |
|
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: 149.08 E-value: 7.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQ 83
Cdd:cd03230 1 IEVRNLSKRY------GKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSisAVNPRKTVREILRepmrhllslkkseqlarasemlkavdlddsvldkrppqLSGGQLQRVCLA 163
Cdd:cd03230 68 PEEVKRRIGYLPEEP--SLYENLTVRENLK--------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-231 |
8.98e-45 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 149.12 E-value: 8.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkafRRDIQMVFQdsis 100
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 avnprktvreilrepmrhllslkkseqlaraseMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:cd03214 81 ---------------------------------ALELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-228 |
2.41e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 148.84 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR-----AQRKAFRRDIQMvfqdsisa 101
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrigyvPQRRSIDRDFPI-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 vnprkTVREI----LREPMRHLLSLKKSEQlARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:cd03235 86 -----SVRDVvlmgLYGHKGLFRRLSKADK-AKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNG 228
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-232 |
2.87e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 150.71 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSH--HYAHGGFngKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKL 79
Cdd:PRK15112 3 TLLEVRNLSKtfRYRTGWF--RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 N---RAQRkafrrdIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQ 156
Cdd:PRK15112 81 DysyRSQR------IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-232 |
2.99e-44 |
|
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: 149.76 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdSIs 100
Cdd:cd03295 11 GGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKIGYVIQ-QI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVRE-ILREPmrHLLSLKKSEQLARASEMLKAVDLDD-SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:cd03295 85 GLFPHMTVEEnIALVP--KLLKWPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-232 |
3.18e-44 |
|
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: 150.49 E-value: 3.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRR-DIQMVFQDsiSAVNPRK 106
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMrHLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:cd03294 118 TVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-232 |
6.99e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 151.80 E-value: 6.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraqRKAFRRDIQMVFQDSisAVNPRK 106
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-----RSIQQRDICMVFQSY--ALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRhLLSLKKSEQLARASEMLKAVDLD---DSVLDkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK11432 94 SLGENVGYGLK-MLGVPKEERKQRVKEALELVDLAgfeDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 184 LVLQAGVIRLLKKLQQQFGTACLFITHDlrLVERFC--QRVMVMDNGQIVE 232
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHD--QSEAFAvsDTVIVMNKGKIMQ 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-231 |
2.58e-43 |
|
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: 147.44 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAhggfNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRA 82
Cdd:TIGR02315 1 MLEVENLSKVYP----NGKQ----ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFRRDIQMVFQDSisAVNPRKTVREILREP-------MRHLLSLKKSEQLARASEMLKAVDLDDSVLdKRPPQLSGG 155
Cdd:TIGR02315 73 KLRKLRRRIGMIFQHY--NLIERLTVLENVLHGrlgykptWRSLLGRFSEEDKERALSALERVGLADKAY-QRADQLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-233 |
3.37e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 147.08 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPL---AKLNRAQRKAFRRDIQMV 94
Cdd:PRK11124 11 FYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 FQDsisaVN--PRKTVREILRE-PMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPK 171
Cdd:PRK11124 88 FQQ----YNlwPHLTVQQNLIEaPCR-VLGLSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
24-229 |
3.56e-43 |
|
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: 146.24 E-value: 3.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDSisAVN 103
Cdd:TIGR02673 14 GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRIGVVFQDF--RLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:TIGR02673 92 PDRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLEHK-ADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 184 LVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:TIGR02673 170 PDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-230 |
3.80e-43 |
|
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: 146.72 E-value: 3.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaklNRAQRKAFRRDIQMVFQDsiSAVNPRKT 107
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE-----DATDVPVQERNVGFVFQH--YALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREI----LRepMRHLLSLK-KSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:cd03296 91 VFDNvafgLR--VKPRSERPpEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131352 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-231 |
1.12e-42 |
|
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: 144.75 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLkSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklNRAQRKAF----RRDIQMVFQDSisAVNPR 105
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL---FDSRKKINlppqQRKIGLVFQQY--ALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRhllSLKKSEQLARASEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:cd03297 90 LNVRENLAFGLK---RKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
32-231 |
1.33e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.28 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 32 SLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKafrrdIQMVFQDSisavN--PRKTVR 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-----VSMLFQEN----NlfPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 E-I---LREPMRhlLSlkkSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:COG3840 90 QnIglgLRPGLK--LT---AEQRAQVEQALERVGLAG-LLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-231 |
3.70e-42 |
|
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: 143.17 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAHGGFngkhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnraqRK 85
Cdd:cd03226 2 IENISFSYKKGTE--------ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRDIQMVFQDSISAVNpRKTVREILRepmrhlLSLK-KSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLAR 164
Cdd:cd03226 68 ERRKSIGYVMQDVDYQLF-TDSVREELL------LGLKeLDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
4.51e-42 |
|
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: 144.41 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:COG0411 2 DPLLEVRGLTKRF--GGL-------VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAQRkaFRRDIQMVFQdsISAVNPRKTVRE------------ILREPMRHLLSLKKSEQ--LARASEMLKAVDLDDsVLD 146
Cdd:COG0411 73 PHRI--ARLGIARTFQ--NPRLFPELTVLEnvlvaaharlgrGLLAALLRLPRARREEReaRERAEELLERVGLAD-RAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
....*
gi 16131352 227 NGQIV 231
Cdd:COG0411 228 FGRVI 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-231 |
6.71e-42 |
|
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: 146.78 E-value: 6.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLakLNRAQR---KAFRRDIQMVFQDSisAVNPRK 106
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGiflPPHRRRIGYVFQEA--RLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLKKSEQLARASEMLKAVDLddsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVVELLGIGHL----LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-233 |
5.20e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.92 E-value: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAhggfnGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAK-- 78
Cdd:COG4525 1 MSMLTVRHVSVRYP-----GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNRAqrkafrrdiqMVFQDSisAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQ 158
Cdd:COG4525 76 ADRG----------VVFQKD--ALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLAD-FARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL--------RLVerfcqrVMVMDNGQI 230
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeealflatRLV------VMSPGPGRI 215
|
...
gi 16131352 231 VET 233
Cdd:COG4525 216 VER 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-232 |
8.16e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.92 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPL---AKLNRAQRKAFRRDIQMV 94
Cdd:COG4161 11 FYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 FQDsisaVN--PRKTVREILRE-PMRhLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPK 171
Cdd:COG4161 88 FQQ----YNlwPHLTVMENLIEaPCK-VLGLSKEQAREKAMKLLARLRLTDK-ADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-232 |
1.18e-40 |
|
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: 140.16 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkafRRDIQMVFQDSisAVNPRK 106
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNY--ALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLKKS--EQLARASEMLKAvdldDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEieRKVLEIAEMLGI----DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131352 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-233 |
1.38e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 142.57 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAhggfNGKHQHQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-ESPAQ---GNISWRGEPL 76
Cdd:PRK11022 1 MALLNVDKLSVHFG----DESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGRvmaEKLEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 77 AKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDD--SVLDKRPPQLS 153
Cdd:PRK11022 76 QRISeKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-233 |
2.66e-40 |
|
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: 146.44 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkafRRDIQMVFQDSisaV 102
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNP---Y 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVREILRepmrhllsLKKS----EQLARAsemLKAVDLD----------DSVLDKRPPQLSGGQLQRVCLARALAV 168
Cdd:COG4988 422 LFAGTIRENLR--------LGRPdasdEELEAA---LEAAGLDefvaalpdglDTPLGEGGRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQ 552
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-231 |
5.00e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.10 E-value: 5.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHggfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRA 82
Cdd:COG4559 1 MLEAENLSVRLGG---------RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRkAFRRdiqmvfqdsisAVNPRK-------TVREIL---REPmrHLLSLKKSEQLARasEMLKAVDLDDsvLDKRP-PQ 151
Cdd:COG4559 72 EL-ARRR-----------AVLPQHsslafpfTVEEVValgRAP--HGSSAAQDRQIVR--EALALVGLAH--LAGRSyQT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALA-------VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMV 224
Cdd:COG4559 134 LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILL 212
|
....*..
gi 16131352 225 MDNGQIV 231
Cdd:COG4559 213 LHQGRLV 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-232 |
6.08e-40 |
|
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: 145.29 E-value: 6.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:COG4987 334 LELEDVSFRYPGAG-------RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RkafRRDIQMVFQDS--ISAvnprkTVREILRepmrhllslkkseqLAR--ASE-----MLKAVDLDDsVLDKRPP---- 150
Cdd:COG4987 407 L---RRRIAVVPQRPhlFDT-----TLRENLR--------------LARpdATDeelwaALERVGLGD-WLAALPDgldt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 151 -------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFcQRVM 223
Cdd:COG4987 464 wlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRIL 540
|
....*....
gi 16131352 224 VMDNGQIVE 232
Cdd:COG4987 541 VLEDGRIVE 549
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
1.14e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 141.24 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLn 80
Cdd:PRK09452 12 SPLVELRGISKSF---------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 raqrKAFRRDIQMVFQDsiSAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:PRK09452 82 ----PAENRHVNTVFQS--YALFPHMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLEE-FAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
1.44e-39 |
|
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: 137.57 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:cd03219 1 LEVRGLTKRF--GGL-------VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RkaFRRDIQMVFQdsISAVNPRKTVRE--------ILREPMRHLLSLKKSEQL-ARASEMLKAVDLDDsVLDKRPPQLSG 154
Cdd:cd03219 72 I--ARLGIGRTFQ--IPRLFPELTVLEnvmvaaqaRTGSGLLLARARREEREArERAEELLERVGLAD-LADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
2.42e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 143.31 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAHGGfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLA-RLLVGLESPA----QGNISWRGEP 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQ-----TVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPvvypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 76 LAKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREILREpmrhLLSLKK--SEQLARAsEMLKAVDL-----DDSVLDK 147
Cdd:PRK15134 78 LLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYE----VLSLHRgmRREAARG-EILNCLDRvgirqAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
....*..
gi 16131352 228 GQIVETQ 234
Cdd:PRK15134 233 GRCVEQN 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
26-232 |
3.11e-39 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 139.09 E-value: 3.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESpAQGNIS----WRGEPLAKLNRAQRKAFR-RDIQMVFQDSIS 100
Cdd:PRK09473 31 AV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGgsatFNGREILNLPEKELNKLRaEQISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSvlDKR----PPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEA--RKRmkmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
3.15e-39 |
|
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: 134.09 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahGGFngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaq 83
Cdd:cd03216 1 LELRGITKRF--GGV-------KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQdsisavnprktvreilrepmrhllslkkseqlarasemlkavdlddsvldkrppqLSGGQLQRVCLA 163
Cdd:cd03216 70 RDARRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-231 |
5.73e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.44 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkAFRRdiqmvfqdsisAVN 103
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL-ARRR-----------AVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRK-------TVREIL---REPmrHLLSLKKSEQLARAseMLKAVDLDDsvLDKRP-PQLSGGQLQRVCLARALA----- 167
Cdd:PRK13548 82 PQHsslsfpfTVEEVVamgRAP--HGLSRAEDDALVAA--ALAQVDLAH--LAGRDyPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 168 -VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-238 |
7.42e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.20 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraqrKAFRRDIQMVFQD 97
Cdd:PRK11607 29 FDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 siSAVNPRKTVREILREPMRHlLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:PRK11607 100 --YALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 178 AVSNLDLVL----QAGVIRLLKKLqqqfGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqvVGE 238
Cdd:PRK11607 176 PMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ---IGE 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-238 |
2.24e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 141.92 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHggfngKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR- 81
Cdd:PRK10261 12 VLAVENLNIAFMQ-----EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 ---------AQRKAFR-RDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDS--VLDKRP 149
Cdd:PRK10261 87 vielseqsaAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAqtILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
....*....
gi 16131352 230 IVETQVVGE 238
Cdd:PRK10261 247 AVETGSVEQ 255
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-230 |
2.32e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.52 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKA---------FRrdiQMV 94
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVgfvfqhyalFR---HMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 FQDSIS---AVNPRKT--VREILREPMRHLLSLKKSEQLArasemlkavdlddsvlDKRPPQLSGGQLQRVCLARALAVE 169
Cdd:PRK10851 91 VFDNIAfglTVLPRRErpNAAAIKAKVTQLLEMVQLAHLA----------------DRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-268 |
6.46e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 6.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkAFRRDIQMVFQDsISAVnPRK 106
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD--AQAAGIAIIHQE-LNLV-PNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVRE---ILREPMRHLLsLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:COG1129 95 SVAEnifLGREPRRGGL-IDWRAMRRRARELLARLGLDIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 184 lvlQAGVIRLLK---KLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEkltFSSDA------GRVLQNav 254
Cdd:COG1129 173 ---EREVERLFRiirRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE---LTEDElvrlmvGRELED-- 243
|
250
....*....|....
gi 16131352 255 lpAFPVRRRTTEKV 268
Cdd:COG1129 244 --LFPKRAAAPGEV 255
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-230 |
1.30e-37 |
|
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: 131.76 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDsiSAVNPR 105
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:cd03292 93 RNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03292 171 TTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-230 |
1.42e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 132.25 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYAHGGFngkhqHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRA 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSV-----QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAFR-RDIQMVFQdsISAVNPRKTVREILREPMrhLLSLKKSEQL-ARASEMLKAVDLDDSVlDKRPPQLSGGQLQRV 160
Cdd:PRK11629 80 AKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPL--LIGKKKPAEInSRALEMLAAVGLEHRA-NHRPSELSGGERQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQI 230
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
27-233 |
2.06e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 134.26 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESP----AQGNISWRGEPLAKLNRAQRKAF-RRDIQMVFQDSISA 101
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIiGREIAMIFQEPSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 VNPRKTVREILREPMRHLlSLK------KSEQLARASEMLKAVDLDD--SVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
Cdd:COG4170 102 LDPSAKIGDQLIEAIPSW-TFKgkwwqrFKWRKKRAIELLHRVGIKDhkDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-232 |
2.65e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 138.37 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQDSI--SAvnp 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE---SLRRQIGVVPQDTFlfSG--- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rkTVREILRepmrhlLSLKKS--EQLARAsemLKAVDLD----------DSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
Cdd:COG1132 429 --TIRENIR------YGRPDAtdEEVEEA---AKAAQAHefiealpdgyDTVVGERGVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 173 LILDEAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
Cdd:COG1132 498 LILDEATSALDteteALIQEALERLMK------GRTTIVIAHRLSTI-RNADRILVLDDGRIVE 554
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-232 |
2.53e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQd 97
Cdd:PRK13635 13 FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD---VRRQVGMVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 sisavNPRK-----TVRE----------ILREPMrhllslkkseqLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCL 162
Cdd:PRK13635 89 -----NPDNqfvgaTVQDdvafglenigVPREEM-----------VERVDQALRQVGMED-FLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-230 |
2.88e-36 |
|
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: 131.77 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 31 VSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAK-LNRAQRKAFRRDIQMVFQDSisAVNPRKTVR 109
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsRKGIFLPPEKRRIGYVFQEA--RLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 EILREPMRHLLSLKKSEQLARASEMLKAvdldDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131352 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-230 |
3.60e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 131.50 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAhggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:PRK11650 1 MAGLKLQAVRKSYD-----GKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAQRkafrrDIQMVFQDSisAVNPRKTVREILRepmrhlLSLK-----KSEQLARASEMLKAVDLDDsVLDKRPPQLSGG 155
Cdd:PRK11650 73 PADR-----DIAMVFQNY--ALYPHMSVRENMA------YGLKirgmpKAEIEERVAEAARILELEP-LLDRKPRELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGvIRL-LKKLQQQFGTACLFITHDlrLVE--RFCQRVMVMDNGQI 230
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHD--QVEamTLADRVVVMNGGVA 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
27-222 |
7.99e-36 |
|
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: 126.82 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnRAQRKAFRRDIQMVFQDSisAVNPRK 106
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRLAYLGHAD--GLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILRepmrHLLSLKKSEQ-LARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlv 185
Cdd:COG4133 91 TVRENLR----FWAALYGLRAdREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD-- 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131352 186 lQAGVIRLLKKLQQ--QFGTACLFITHDLRLVErFCQRV 222
Cdd:COG4133 164 -AAGVALLAELIAAhlARGGAVLLTTHQPLELA-AARVL 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-238 |
1.47e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 127.51 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPA----QGNISWRGEPLAKlnraqrKAFR-RDIQMVFQDS 98
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAP------CALRgRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 ISAVNPRKTVREILREPmrhLLSLKKSEQLARASEMLKAVDLDDS--VLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:PRK10418 89 RSAFNPLHTMHTHARET---CLALGKPADDATLTAALEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-230 |
1.76e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.49 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHggfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnr 81
Cdd:PRK11247 11 TPLLLNAVSKRYGE---------RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 aqrkafRRDIQMVFQDsiSAVNPRKTVREILRepmrhlLSLKKSEQlARASEMLKAVDLDDSVLDkRPPQLSGGQLQRVC 161
Cdd:PRK11247 80 ------REDTRLMFQD--ARLLPWKKVIDNVG------LGLKGQWR-DAALQALAAVGLADRANE-WPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
9.03e-35 |
|
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: 124.54 E-value: 9.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahgGFNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnRAQ 83
Cdd:cd03263 1 LQIRNLTKTY---KKGTKP----AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSIsaVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLA 163
Cdd:cd03263 70 RKAARQSLGYCPQFDA--LFDELTVREHLRFYAR-LKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-228 |
2.40e-34 |
|
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: 123.73 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrkafrrDIQMVFQDSisAVNPRKT 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP--------DRMVVFQNY--SLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VRE-ILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:TIGR01184 71 VREnIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131352 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-231 |
3.26e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.22 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 20 GKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ-------Rkafrrdiq 92
Cdd:COG4152 12 GDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 93 mvfqdsisAVNPRKTVREILRepmrHLLSLK---KSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVE 169
Cdd:COG4152 81 --------GLYPKMKVGEQLV----YLARLKglsKAEAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-231 |
4.11e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsisav 102
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---IRKKIGIIFQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRK-----TV----------REILREPMRhllslKKSEQLArasemlKAVDLDDsVLDKRPPQLSGGQLQRVCLARALA 167
Cdd:PRK13632 91 NPDNqfigaTVeddiafglenKKVPPKKMK-----DIIDDLA------KKVGMED-YLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLF-ITHDLRLVERfCQRVMVMDNGQIV 231
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKT-RKKTLIsITHDMDEAIL-ADKVIVFSEGKLI 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-230 |
5.39e-34 |
|
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: 121.17 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQDsisavnp 104
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDHVGYLPQD------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rktvreilrepmrhllslkksEQLarasemlkavdLDDSVLDKrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:cd03246 85 ---------------------DEL-----------FSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 185 VLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERfCQRVMVMDNGQI 230
Cdd:cd03246 130 EGERALNQAIAALKAAGATR-IVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-231 |
7.14e-34 |
|
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: 121.92 E-value: 7.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGgfngkhqhqAVLNNVSLTLKSGETvALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnRAQ 83
Cdd:cd03264 1 LQLENLTKRYGKK---------RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSisAVNPRKTVREILRepmrHLLSLK---KSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:cd03264 67 PQKLRRRIGYLPQEF--GVYPNFTVREFLD----YIAWLKgipSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-232 |
8.48e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 122.19 E-value: 8.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 11 HHYAHGGFNGKHQhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFR-R 89
Cdd:PRK10584 10 HHLKKSVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 90 DIQMVFQDS--ISAVNPRKTVR--EILREPmrhllSLKKSEQlaRASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARA 165
Cdd:PRK10584 89 HVGFVFQSFmlIPTLNALENVElpALLRGE-----SSRQSRN--GAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-233 |
2.71e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.44 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrGEPL--AKLNRAQRKAFRRDIQMVFQDSISAVNPR 105
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPLRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRhlLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK13634 102 TVEKDICFGPMN--FGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131352 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-231 |
2.77e-33 |
|
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: 120.62 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:cd03224 1 LEVENLNAGY------GKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RkaFRRDIQMVFQDsiSAVNPRKTVREILREPMRHLLSLKKSEQLARASEM---LKAvdlddsVLDKRPPQLSGGQLQRV 160
Cdd:cd03224 72 R--ARAGIGYVPEG--RRIFPELTVEENLLLGAYARRRAKRKARLERVYELfprLKE------RRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
28-238 |
3.15e-33 |
|
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: 120.55 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQRKAFRRDIQMVFQDSisAVNPRKT 107
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRIGIVFQDL--SVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREILrEPMRHLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
Cdd:cd03265 90 GWENL-YIHARLYGVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-232 |
6.19e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGE--------- 74
Cdd:PRK10619 6 LNVIDLHKRY------GEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 75 -PLAKLNRAQRKAFRRDIQMVFQDSisAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLS 153
Cdd:PRK10619 77 gQLKVADKNQLRLLRTRLTMVFQHF--NLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-231 |
9.55e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.35 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQR---------------------K 85
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRDIQMVFQDSISAVNPRKTVREILREPMRhlLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARA 165
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVS--MGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-233 |
1.01e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.03 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahGGFNGkhqhqavLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGE-----PLA 77
Cdd:PRK11701 6 LLSVRGLTKLY--GPRKG-------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 78 KLNRAQRKA-FRRDIQMVFQdsisavNPRKTVR-------EILREPM----RHLLSLKkseqlARASEMLKAVDLDDSVL 145
Cdd:PRK11701 77 ALSEAERRRlLRTEWGFVHQ------HPRDGLRmqvsaggNIGERLMavgaRHYGDIR-----ATAGDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 146 DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
....*...
gi 16131352 226 DNGQIVET 233
Cdd:PRK11701 226 KQGRVVES 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-233 |
1.32e-32 |
|
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: 119.25 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraqRKAFRRDIQMVFQ 96
Cdd:cd03254 11 SYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DSISAvnpRKTVREILRepMRHLLSLKKSEQLArasemLKAVDLD----------DSVLDKRPPQLSGGQLQRVCLARAL 166
Cdd:cd03254 85 DTFLF---SGTIMENIR--LGRPNATDEEVIEA-----AKEAGAHdfimklpngyDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 167 AVEPKLLILDEAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
Cdd:cd03254 155 LRDPKILILDEATSNIDteteKLIQEALEKLMK------GRTSIIIAHRLSTI-KNADKILVLDDGKIIEE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
27-238 |
1.33e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.57 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaKLNRAQRKAFRRDIQMVFQ---DSISAvn 103
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQnpdDQLFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 prKTVRE-ILREPMRhlLSLKKSEQLARASEMLKAVDLDDSvlDKRPPQ-LSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:PRK13639 94 --PTVEEdVAFGPLN--LGLSKEEVEKRVKEALKAVGMEGF--ENKPPHhLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-231 |
1.43e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYAHGG-FNGKhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlNRAQR 84
Cdd:PRK13637 5 IENLTHIYMEGTpFEKK-----ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 85 KAFRRDIQMVFQDSISAVNPRKTVREILREPMRhlLSLKKSEQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLA 163
Cdd:PRK13637 79 SDIRKKVGLVFQYPEYQLFEETIEKDIAFGPIN--LGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-232 |
1.88e-32 |
|
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: 118.87 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQDSI-----S 100
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVFlfndtV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVREILREPMRHLLslkkseQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:cd03251 93 AENIAYGRPGATREEVEEAA------RAANAHEFIMELPEGyDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:cd03251 167 SALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-232 |
2.96e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.66 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPlAKLNRAQRKAFRRDIQMVFQDSisAVN 103
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-VNDPKVDERLIRQEAGMVFQQF--YLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK09493 90 PHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 184 LVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-232 |
3.31e-32 |
|
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: 118.36 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQDSisaVNPRK 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQVGVVLQEN---VLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVRE--ILREPMRHLLSLKKSEQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:cd03252 91 SIRDniALADPGMSMERVIEAAKLAGAHDFISELPEGyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 184 LVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
27-231 |
4.25e-32 |
|
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: 117.38 E-value: 4.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnraqrKAFRRDIQMVFQDsiSAVNPRK 106
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRIGYLPEE--RGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:cd03269 86 KVIDQLVYLAQ-LKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 187 QAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03269 164 VELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-232 |
1.25e-31 |
|
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: 116.95 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraQRKAFRRDIQMVFQDS--- 98
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAIGVVPQDTvlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 -------ISAVNPRKTVREIlrepmrhllslkksEQLARAS----EMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
Cdd:cd03253 88 ndtigynIRYGRPDATDEEV--------------IEAAKAAqihdKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-231 |
1.44e-31 |
|
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: 116.66 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 16 GGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQRKAFRRDIQMVF 95
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK----RRKKFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 96 -QDS-----ISAVNPRKTVREILREPMRHLlslkkSEQLARASEMLKAVDLddsvLDKRPPQLSGGQLQRVCLARALAVE 169
Cdd:cd03267 101 gQKTqlwwdLPVIDSFYLLAAIYDLPPARF-----KKRLDELSELLDLEEL----LDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-231 |
3.65e-31 |
|
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: 115.46 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLn 80
Cdd:COG0410 1 MPMLEVENLHAGY------GGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAQRKAfRRDIQMVFQDSisAVNPRKTVREILREPMRHLLSLKKSEQ-LARASEMLkavdlddSVLDKRPPQ----LSGG 155
Cdd:COG0410 71 PPHRIA-RLGIGYVPEGR--RIFPSLTVEENLLLGAYARRDRAEVRAdLERVYELF-------PRLKERRRQragtLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-230 |
4.05e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsis 100
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD---IRHKIGMVFQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 avNPRK-----TVREILREPMRHLlSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:PRK13650 89 --NPDNqfvgaTVEDDVAFGLENK-GIPHEEMKERVNEALELVGMQD-FKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVErFCQRVMVMDNGQI 230
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-232 |
4.54e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAvLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRG-EPLAKLNRAQRKAFRRDIQMVFQDSIS 100
Cdd:PRK13646 18 YEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVREILREPMRHLLSLKKSEqlARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:PRK13646 97 QLFEDTVEREIIFGPKNFKMNLDEVK--NYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
27-233 |
5.54e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.22 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQDS-------- 98
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQ---AVRRQLGVVLQNGrlmsgsif 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 --ISAVNPrktvreilrepmrhlLSLKKSEQLARASEMlkAVDLDD------SVLDKRPPQLSGGQLQRVCLARALAVEP 170
Cdd:TIGR03797 545 enIAGGAP---------------LTLDEAWEAARMAGL--AEDIRAmpmgmhTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVeRFCQRVMVMDNGQIVET 233
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLERLK---VTR-IVIAHRLSTI-RNADRIYVLDAGRVVQQ 665
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-231 |
5.81e-31 |
|
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: 114.39 E-value: 5.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 15 HGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplAKLNRAQRKAFRRdiqMV 94
Cdd:cd03266 8 TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEARRR---LG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 FQDSISAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAG-LYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-231 |
6.29e-31 |
|
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: 114.61 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkafRRDIQMVFQDS--IS 100
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVtlFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AvnprkTVREILRepMRHLLSlkKSEQLARASEMLKAVDL-------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
Cdd:cd03245 92 G-----TLRDNIT--LGAPLA--DDERILRAAELAGVTDFvnkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 174 ILDEAVSNLDLVLQAgviRLLKKLQQQFGT-ACLFITHDLRLVErFCQRVMVMDNGQIV 231
Cdd:cd03245 163 LLDEPTSAMDMNSEE---RLKERLRQLLGDkTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-212 |
6.75e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.57 E-value: 6.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNrA 82
Cdd:PRK11248 1 MLQISHLYADY---------GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKafrrdiqMVFQDsiSAVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSvlDKRPP-QLSGGQLQRVC 161
Cdd:PRK11248 71 ERG-------VVFQN--EGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGA--EKRYIwQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-232 |
1.12e-30 |
|
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: 112.79 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAfrrdiqmvfqd 97
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 sISAVNPRKtvreilrepmrHLlslkkseqlarasemlkavdLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:cd03247 77 -ISVLNQRP-----------YL--------------------FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 178 AVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQIVE 232
Cdd:cd03247 125 PTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-233 |
1.18e-30 |
|
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: 114.17 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRDIQMVFQDSISAVNprk 106
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL---RWLRSQIGLVSQEPVLFDG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILR--EPMRHLLSLKKSEQLARASEMLKAV-DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:cd03249 92 TIAENIRygKPDATDEEVEEAAKKANIHDFIMSLpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 184 ----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
Cdd:cd03249 172 aeseKLVQEALDRAMK------GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQ 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-229 |
1.68e-30 |
|
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: 113.68 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHyahggFNGKHQHQA---VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRgEPLAK 78
Cdd:COG4778 3 TLLEVENLSKT-----FTLHLQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNRAQrkAFRRDIQMVFQDSISAVN------PRKTVREILREPMRHLlSLKKSEQLARASEMLKAVDLDDSVLDKRPPQL 152
Cdd:COG4778 77 VDLAQ--ASPREILALRRRTIGYVSqflrviPRVSALDVVAEPLLER-GVDREEARARARELLARLNLPERLWDLPPATF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-231 |
2.76e-30 |
|
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: 118.70 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDI----QMV--FQ 96
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRHIgylpQDVelFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DSISA-------VNPRKTVreilrepmrhllslkKSEQLARASEM-LKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAV 168
Cdd:COG4618 420 GTIAEniarfgdADPEKVV---------------AAAKLAGVHEMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
6.68e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 6.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAhggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:PRK13652 1 MHLIETRDLCYSYS--------GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RaqrKAFRRDIQMVFQDSISAVNPRKTVREILREPMRhlLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRV 160
Cdd:PRK13652 73 I---REVRKFVGLVFQNPDDQIFSPTVEQDIAFGPIN--LGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-232 |
1.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.00 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPL-AKLNRAQRKAFRRDIQMVFQDSISAVNPRK 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPmrhlLSLKKSEQLAR--ASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:PRK13641 103 VLKDVEFGP----KNFGFSEDEAKekALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131352 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-231 |
1.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.92 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQR-KAFRRDIQMVFQDSISAVNPRK 106
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDiKQIRKKVGLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLKKSEQLARasEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 187 QAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-235 |
1.14e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.12 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNprKT 107
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD--RT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREILREPMrhLLSLKKSEQL-ARASEMLKAVDLddsvLDKR---PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK10908 96 VYDNVAIPL--IIAGASGDDIrRRVSAALDKVGL----LDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 184 LVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQV 235
Cdd:PRK10908 170 DALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-234 |
1.14e-29 |
|
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: 111.05 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 32 SLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkafRRDIQMVFQDSisAVNPRKTVRE- 110
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQEN--NLFAHLTVEQn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 111 --ILREPMRHLlslkKSEQLARASEMLKAVDLDDsvLDKR-PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
Cdd:cd03298 91 vgLGLSPGLKL----TAEDRQAIEVALARVGLAG--LEKRlPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131352 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-232 |
1.60e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.46 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 3 LLNISGLSHHYahggfngKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRA 82
Cdd:PRK11160 338 SLTLNNVSFTY-------PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 83 QRKAfrrdiqmvfqdSISAVNPR-----KTVREILrepmrhLLSLKKS--EQLaraSEMLKAVDLdDSVLDKRPP----- 150
Cdd:PRK11160 411 ALRQ-----------AISVVSQRvhlfsATLRDNL------LLAAPNAsdEAL---IEVLQQVGL-EKLLEDDKGlnawl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 151 -----QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFcQRVMVM 225
Cdd:PRK11160 470 geggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVM 546
|
....*..
gi 16131352 226 DNGQIVE 232
Cdd:PRK11160 547 DNGQIIE 553
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-239 |
1.65e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.29 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplAKLNRAQRKAFRR-------DIQMvF 95
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDRETFGKhigylpqDVEL-F 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 96 QDSISA--------VNPRKTVreilrepmrhllslkKSEQLARASEM-LKAVDLDDSVLDKRPPQLSGGQLQRVCLARAL 166
Cdd:TIGR01842 405 PGTVAEniarfgenADPEKII---------------EAAKLAGVHELiLRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVErFCQRVMVMDNGQIvetQVVGEK 239
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITV-VVITHRPSLLG-CVDKILVLQDGRI---ARFGER 537
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
3.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAhggfNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaKLNR 81
Cdd:PRK13636 4 YILKVEELNYNYS----DGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRhlLSLKKSEQLARASEMLKAVDLddSVLDKRPPQ-LSGGQLQRV 160
Cdd:PRK13636 75 KGLMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVN--LKLPEDEVRKRVDNALKRTGI--EHLKDKPTHcLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-232 |
4.79e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.22 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISW------RGEPLAKlNRAQRKAFRRDI 91
Cdd:PRK11264 13 FHG----QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQ-QKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 92 QMVFQDSisAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPK 171
Cdd:PRK11264 88 GFVFQNF--NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLfITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
27-233 |
5.27e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.16 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLES--PAQGNISWRGEPLAKLN---RAqrkafRRDIQMVFQD--SI 99
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSpdeRA-----RAGIFLAFQYpvEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SAVnprkTVREILREPM--RHLLSLKKSEQLARASEMLKAVDLDDSVLDkRP--PQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:COG0396 90 PGV----SVSNFLRTALnaRRGEELSAREFLKLLKEKMKELGLDEDFLD-RYvnEGFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 176 DEAVSNLDL-VLQAgVIRLLKKLQQQfGTACLFITHDLRLVERF-CQRVMVMDNGQIVET 233
Cdd:COG0396 165 DETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVDGRIVKS 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-232 |
5.55e-29 |
|
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: 109.51 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraqRKAFRRDIQMVFQDsisAVNPRK 106
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQD---PVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPmrhlLSLKKSEQLARASEM--LKAV-----DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:cd03244 93 TIRSNL-DP----FGEYSDEELWQALERvgLKEFveslpGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 180 SNLDLVLQAgviRLLKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:cd03244 168 ASVDPETDA---LIQKTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-233 |
9.82e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.10 E-value: 9.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQ-AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWR--------GEPLAKLNRAQRK--- 85
Cdd:PRK13631 31 FDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSKKikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 --AFRRDIQMVFQ--------DSISavnprktvREILREPMRhlLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGG 155
Cdd:PRK13631 111 fkELRRRVSMVFQfpeyqlfkDTIE--------KDIMFGPVA--LGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-238 |
1.28e-28 |
|
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: 113.74 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWR-GEP---LAKLNRAQRKAFRRDIQMVFQDSisAVN 103
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPDGRGRAKRYIGILHQEY--DLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPmrhlLSLKKSEQLAR--ASEMLKAVDLDD----SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:TIGR03269 378 PHRTVLDNLTEA----IGLELPDELARmkAVITLKMVGFDEekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET----QVVGE 238
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIgdpeEIVEE 518
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-231 |
1.88e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR---AQRKAFRRDIQMVFQDS 98
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 isavnprkTVREIL---REPMRHL---LSLKKSEQLARASEMLKAVDLddsvLDKRPPQLSGGQLQRVCLARALAVEPKL 172
Cdd:PRK11231 92 --------TVRELVaygRSPWLSLwgrLSAEDNARVNQAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-233 |
2.58e-28 |
|
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: 113.30 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahgGFNGKhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:TIGR01193 474 IVINDVSYSY---GYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkaFRRDIQMVFQDS-----------ISAVNPRKTVREILRepmrhllSLKKSEQLARASEMLKAVDLDdsvLDKRPPQL 152
Cdd:TIGR01193 546 ---LRQFINYLPQEPyifsgsilenlLLGAKENVSQDEIWA-------ACEIAEIKDDIENMPLGYQTE---LSEEGSSI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgtACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
.
gi 16131352 233 T 233
Cdd:TIGR01193 689 Q 689
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-240 |
3.29e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ-RKAFRRDIQMVFQDSisAVNPRK 106
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElREVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:PRK10070 122 TVLDNTAFGME-LAGINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKL 240
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-233 |
3.40e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.69 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRDIQMVFQdsisavNP-RK 106
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF---EKLRKHIGIVFQ------NPdNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPM-----RHLLSLKKSEQlaRASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:PRK13648 96 FVGSIVKYDVafgleNHAVPYDEMHR--RVSEALKQVDMLERA-DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDL-RLVErfCQRVMVMDNGQIVET 233
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLsEAME--ADHVIVMNKGTVYKE 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-232 |
3.75e-28 |
|
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: 107.23 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraqrkafrrDIQMVFq 96
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL----------GLGGGF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 dsisavNPRKTVREILRepMRHLLS-LKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:cd03220 96 ------NPELTGRENIY--LNGRLLgLSRKEIDEKIDEIIEFSELGD-FIDLPVKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-231 |
5.18e-28 |
|
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: 107.48 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGN-ISWRGEPLAKLNRAQrkaFRRDIQMVFQDSISAVNPR 105
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWE---LRKRIGLVSPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREIL-----------REPMRhllslkksEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
Cdd:COG1119 95 ETVLDVVlsgffdsiglyREPTD--------EQRERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-211 |
5.42e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.41 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESP---AQGNISWRGEPLAKLNRAQRKafrrdIQMVFQDS 98
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-----IGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 IsaVNPRKTVREILREPMRHllSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:COG4136 86 L--LFPHLSVGENLAFALPP--TIGRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 16131352 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-238 |
9.16e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 106.46 E-value: 9.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnRAQ 83
Cdd:TIGR03410 1 LEVSNLNVYY------GQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL-PPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAfRRDI------QMVFqdsisavnPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDlddSVLDKRPPQLSGGQL 157
Cdd:TIGR03410 71 ERA-RAGIayvpqgREIF--------PRLTVEENLLTGLA-ALPRRSRKIPDEIYELFPVLK---EMLGRRGGDLSGGQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 158 QRVCLARALAVEPKLLILDEAVSNldlvLQAGVI----RLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:TIGR03410 138 QQLAIARALVTRPKLLLLDEPTEG----IQPSIIkdigRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
....*
gi 16131352 234 QVVGE 238
Cdd:TIGR03410 214 GAGDE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-230 |
1.49e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISwrgeplaklnraqrkaFRRDIQMVF--QDSISa 101
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS----------------IPKGLRIGYlpQEPPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 vNPRKTVREILREPMRHLLSLKK----------------------SEQL---------ARASEMLKAVDLDDSVLDKRPP 150
Cdd:COG0488 73 -DDDLTVLDTVLDGDAELRALEAeleeleaklaepdedlerlaelQEEFealggweaeARAEEILSGLGFPEEDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvLQAgvIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES--IEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-238 |
1.81e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklNRAQRKAFRRDIQMVFQDsISAVnPRKT 107
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR--IRSPRDAIALGIGMVHQH-FMLV-PNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VRE--IL-REPMRHL-LSLKK-SEQLARASEMLK-AVDLDDSVLDkrppqLSGGQLQRVCLARALAVEPKLLILDE--AV 179
Cdd:COG3845 97 VAEniVLgLEPTKGGrLDRKAaRARIRELSERYGlDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEptAV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 180 snldLVLQ--AGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:COG3845 172 ----LTPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-240 |
2.07e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.58 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 29 NNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkafrrDIQMVFQDSisAVNPRKTV 108
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER-----GVGMVFQSY--ALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 109 REILREPMRhLLSLKKSEQLAR---ASEMLKAVDLddsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK11000 93 AENMSFGLK-LAGAKKEEINQRvnqVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqvVGEKL 240
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ---VGKPL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-232 |
2.75e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.89 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLAR-------LLVGLEspAQGNISWRGEPL 76
Cdd:COG1117 12 IEVRNLNVYY------GDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 77 --AKLNRAQrkaFRRDIQMVFQDSisavNP-RKTVRE-I---LRepMRHLLSLKKSEQLARASemLKAVDLDDSV---LD 146
Cdd:COG1117 81 ydPDVDVVE---LRRRVGMVFQKP----NPfPKSIYDnVaygLR--LHGIKSKSELDEIVEES--LRKAALWDEVkdrLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMD 226
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFY 227
|
....*.
gi 16131352 227 NGQIVE 232
Cdd:COG1117 228 LGELVE 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-241 |
3.24e-27 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 107.20 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAHGGFNGKhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPaqgniSWRGEP----- 75
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVK-----AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD-----NWRVTAdrmrf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 76 ----LAKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTV-REILRE--------PMRHLLSLKKSeqlaRASEMLKAVDLD 141
Cdd:PRK15093 71 ddidLLRLSpRERRKLVGHNVSMIFQEPQSCLDPSERVgRQLMQNipgwtykgRWWQRFGWRKR----RAIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 142 D--SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFC 219
Cdd:PRK15093 147 DhkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
250 260
....*....|....*....|..
gi 16131352 220 QRVMVMDNGQIVETQVVGEKLT 241
Cdd:PRK15093 227 DKINVLYCGQTVETAPSKELVT 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-245 |
3.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsisavNPRK- 106
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN---LRRKIGMVFQ------NPDNq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 ----TVREILREPMRHLlSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:PRK13642 94 fvgaTVEDDVAFGMENQ-GIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQVVGEKLTFSSD 245
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-225 |
3.76e-27 |
|
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: 109.68 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RkafRRDIQMVFQdsiSAVNPRKTVREILR--EPMRHLLSLKKSEQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRV 160
Cdd:TIGR02857 394 W---RDQIAWVPQ---HPFLFAGTIAENIRlaRPDASDAEIREALERAGLDEFVAALPQGlDTPIGEGGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVM 225
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-231 |
3.96e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIS------WRgeplaklnraQRKAFRRDIQMV 94
Cdd:COG4586 32 YREVEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpFK----------RRKEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 F-QDS-----ISAVNPRKTVREILREPMRHLlslkkSEQLARASEMLkavDLDDsVLDKRPPQLSGGQLQRVCLARALAV 168
Cdd:COG4586 101 FgQRSqlwwdLPAIDSFRLLKAIYRIPDAEY-----KKRLDELVELL---DLGE-LLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-231 |
5.76e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 19 NGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGepLAKLNRAQRKAFRRDIQMVFQds 98
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 isavNP-RKTVREILREPMR---HLLSLKKSEQLARASEMLKAVDLDDsvLDKRPPQ-LSGGQLQRVCLARALAVEPKLL 173
Cdd:PRK13633 93 ----NPdNQIVATIVEEDVAfgpENLGIPPEEIRERVDESLKKVGMYE--YRRHAPHlLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHdlrLVERFCQ--RVMVMDNGQIV 231
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH---YMEEAVEadRIIVMDSGKVV 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-233 |
7.83e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.90 E-value: 7.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQ 96
Cdd:PRK13657 343 SYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DsisAVNPRKTVREILR--EPMRHLLSLKKSEQLARASE-MLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
Cdd:PRK13657 417 D---AGLFNRSIEDNIRvgRPDATDEEMRAAAERAQAHDfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 174 ILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTV-RNADRILVFDNGRVVES 550
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-232 |
1.04e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGE--PLAKLNraqrkafrrdiqmvfqds 98
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLELG------------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 iSAVNPRKTVRE--ILRepMRhLLSLKKSEQLARA------SEMLKAVDLddsvldkrpP--QLSGGQLQRVCLARALAV 168
Cdd:COG1134 97 -AGFHPELTGREniYLN--GR-LLGLSRKEIDEKFdeivefAELGDFIDQ---------PvkTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG1134 164 DPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-232 |
1.83e-26 |
|
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: 107.88 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN----RAQRKAFRRDIqMVFQDSISA 101
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslRRQVALVSQDV-VLFNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 VNPRKTVREILREPMRHLLslkkseQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:TIGR02203 425 NIAYGRTEQADRAEIERAL------AAAYAQDFVDKLPLGlDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 181 NLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-232 |
2.49e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.89 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraqRKAFRRDIQMVFQDSIsavnp 104
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD---HHYLHRQVALVGQEPV----- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rkTVREILREPMRHLLSLKKSEQLARASEMLKAVDL-------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:TIGR00958 566 --LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFimefpngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 178 AVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:TIGR00958 644 ATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-230 |
2.69e-26 |
|
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: 101.35 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnRAQRKAFRRDIQMVFQDsisavnpR 105
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRDAIRAGIAYVPED-------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRHLLSLkkseqlarasemlkavdlddsvldkrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:cd03215 85 KREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-230 |
2.82e-26 |
|
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: 102.55 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklNRAQRKAFRRDIQMVFQDSisaVN 103
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEP---VL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPMRH--LLSLKKSEQLARA----SEMLKAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:cd03248 100 FARSLQDNIAYGLQScsFECVKEAAQKAHAhsfiSELASGYDTE---VGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVMVMDNGQI 230
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-231 |
2.90e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaKLNRAQRKAFRRDIQMVFQDSISAVNPRKT 107
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWVRSKVGLVFQDPDDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREILREPMRhlLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
Cdd:PRK13647 98 WDDVAFGPVN--MGLDKDEVERRVEEALKAVRMWD-FRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131352 188 AGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-232 |
3.78e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnrAQRKAFRRDIQMVFQ 96
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 dsISAVNPRKTVREILREPMRHL-LSLKKSEqlARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:PRK13536 122 --FDNLDLEFTVRENLLVFGRYFgMSTREIE--AVIPSLLEFARLESKA-DARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNG-QIVE 232
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-231 |
4.92e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISwRGEPLAKLNRAQR--KAFRRDIQMVFQDSISAVNPR 105
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQKeiKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRHLLSLKKSEQLAraSEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIA--AEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
1.36e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYAHggfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklN 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGD---------TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE--A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAQRKAFRRdIQMVFQDSISAVNPR-KTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQR 159
Cdd:PRK09536 70 LSARAASRR-VASVPQDTSLSFEFDvRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFA-DRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-233 |
1.52e-25 |
|
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: 99.98 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraqRKAFRRDIQMVfqdSIS 100
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN----IEALRRIGALI---EAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVREILRepmRHLLSLKKSEQlaRASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:cd03268 82 GFYPNLTARENLR---LLARLLGIRKK--RIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-232 |
2.72e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYahggfNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-----ESPAQGNISWRGEPL 76
Cdd:PRK14239 4 PILQVSDLSVYY-----NKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 77 AKlNRAQRKAFRRDIQMVFQDSisavNPRK-TVREILREPMRhLLSLKKSEQLARASEM-LKAVDLDDSVLDK---RPPQ 151
Cdd:PRK14239 75 YS-PRTDTVDLRKEIGMVFQQP----NPFPmSIYENVVYGLR-LKGIKDKQVLDEAVEKsLKGASIWDEVKDRlhdSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
.
gi 16131352 232 E 232
Cdd:PRK14239 227 E 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-231 |
2.85e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaKLNRAQRKAF----RRDIQMVFQDSisAVNPR 105
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKGIClppeKRRIGYVFQDA--RLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREPMRHllslKKSEQLARASEMLKAvdldDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK11144 91 YKVRGNLRYGMAK----SMVAQFDKIVALLGI----EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-231 |
4.82e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.04 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MT-LLNISGLSHHYAHGgfngkHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKL 79
Cdd:PRK10535 1 MTaLLELKDIRRSYPSG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 NRAQRKAFRRD-IQMVFQdsisavnprktvreilrepMRHLLS----------------LKKSEQLARASEMLKAVDLDD 142
Cdd:PRK10535 76 DADALAQLRREhFGFIFQ-------------------RYHLLShltaaqnvevpavyagLERKQRLLRAQELLQRLGLED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 143 SVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDlRLVERFCQRV 222
Cdd:PRK10535 137 RV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAERV 213
|
....*....
gi 16131352 223 MVMDNGQIV 231
Cdd:PRK10535 214 IEIRDGEIV 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-230 |
6.02e-25 |
|
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: 99.15 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQ 83
Cdd:cd03218 1 LRAENLSKRY------GKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKafRRDIQMVFQDSIsaVNPRKTVREILREPMRhLLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLA 163
Cdd:cd03218 72 RA--RLGIGYLPQEAS--IFRKLTVEENILAVLE-IRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKL-QQQFGtacLFIT-HDLRLVERFCQRVMVMDNGQI 230
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
28-231 |
6.52e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkAFRRDIQMVFQDSISAVNPRKT 107
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREILREPMRhlLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
Cdd:PRK13644 96 EEDLAFGPEN--LCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131352 188 AGVIRLLKKLQQQfGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
Cdd:PRK13644 173 IAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-212 |
6.85e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.84 E-value: 6.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDsiSAVNPRK 106
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLkkSEQLARASEMLK--AVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:PRK11831 100 NVFDNVAYPLREHTQL--PAPLLHSTVMMKleAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*...
gi 16131352 185 VLQAGVIRLLKKLQQQFGTACLFITHDL 212
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-211 |
6.95e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRdiqmvfQDSISAVNP 104
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQ------QVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 R---KTVREILREP--MRHllslkKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PRK10247 91 TlfgDTVYDNLIFPwqIRN-----QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|..
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-231 |
7.94e-25 |
|
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: 97.62 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 13 YAHGGFNGKHQHQaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQ--GNISWRGEPLAKlnraqrKAFRRD 90
Cdd:cd03213 11 VTVKSSPSKSGKQ-LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK------RSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 91 IQMVFQDSIsaVNPRKTVREILRepmrhlLSLKkseqlarasemLKavdlddsvldkrppQLSGGQLQRVCLARALAVEP 170
Cdd:cd03213 84 IGYVPQDDI--LHPTLTVRETLM------FAAK-----------LR--------------GLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLR-LVERFCQRVMVMDNGQIV 231
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-250 |
1.04e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 32 SLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKafrrdIQMVFQDSisavN--PRKTVR 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP-----VSMLFQEN----NlfSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 EILREPMRHLLSLKkSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
Cdd:PRK10771 90 QNIGLGLNPGLKLN-AAQREKLHAIARQMGIED-LLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLTFSSDAGRVL 250
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-232 |
1.74e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHhyahgGFNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrGEplaklnr 81
Cdd:COG0488 314 KVLELEGLSK-----SYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 aqrkafrrDIQMVF--QDSiSAVNPRKTVREILREpmrhlLSLKKSEQLARAseMLKAVDLDDSVLDKRPPQLSGGQLQR 159
Cdd:COG0488 377 --------TVKIGYfdQHQ-EELDPDKTVLDELRD-----GAPGGTEQEVRG--YLGRFLFSGDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 160 VCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIE----TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-233 |
1.78e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQDSIS 100
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPES---WRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 avnPRKTVREILR--------EPMRHLLslkkseQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
Cdd:PRK11174 435 ---PHGTLRDNVLlgnpdasdEQLQQAL------ENAWVSEFLPLLPQGlDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQ 564
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-231 |
1.86e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 15 HGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMV 94
Cdd:PRK13640 10 HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 FQdsisavNPRK-----TV----------REILREPMRHLLSlkkseqlarasEMLKAVDLDDSVlDKRPPQLSGGQLQR 159
Cdd:PRK13640 90 FQ------NPDNqfvgaTVgddvafglenRAVPRPEMIKIVR-----------DVLADVGMLDYI-DSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQrVMVMDNGQIV 231
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQ-VLVLDDGKLL 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-234 |
2.92e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPA---QGNISWRGEPLaklnRAQ--RKAFRRDIQMVFQDsiSAV 102
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL----QASniRDTERAGIAIIHQE--LAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVREIL---REPMRHLLsLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PRK13549 94 VKELSVLENIflgNEITPGGI-MDYDAMYLRAQKLLAQLKLDINP-ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTR 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-231 |
4.84e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFrrdIQMVFQDSISAVNPRK 106
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY---IGRVFQDPMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREIL-----REPMRHLLSLKKSEQLARASEMLKAVDLDdsvLDKRPPQ----LSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:COG1101 98 TIEENLalayrRGKRRGLRRGLTKKRRELFRELLATLGLG---LENRLDTkvglLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-212 |
8.60e-24 |
|
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: 100.13 E-value: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGgfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAq 83
Cdd:TIGR02868 335 LELRDLSAGYPGA--------PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkAFRRDIQMVFQDS--ISAvnprkTVREILR--------EPMRHLLSLKKSEQLARASEmlkavDLDDSVLDKRPPQLS 153
Cdd:TIGR02868 406 --EVRRRVSVCAQDAhlFDT-----TVRENLRlarpdatdEELWAALERVGLADWLRALP-----DGLDTVLGEGGARLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDL 212
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-229 |
1.39e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.90 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrgeplaklnraq 83
Cdd:cd03221 1 IELENLSKTY--GG-------KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkafrrdiqmvfqdsISAVNprktvreilrepMRHLlslkkseqlarasemlkavdlddsvldkrpPQLSGGQLQRVCLA 163
Cdd:cd03221 60 ---------------GSTVK------------IGYF------------------------------EQLSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-238 |
1.46e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkAFRRDIQMVFQD--- 97
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL-ALRQQVATVFQDpeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 SISAVNPRKTVREILREpmrhlLSLKKSEQLARASEMLKAVDLDDsvLDKRPPQ-LSGGQLQRVCLARALAVEPKLLILD 176
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRN-----LGVPEAEITRRVDEALTLVDAQH--FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGE 238
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-234 |
2.12e-23 |
|
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: 98.74 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL--ESPAQGNISWRGEPLAKlnRAQRKAFRRDIQMVFQDSisAVNPR 105
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKA--SNIRDTERAGIVIIHQEL--TLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILRepMRHLLSLK-----KSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:TIGR02633 93 LSVAENIF--LGNEITLPggrmaYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATK 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-241 |
2.45e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-----ESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsISA 101
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE---LRRRVQMVFQ--IPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 VNPRKTVRE-ILREPMRHLLSLKKSEQLARASEMLKAVDLDDSV---LDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:PRK14247 93 PIPNLSIFEnVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLT 241
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-232 |
1.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLEspaqgnISWRGEPL-------AKLNRAQR-KAFRRDIQMVFQDSI 99
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIvgdyaipANLKKIKEvKRLRKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SAVNPRKTVREILREPMRhlLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PRK13645 101 YQLFQETIEKDIAFGPVN--LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-232 |
1.26e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.63 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaKLNRAQRKAFRRDIQMV------FQDSIS- 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLRNQVALVsqnvhlFNDTIAn 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 ----AVNPRKTVREIlrepmrhllslKKSEQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:PRK11176 436 niayARTEQYSREQI-----------EEAARMAYAMDFINKMDNGlDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-231 |
1.68e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklNRAQRKAFRRDIQMVFQDsisavnpRK 106
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRAGIAYVPED-------RK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 T--------VRE-----ILREPMRHLLsLKKSEQLARASEMLKAVDLddsvldkRPP-------QLSGGQLQRVCLARAL 166
Cdd:COG1129 338 GeglvldlsIREnitlaSLDRLSRGGL-LDRRRERALAEEYIKRLRI-------KTPspeqpvgNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
1.94e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKL- 79
Cdd:COG1137 1 MMTLEAENLVKSY------GKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 80 --NRAqrkafRRDIQMVFQD-SISavnpRK-TVRE----ILRepmrhLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQ 151
Cdd:COG1137 72 mhKRA-----RLGIGYLPQEaSIF----RKlTVEDnilaVLE-----LRKLSKKEREERLEELLEEFGITH-LRKSKAYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALAVEPKLLILDE--------AVSNldlvLQAgVIRLLKklQQQFGtacLFIT-HDLRLVERFCQRV 222
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEpfagvdpiAVAD----IQK-IIRHLK--ERGIG---VLITdHNVRETLGICDRA 206
|
....*...
gi 16131352 223 MVMDNGQI 230
Cdd:COG1137 207 YIISEGKV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-233 |
3.06e-22 |
|
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: 91.05 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLES--PAQGNISWRGEPLAKLNRAQRkaFRRDIQMVFQDS--ISAV 102
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEER--ARLGIFLAFQYPpeIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 nprkTVREILRepmrhllslkkseqlarasemlkavDLDDSvldkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:cd03217 93 ----KNADFLR-------------------------YVNEG--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERF-CQRVMVMDNGQIVET 233
Cdd:cd03217 136 DIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS 186
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-229 |
6.46e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnRAQRKafRRDIQMVFQdsISAVNP 104
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHA--RQRVGVVPQ--FDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVREILREPMRHlLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:PRK13537 94 DFTVRENLLVFGRY-FGLSAAAARALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:PRK13537 172 QARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-244 |
6.91e-22 |
|
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: 94.48 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLES--PAQGNISWR----------------GEP---- 75
Cdd:TIGR03269 10 FDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvGEPcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 76 ----------LAKLNRAQRKAFRRDIQMVFQDSIsAVNPRKTVREILREPMrHLLSLKKSEQLARASEMLKAVDLDDSVL 145
Cdd:TIGR03269 86 ggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEAL-EEIGYEGKEAVGRAVDLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 146 D-KRppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
Cdd:TIGR03269 164 HiAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIW 241
|
250 260
....*....|....*....|
gi 16131352 225 MDNGQIVEtqvVGEKLTFSS 244
Cdd:TIGR03269 242 LENGEIKE---EGTPDEVVA 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-231 |
7.45e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRDIQMVFQDSISAVNprK 106
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQLPAAEG--M 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK10575 101 TVRELVaigRYPWHGALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131352 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-217 |
1.04e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplaklnrAQRKAFrrdiqMVFQDSISAVNP 104
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------GARVAY-----VPQRSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rKTVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDDsvLDKRPPQ-LSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:NF040873 72 -LTVRDLVamgRWARRGLWRRLTRDDRAAVDDALERVGLAD--LAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVER 217
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-232 |
1.27e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.01 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMVFQDSIsavnp 104
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGVAMVQQDPV----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rktvreILREPMRHLLSLKKSEQLARASEMLKAVDLDD----------SVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
Cdd:PRK10790 426 ------VLADTFLANVTLGRDISEEQVWQALETVQLAElarslpdglyTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLR-LVErfCQRVMVMDNGQIVE 232
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLStIVE--ADTILVLHRGQAVE 554
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-268 |
1.79e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraQRKAFRRDIQMVFQDsISAVNpRKT 107
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD--HKLAAQLGIGIIYQE-LSVID-ELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VRE---ILREPMRHLLSLKK---SEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:PRK09700 97 VLEnlyIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 182 LD------LVLqagVIRLLKKLqqqfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEkltFSSD------AGRV 249
Cdd:PRK09700 176 LTnkevdyLFL---IMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD---VSNDdivrlmVGRE 245
|
250
....*....|....*....
gi 16131352 250 LQNavlpAFPVRRRTTEKV 268
Cdd:PRK09700 246 LQN----RFNAMKENVSNL 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-231 |
2.41e-21 |
|
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: 89.25 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 16 GGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL---ESPAQGNISWRGEPLaklnraQRKAFRRDIQ 92
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR------KPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 93 MVFQDSISAvnPRKTVREILR-EPMRHLLSLKKSEQLARASEMLKAVDLDDSVL-DKRPPQLSGGQLQRVCLARALAVEP 170
Cdd:cd03234 85 YVRQDDILL--PGLTVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItHDLR--LVERFcQRVMVMDNGQIV 231
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-HQPRsdLFRLF-DRILLLSSGEIV 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-231 |
2.90e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaKLNRAQRKAFRRDIQMVFQDsisAVNPRK 106
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE---HIQHYASKEVARRIGLLAQN---ATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 -TVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:PRK10253 96 iTVQELVargRYPHQPLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-231 |
3.09e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 89.89 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVG-LESPA-------QGNISWRGEPLAKLNrAQRKAFRRdiqmv 94
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAID-APRLARLR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 fqdsisAVNPRK-------TVREIL---REPMRH---LLSLKKSEQLARASEMLKAvdldDSVLDKRPPQLSGGQLQRVC 161
Cdd:PRK13547 86 ------AVLPQAaqpafafSAREIVllgRYPHARragALTHRDGEIAWQALALAGA----TALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 162 LARALA---------VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK13547 156 FARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-231 |
9.06e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYahggfngkhQHQAVLNNVSLTLKSGETVALLGRSGCGKSTL----ARLLvgleSPAQGNISWRGEPLAKLN- 80
Cdd:COG4604 4 IKNVSKRY---------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLL----PPDSGEVLVDGLDVATTPs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 --RAQRKAFRRdiqmvfQDSisAVNPRKTVREIL---REPM-RHLLSLKKSEQLARASEMLKAVDLDDSVLDkrppQLSG 154
Cdd:COG4604 71 reLAKRLAILR------QEN--HINSRLTVRELVafgRFPYsKGRLTAEDREIIDEAIAYLDLEDLADRYLD----ELSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-230 |
2.35e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAvLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL---ESPAQGNISWRGEPL---AKLNRAQRKAfRRDIQMVF 95
Cdd:PRK09984 15 NQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVqreGRLARDIRKS-RANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 96 QdSISAVNPRKTVREILREPM------RHLLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVE 169
Cdd:PRK09984 93 Q-QFNLVNRLSVLENVLIGALgstpfwRTCFSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-232 |
2.41e-20 |
|
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: 90.26 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkAFRRDIQMV------FQDSIs 100
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA---SLRAAIGIVpqdtvlFNDTI- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVN-----PRKTVREIlrepmrhllslkksEQLARASEmlkavdLDDSVldKRPPQ------------LSGGQLQRVCLA 163
Cdd:COG5265 449 AYNiaygrPDASEEEV--------------EAAARAAQ------IHDFI--ESLPDgydtrvgerglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-210 |
3.05e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.63 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnRAQRKAFRRDiqMVFQDSISAVNPRKTVR 109
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQD--LLYLGHQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 EILR--EPMRHLLSlkkSEQLARAsemLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQ 187
Cdd:PRK13538 93 ENLRfyQRLHGPGD---DEALWEA---LAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID---K 162
|
170 180
....*....|....*....|....*
gi 16131352 188 AGVIRLLKKLQQ--QFGTACLFITH 210
Cdd:PRK13538 163 QGVARLEALLAQhaEQGGMVILTTH 187
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-232 |
3.87e-20 |
|
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: 85.54 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRDIQMVFQDSISAVNprk 106
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL---EDLRSSLTIIPQDPTLFSG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPMRHLlslkkSEQlarasEMLKAVDLDDSVLDkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:cd03369 97 TIRSNL-DPFDEY-----SDE-----EIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131352 187 QAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:cd03369 161 DALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKE 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-247 |
4.60e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPA---QGNISWRGEPLAKLNRAQRKAFrrdiqmVFQDSISAvnP 104
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY------VQQDDLFI--P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVREILREpMRHLL---SLKKSEQLARASEMLKAVDLDDSV-----LDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:TIGR00955 113 TLTVREHLMF-QAHLRmprRVTKKEKRERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItHD--LRLVERFCQrVMVMDNGQIVETQVVGEKLTFSSDAG 247
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQpsSELFELFDK-IILMAEGRVAYLGSPDQAVPFFSDLG 262
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-228 |
5.79e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYahGGFngkhqhQAVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:PRK11300 4 PLLSVSGLMMRF--GGL------LAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQ--RKAFRRDIQMV--FQDsisavnprKTVRE-ILREPMRHLLS-----------LKKSEQ--LARASEMLKAVDLDDs 143
Cdd:PRK11300 75 HQiaRMGVVRTFQHVrlFRE--------MTVIEnLLVAQHQQLKTglfsgllktpaFRRAESeaLDRAATWLERVGLLE- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 144 VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM 223
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
....*
gi 16131352 224 VMDNG 228
Cdd:PRK11300 226 VVNQG 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-241 |
7.33e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPL---AKLNRAQRKAFRRDIQMVFQDSISA 101
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 102 vnPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 179 VSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLT 241
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-215 |
7.38e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIswrgeplaklnraQRKAFRRdIQMVFQD-SISAVN 103
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLR-IGYVPQKlYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRkTVREILRepmrhLLSLKKSEQLARASEMLKAVDLDDSVLDKrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK09544 83 PL-TVNRFLR-----LRPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|..
gi 16131352 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-217 |
9.29e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-----ESPAQGNISWRGEPLAKlNRAQRKAFRRDIQ 92
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 93 MVFQDS----ISAV-NPRKTVREILREPMRHLLSLKKSEqlarasemLKAVDLDDSV---LDKRPPQLSGGQLQRVCLAR 164
Cdd:PRK14258 92 MVHPKPnlfpMSVYdNVAYGVKIVGWRPKLEIDDIVESA--------LKDADLWDEIkhkIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVER 217
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-246 |
1.40e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrKAFRRDIQMVFQDSIsaVNPRK 106
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGIYLVPQEPL--LFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVRE-ILREPMRHLLSLKKSEQLARAsemlKAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK15439 102 SVKEnILFGLPKRQASMQKMKQLLAA----LGCQLD---LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVetqVVGEKLTFSSDA 246
Cdd:PRK15439 175 ETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA---LSGKTADLSTDD 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-216 |
2.34e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQRKAFRRdiQMVFQDSISAVNPR 105
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDEPHE--NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREpMRHLLSlkkSEQLArASEMLKAVDLDDsvLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDl 184
Cdd:TIGR01189 88 LSALENLHF-WAAIHG---GAQRT-IEDALAAVGLTG--FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD- 159
|
170 180 190
....*....|....*....|....*....|....*
gi 16131352 185 vlQAGVIRLLKKLQQ--QFGTACLFITH-DLRLVE 216
Cdd:TIGR01189 160 --KAGVALLAGLLRAhlARGGIVLLTTHqDLGLVE 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-231 |
2.71e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPAQGNISWRGEPLAKLNR---AQRKAFrrdiqMVFQDSISAVNP 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelARHRAY-----LSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rktVREILREPMRHLLSLKKSEQLAraSEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARAL-----AVEP--KLLILDE 177
Cdd:COG4138 86 ---VFQYLALHQPAGASSEAVEQLL--AQLAEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 178 AVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
27-233 |
4.51e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 83.54 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGleSPA----QGNISWRGEPLAKLNRAQRKafRRDIQMVFQD--SIS 100
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERA--HLGIFLAFQYpiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKTVREIL--REPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQ-LSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:CHL00131 98 GVSNADFLRLAYnsKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 178 AVSNLD---LVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFC-QRVMVMDNGQIVET 233
Cdd:CHL00131 178 TDSGLDidaLKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-232 |
8.67e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 17 GFNGKhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGnISWRGEPL----AKLNRAQRKAFRRDIQ 92
Cdd:PRK14271 30 GFAGK----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 93 MVFQDSISAvnPRKTVREILREPMRHLLSLKKsEQLARASEMLKAVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVE 169
Cdd:PRK14271 105 MLFQRPNPF--PMSIMDNVLAGVRAHKLVPRK-EFRGVAQARLTEVGLWDAVKDRlsdSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-236 |
9.12e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIswrgeplaklnraqrkAFRRDIQMVFQdsisavnP 104
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------ARPAGARVLFL-------P 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RK------TVREILREPmrHLLSLKKSEQLARAsemLKAVDLDDSV--LDKRPP---QLSGGQLQRVCLARALAVEPKLL 173
Cdd:COG4178 433 QRpylplgTLREALLYP--ATAEAFSDAELREA---LEAVGLGHLAerLDEEADwdqVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 174 ILDEAVSNLDLVLQAgviRLLKKLQQQF-GTACLFITHDLRLvERFCQRVMVMDNGQIVETQVV 236
Cdd:COG4178 508 FLDEATSALDEENEA---ALYQLLREELpGTTVISVGHRSTL-AAFHDRVLELTGDGSWQLLPA 567
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-217 |
1.20e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLAR-------LLVGLEspAQGNISWRGEPLAKlNRAQRKAFRRDIQMVFQDSis 100
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 avNP-RKTVREILREPMRHLLSLKKSEQLARASemLKAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILD 176
Cdd:PRK14243 101 --NPfPKSIYDNIAYGARINGYKGDMDELVERS--LRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVER 217
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-231 |
1.24e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKafRRDIQMVFQDsiSAVNPRK 106
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYLPQE--ASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131352 187 QAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-232 |
1.86e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-----ESPAQGNISWRGEPL--AKLNRAQrkaFRRDIQMVFQdsI 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPIE---VRREVGMVFQ--Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SAVNPRKTVREILREPMRHLLSLKKSEQL-ARASEMLKAVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKELdERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-232 |
2.94e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.87 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGFNgkhqhqavLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAq 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--------VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 rkAFRRDIQMVFQD----------SISAVNPRKTVREILREPMRHLLSLKkseqlarasemlkavdlDDSVLDkrpPQLS 153
Cdd:PRK10522 394 --DYRKLFSAVFTDfhlfdqllgpEGKPANPALVEKWLERLKMAHKLELE-----------------DGRISN---LKLS 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-230 |
3.31e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRkaFRRDIQMVFQDsisavnpRKTVR 109
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR--LARGLVYLPED-------RQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 110 EILREPMR--------HLLS--LKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PRK15439 352 LYLDAPLAwnvcalthNRRGfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-231 |
4.87e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYAHGGfngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNR 81
Cdd:COG3845 256 VVLEVENLSVRDDRGV--------PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 AQRkafrRDIQMVFqdsIS------AVNPRKTVRE--IL----REPMRHLLSLKKSEQLARASEMLKAVDLddsvldkRP 149
Cdd:COG3845 328 RER----RRLGVAY---IPedrlgrGLVPDMSVAEnlILgryrRPPFSRGGFLDRKAIRAFAEELIEEFDV-------RT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 150 P-------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRV 222
Cdd:COG3845 394 PgpdtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRI 472
|
....*....
gi 16131352 223 MVMDNGQIV 231
Cdd:COG3845 473 AVMYEGRIV 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-210 |
6.25e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnraqrkaFRRDIQMVfqDSISAV 102
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ---------FGREASLI--DAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVREILrepmrhllslkkseqlarasemlKAVDLDDSVLDKRPP-QLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:COG2401 110 GDFKDAVELL-----------------------NAVGLSDAVLWLRRFkELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180
....*....|....*....|....*....
gi 16131352 182 LDLVLQAGVIRLLKKLQQQFGTACLFITH 210
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-233 |
3.01e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNraQRKAFRRDIQMVFQDsISAVnPRKT 107
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS--TTAALAAGVAIIYQE-LHLV-PEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREIL---REPMRHLLsLKKSEQLARASEMLKAVDLDdsvLDKRPP--QLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:PRK11288 96 VAENLylgQLPHKGGI-VNRRLLNYEAREQLEHLGVD---IDPDTPlkYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:PRK11288 172 SAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-183 |
3.30e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAF--RRDiqmvfqdsisAVN 103
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlgHRN----------AMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILrEPMRHLLslkkSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:PRK13539 86 PALTVAENL-EFWAAFL----GGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-224 |
3.43e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAvLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnraqRKAFRRD-IQMVFQDSISAV 102
Cdd:PRK15056 20 HTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKNlVAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLddsvLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILD 176
Cdd:PRK15056 92 SFPVLVEDVVmmgRYGHMGWLRRAKKRDRQIVTAALARVDM----VEFRHRQigeLSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQ-RVMV 224
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDyTVMV 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-267 |
5.11e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 78.36 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESpAQGNI-----SWRGEPLAK 78
Cdd:cd03289 3 MTVKDLTAKYTEGG-------NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIqidgvSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LnraqRKAFRRDIQMVFQDSisavnprKTVREILREPMRHllslkKSEQLARASEmlkAVDLdDSVLDKRPPQ------- 151
Cdd:cd03289 75 W----RKAFGVIPQKVFIFS-------GTFRKNLDPYGKW-----SDEEIWKVAE---EVGL-KSVIEQFPGQldfvlvd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 ----LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlQAGVIRllKKLQQQFGTaCLFITHDLRLVERF-CQRVMVMD 226
Cdd:cd03289 135 ggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI-TYQVIR--KTLKQAFAD-CTVILSEHRIEAMLeCQRFLVIE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16131352 227 NGQIVETQVVGEKLTFSSdagrVLQNAVLPA-----FPVRRRTTEK 267
Cdd:cd03289 211 ENKVRQYDSIQKLLNEKS----HFKQAISPSdrlklFPRRNSSKSK 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-226 |
5.60e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 77.83 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 34 TLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnRAQRkafrrdiqmvfqdsISAVNPrKTVREILR 113
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQY--------------IKADYE-GTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 114 EPMRHLLSLKKSEqlaraSEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRL 193
Cdd:cd03237 84 SITKDFYTHPYFK-----TEIAKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 16131352 194 LKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-245 |
9.42e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 9.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIS--------------WRG-------EPLAKLNRAQR- 84
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlkwWRSkigvvsqDPLLFSNSIKNn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 85 -----------KAFRRDIQMVFQDSISAVNPRKTVREILREPMR---------HLLSLKKSEQLARASEML---KAV--- 138
Cdd:PTZ00265 480 ikyslyslkdlEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNdmsnttdsnELIEMRKNYQTIKDSEVVdvsKKVlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 139 -------DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
Cdd:PTZ00265 560 dfvsalpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250 260 270
....*....|....*....|....*....|....*..
gi 16131352 212 LRLVeRFCQRVMVMDN---GQIVETQVVGEKLTFSSD 245
Cdd:PTZ00265 640 LSTI-RYANTIFVLSNrerGSTVDVDIIGEDPTKDNK 675
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-231 |
2.53e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.45 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISG--LSHHYAhggfngkhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplAK 78
Cdd:PRK11147 1 MSLISIHGawLSFSDA-----------PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD--LI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNRAQRKAFRRDIQMVFqDSISAvnPRKTVREILRE--PMRHLLSLKKSE----QLARASEMLKAVD---LDD---SVL- 145
Cdd:PRK11147 68 VARLQQDPPRNVEGTVY-DFVAE--GIEEQAEYLKRyhDISHLVETDPSEknlnELAKLQEQLDHHNlwqLENrinEVLa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 146 ------DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFC 219
Cdd:PRK11147 145 qlgldpDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMA 220
|
250
....*....|..
gi 16131352 220 QRVMVMDNGQIV 231
Cdd:PRK11147 221 TRIVDLDRGKLV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-216 |
4.10e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQRKAFRRDiqMVFQDSISAVNPR 105
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILrepmRHLLSLKKSEQLARAsemLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlv 185
Cdd:cd03231 88 LSVLENL----RFWHADHSDEQVEEA---LARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-- 157
|
170 180 190
....*....|....*....|....*....|....
gi 16131352 186 lQAGVIRLLKKLQQ--QFGTACLFITH-DLRLVE 216
Cdd:cd03231 158 -KAGVARFAEAMAGhcARGGMVVLTTHqDLGLSE 190
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-232 |
1.28e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.99 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 7 SGLSHHYAHGgfngKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAqrkA 86
Cdd:COG4615 331 RGVTYRYPGE----DGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRE---A 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 87 FRRDIQMVFQDsisavnprktvreilrepmRHLLSLKKSEQLARASEMLKAVDLDD--SVLDKR--PPQLSGGQLQRVCL 162
Cdd:COG4615 404 YRQLFSAVFSDfh---------------lfDRLLGLDGEADPARARELLERLELDHkvSVEDGRfsTTDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 163 ARALAVEPKLLILDE--AvsnlDlvlQAGVIR------LLKKLQQQfGTACLFITHDlrlvERF---CQRVMVMDNGQIV 231
Cdd:COG4615 469 LVALLEDRPILVFDEwaA----D---QDPEFRrvfyteLLPELKAR-GKTVIAISHD----DRYfdlADRVLKMDYGKLV 536
|
.
gi 16131352 232 E 232
Cdd:COG4615 537 E 537
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-210 |
1.28e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.19 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISwrgeplaklnraqrKAFRRDIQMVFQDSISav 102
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------MPEGEDLLFLPQRPYL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 nPRKTVREILREPmrhllslkkseqlarasemlkavdLDDsvldkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:cd03223 76 -PLGTLREQLIYP------------------------WDD--------VLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 16131352 183 DLVLQAGVIRLLKKLqqqfGTACLFITH 210
Cdd:cd03223 123 DEESEDRLYQLLKEL----GITVISVGH 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-212 |
1.29e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 34 TLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNI----SW-------RGEPL----AKLNRAQRKAFRRdIQMVfqDS 98
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepSWdevlkrfRGTELqnyfKKLYNGEIKVVHK-PQYV--DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 ISAVnPRKTVREILrepmrhllslKKSEQLARASEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:PRK13409 172 IPKV-FKGKVRELL----------KKVDERGKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 16131352 179 VSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDL 212
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-226 |
1.54e-15 |
|
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: 75.98 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 34 TLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRgeplAKLN-RAQRkaFRRDIQMvfqdsisavnprkTVREIL 112
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISyKPQY--ISPDYDG-------------TVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 113 REPMRHLLSLKKSEqlaraSEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR 192
Cdd:COG1245 423 RSANTDDFGSSYYK-----TEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|....
gi 16131352 193 LLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
Cdd:COG1245 497 AIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-226 |
1.60e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 2 TLLNISGLSHHYahGGFngkhqhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrgeplaKLNR 81
Cdd:PRK13409 339 TLVEYPDLTKKL--GDF--------SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP------ELKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 82 A---QRkaFRRDIQMvfqdsisavnprkTVREILREPMRHLLS--LKkseqlaraSEMLKAVDLDDsVLDKRPPQLSGGQ 156
Cdd:PRK13409 403 SykpQY--IKPDYDG-------------TVEDLLRSITDDLGSsyYK--------SEIIKPLQLER-LLDKNVKDLSGGE 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-232 |
2.76e-15 |
|
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: 75.37 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQDSISAVNprk 106
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFKITIIPQDPVLFSG--- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPmrhlLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:TIGR00957 1375 SLRMNL-DP----FSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131352 180 SNLDL----VLQAGVirllkklQQQFGT-ACLFITHDLRLVERFcQRVMVMDNGQIVE 232
Cdd:TIGR00957 1450 AAVDLetdnLIQSTI-------RTQFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAE 1499
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-183 |
3.61e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraQRKAFRRDIQMV--- 94
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVsqt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 ---FQDS----ISAVNPRKTVREIlrepmrhllslkksEQLARAS----EMLKAVDLDDSVLDKRPPQLSGGQLQRVCLA 163
Cdd:PRK10789 398 pflFSDTvannIALGRPDATQQEI--------------EHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
170 180
....*....|....*....|
gi 16131352 164 RALAVEPKLLILDEAVSNLD 183
Cdd:PRK10789 464 RALLLNAEILILDDALSAVD 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-267 |
4.53e-15 |
|
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: 74.95 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYAHGGfngkhqhQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESpAQGNI-----SWRGEPLAK 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG-------RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIqidgvSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LnraqRKAFRRDIQMVFqdsISAVNPRKTVREILREPMRHLlsLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQ 158
Cdd:TIGR01271 1290 W----RKAFGVIPQKVF---IFSGTFRKNLDPYEQWSDEEI--WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQ 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 159 RVCLARALAVEPKLLILDEAVSNLDLV-LQagVIRllKKLQQQFGTaCLFITHDLR---LVErfCQRVMVMDNGQIVETQ 234
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVtLQ--IIR--KTLKQSFSN-CTVILSEHRveaLLE--CQQFLVIEGSSVKQYD 1433
|
250 260 270
....*....|....*....|....*....|....
gi 16131352 235 VVGEKLTFSSDAGRVLQNA-VLPAFPVRRRTTEK 267
Cdd:TIGR01271 1434 SIQKLLNETSLFKQAMSAAdRLKLFPLHRRNSSK 1467
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-212 |
6.10e-15 |
|
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: 74.05 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 34 TLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNI----SW-------RG----EPLAKLNRAQRKAFRRdIQMVfqDS 98
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepSWdevlkrfRGtelqDYFKKLANGEIKVAHK-PQYV--DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 ISAVNpRKTVREILrepmrhllslKKSEQLARASEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:COG1245 172 IPKVF-KGTVRELL----------EKVDERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 16131352 179 VSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDL 212
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-240 |
8.03e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLA-KLNRAQRKAfrrDIQMVFQDsisaVN--P 104
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA---GIGIIHQE----LNliP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVREIL---REPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:PRK10762 93 QLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHdlRLVERF--CQRVMVMDNGQ-IVETQV------------VGEKL 240
Cdd:PRK10762 172 LTDTETESLFRVIRELKSQ-GRGIVYISH--RLKEIFeiCDDVTVFRDGQfIAEREVadltedsliemmVGRKL 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
1.13e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 1 MTLLNISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLN 80
Cdd:PRK11614 3 KVMLSFDKVSAHY------GKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 81 RAqrKAFRRDIQMVFQDsiSAVNPRKTVREILrePMRHLLSLKKSEQlaraSEMLKAVDLDDSVLDKRPPQ---LSGGQL 157
Cdd:PRK11614 74 TA--KIMREAVAIVPEG--RRVFSRMTVEENL--AMGGFFAERDQFQ----ERIKWVYELFPRLHERRIQRagtMSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
28-233 |
1.72e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPA---QGNISWRGEPLAklNRAQRKAFRRDIQMVFQDSisAVNP 104
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCR--FKDIRDSEALGIVIIHQEL--ALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVREIL---REPMRHLLsLKKSEQLARASEMLKAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:NF040905 92 YLSIAENIflgNERAKRGV-IDWNETNRRARELLAKVGLDES-PDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-231 |
1.93e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 31 VSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnRAQRKAFRRDIQMV----FQDSISAVnprK 106
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRAGIMLCpedrKAEGIIPV---H 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREIL-------REPMRHLLSLKKSEQLARasEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PRK11288 347 SVADNInisarrhHLRAGCLINNRWEAENAD--RFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-231 |
2.40e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 31 VSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPAQGNISWRGEPLAKLNR---AQRKAF-----RRDIQM-VFQ----- 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelARHRAYlsqqqTPPFAMpVFQyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 --DSISAVNPRKTVREILRepmrhllSLKKSEQLARASEmlkavdlddsvldkrppQLSGGQLQRVCLARA-LAVEP--- 170
Cdd:PRK03695 94 qpDKTRTEAVASALNEVAE-------ALGLDDKLGRSVN-----------------QLSGGEWQRVRLAAVvLQVWPdin 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 171 ---KLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK03695 150 pagQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-241 |
4.18e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklNRAQRKAFRRDIQMVFQDsISAVNPRKT 107
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEALENGISMVHQE-LNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREIL--REPMRHLLsLKKSEQLARASEMLKAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK10982 91 MDNMWlgRYPTKGMF-VDQDKMYRDTKAIFDELDIDIDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVgEKLT 241
Cdd:PRK10982 169 EVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL-AGLT 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-214 |
6.90e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 18 FNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraQRKAFRRdiQMVFQD 97
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQK--QLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 SISAVNPRKTVREilrepmRHLLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:PRK13540 81 HRSGINPYLTLRE------NCLYDIHFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131352 178 AVSNLDlvlQAGVIRLLKKLQQQF--GTACLFITH-DLRL 214
Cdd:PRK13540 154 PLVALD---ELSLLTIITKIQEHRakGGAVLLTSHqDLPL 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-230 |
6.93e-14 |
|
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: 71.01 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-ESPAQGNISWRGEPLAKLNRAQrkAFRRDIQMVFQD----- 97
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrkrhg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 --SISAVNPRKTVREILREPMRHLLSLKKSEQLARASemLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:TIGR02633 350 ivPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSA--IQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-246 |
1.36e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 32 SLTLKSGETVALLGRSGCGKSTLARLLVGLESPAqgniswRGEPLAKLNRAQRKAFRRDIQMV---FQ----DSISAV-- 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLL------SGERQSQFSHITRLSFEQLQKLVsdeWQrnntDMLSPGed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVREILrepmrhLLSLKKSEQLARASEMLKAVDLddsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:PRK10938 97 DTGRTTAEII------QDEVKDPARCEQLAQQFGITAL----LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETqvvGEKLTFSSDA 246
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAET---GEREEILQQA 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-213 |
2.24e-13 |
|
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: 67.36 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRdiqmvFQDSISAVNP- 104
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR-----YSVAYAAQKPw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 --RKTVRE--ILREPMRHllslKKSEQLARASEMLKAVDL----DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:cd03290 90 llNATVEEniTFGSPFNK----QRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131352 177 EAVSNLDL-----VLQAGVIRLLKKLQQQFgtacLFITHDLR 213
Cdd:cd03290 166 DPFSALDIhlsdhLMQEGILKFLQDDKRTL----VLVTHKLQ 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-231 |
3.24e-13 |
|
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: 66.52 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL----ESPaQGNISWRGEPLAKLnraqRKAFRRDIQMVFQDSISavN 103
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSV-EGDIHYNGIPYKEF----AEKYPGEIIYVSEEDVH--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILRepmrhlLSLKkseqlARASEMLKAVdlddsvldkrppqlSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:cd03233 96 PTLTVRETLD------FALR-----CKGNEFVRGI--------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131352 184 lvlQAGVIRLLKKLQQ---QFGTACLFITH--DLRLVERFcQRVMVMDNGQIV 231
Cdd:cd03233 151 ---SSTALEILKCIRTmadVLKTTTFVSLYqaSDEIYDLF-DKVLVLYEGRQI 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-229 |
4.96e-13 |
|
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: 65.95 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplaklnraqRKAFrrdiqmVFQDS--ISAvnp 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAY------VSQEPwiQNG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rkTVRE-IL----REPMRHLLSLKKSeQLARASEMLkaVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:cd03250 81 --TIREnILfgkpFDEERYEKVIKAC-ALEPDLEIL--PDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 180 SNLD-----LVLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQ 229
Cdd:cd03250 156 SAVDahvgrHIFENCILGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-229 |
5.39e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 23 QHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGlesPAQGNiSWRGEPLAKlNRAQRKAFRRDIQMVFQDSIsaV 102
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGN-NFTGTILAN-NRKPTKQILKRTGFVTQDDI--L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 NPRKTVRE------ILREPMrhllSLKKSEQLARASEMLKAVDL---DDSVLDKRPPQ-LSGGQLQRVCLARALAVEPKL 172
Cdd:PLN03211 152 YPHLTVREtlvfcsLLRLPK----SLTKQEKILVAESVISELGLtkcENTIIGNSFIRgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131352 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-211 |
9.39e-13 |
|
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: 67.65 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIswRGEPLAKlnraqrkafrrdIQMVFQDSisAVNPRK 106
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA--RPQPGIK------------VGYLPQEP--QLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSL-------------------KKSEQLARASEMLKAVDLDDsvLDKR----------PP------Q 151
Cdd:TIGR03719 84 TVRENVEEGVAEIKDAldrfneisakyaepdadfdKLAAEQAELQEIIDAADAWD--LDSQleiamdalrcPPwdadvtK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHD 211
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-228 |
1.68e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 19 NGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPA--QGNISWRGEPLaklnraqRKAFRRDIQMVFQ 96
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL-------DKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DSISavNPRKTVREILrepmrhllslkkseqlaRASEMLKAvdlddsvldkrppqLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:cd03232 87 QDVH--SPNLTVREAL-----------------RFSALLRG--------------LSVEQRKRLTIGVELAAKPSILFLD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITH--DLRLVERFcQRVMVMDNG 228
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHqpSASIFEKF-DRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-230 |
2.73e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-ESPAQGNISWRGEPLAKlnRAQRKAFRRDIQMVFQD----- 97
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKI--RNPQQAIAQGIAMVPEDrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 --SISAVNPRKTVREILRepMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:PRK13549 352 ivPVMGVGKNITLAALDR--FTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-230 |
5.07e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklNRAQRKAFRRDIQMVFQDsisavnpRK- 106
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQDGLANGIVYISED-------RKr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 -------TVRE-----ILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
Cdd:PRK10762 339 dglvlgmSVKEnmsltALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-197 |
7.25e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 21 KHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVglESPAQGNISwRGEPLAKlNRAQRKAFRRDIQMVFQDSIS 100
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVN-GRPLDSSFQRSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AvnPRKTVREILR--EPMRHLLSLKKSEQLARASEMLKAVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI- 174
Cdd:TIGR00956 848 L--PTSTVRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEMEsyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180
....*....|....*....|...
gi 16131352 175 LDEAVSNLDLVLQAGVIRLLKKL 197
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-230 |
1.09e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVlNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRK-------AFrrdiqmvfqdS 98
Cdd:NF033858 281 AV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRrvgymsqAF----------S 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 99 ISAvnpRKTVREILrepMRH--LLSLKKSEQLARASEMLKAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:NF033858 350 LYG---ELTVRQNL---ELHarLFHLPAAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 177 EAVSNLDLVLQAGVIRLLKKLQQQFG-TacLFI-THDLRLVERfCQRVMVMDNGQI 230
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGvT--IFIsTHFMNEAER-CDRISLMHAGRV 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-212 |
1.17e-11 |
|
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: 63.15 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 36 KSGETVALLGRSGCGKSTLARLLVGLESP----AQGNISW-------RGEPL----AKLNRAQRKAFRRdIQMVfqDSIS 100
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPnlgkFDDPPDWdeildefRGSELqnyfTKLLEGDVKVIVK-PQYV--DLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 101 AVNPRKtVREILrepmrhllslKKSEQLARASEMLKAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:cd03236 101 KAVKGK-VGELL----------KKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|..
gi 16131352 181 NLDLVLQAGVIRLLKKLQQQfGTACLFITHDL 212
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDL 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-177 |
1.67e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 6 ISGLSHHYahggfnGKHQhqaVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnraqrK 85
Cdd:NF033858 4 LEGVSHRY------GKTV---ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 86 AFRRdiqmvfqdsisAVNPR---------K------TVREIL----RepmrhLLSLKKSEQLARASEMLKAVDLdDSVLD 146
Cdd:NF033858 69 RHRR-----------AVCPRiaympqglgKnlyptlSVFENLdffgR-----LFGQDAAERRRRIDELLRATGL-APFAD 131
|
170 180 190
....*....|....*....|....*....|..
gi 16131352 147 kRPP-QLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:NF033858 132 -RPAgKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-232 |
4.66e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 29 NNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKlnRAQRKAFRRDIQMVFQdsisavNPRKT- 107
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKKGMAYITE------SRRDNg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 --VREILREPMRHLLSLKK------------SEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDggykgamglfheVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-232 |
7.18e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 20 GKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplAKLnraqrkafrrdiqmvfqDSI 99
Cdd:PRK13545 32 KDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AAL-----------------IAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SA-VNPRKTVREILrEPMRHLLSLKKSEQLARASEMLKAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:PRK13545 93 SSgLNGQLTGIENI-ELKGLMMGLTKEKIKEIIPEIIEFADI-GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 179 VSNLDlvlQAGVIRLLKKLQQ--QFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK13545 171 LSVGD---QTFTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-246 |
1.45e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsiSAVNPRK 106
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQ---SPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPMRHLLSLKKSEQLARAsEMLKAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
Cdd:PLN03232 1325 TVRFNI-DPFSEHNDADLWEALERA-HIKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131352 183 DLVLQAGVIRLLKklqQQFGTAC-LFITHDLRLVERfCQRVMVMDNGQIVETQVVGEKLTFSSDA 246
Cdd:PLN03232 1403 DVRTDSLIQRTIR---EEFKSCTmLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-219 |
1.80e-10 |
|
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: 60.72 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 24 HQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrGEPLaklnraqrkafrrDIQMVFQdSISAVN 103
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLAYVDQ-SRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 104 PRKTVREILREPMRHLLsLKKSEQLARAseMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIK-LGKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131352 184 L-VLQAgvirlLKKLQQQFGTACLFITHDLRLVERFC 219
Cdd:TIGR03719 476 VeTLRA-----LEEALLNFAGCAVVISHDRWFLDRIA 507
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-232 |
3.17e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEplaklnraqrkafrrdiqmVFQDSISA-VNPRK 106
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------------VSVIAISAgLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRhLLSLKKSEQLARASEMLKAVDLDDSVLdkRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlv 185
Cdd:PRK13546 101 TGIENIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIY--QPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 186 lQAGVIRLLKKLQQ--QFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
Cdd:PRK13546 176 -QTFAQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-232 |
8.15e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQrkaFRRDIQMVFQdsiSAVNPRK 106
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKVLGIIPQ---APVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPMRHLLSLKKSEQLARASemLKAV------DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:PLN03130 1328 TVRFNL-DPFNEHNDADLWESLERAH--LKDVirrnslGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131352 181 NLDLVLQAgVIRllKKLQQQFgTAC--LFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PLN03130 1404 AVDVRTDA-LIQ--KTIREEF-KSCtmLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-215 |
1.30e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISW-RGEPLAKLNRAQRKAFRRDiqmvfqdsisavnpr 105
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFLRAD--------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 ktvreilREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:PRK10636 392 -------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180 190
....*....|....*....|....*....|
gi 16131352 186 LQAGVIRLLKklqqQFGTACLFITHDLRLV 215
Cdd:PRK10636 465 MRQALTEALI----DFEGALVVVSHDRHLL 490
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-184 |
1.55e-09 |
|
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: 57.17 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplaklnraqrkafrrdiQMVFQDSISAVNPrK 106
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------------RISFSSQFSWIMP-G 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVRE-----ILREPMRHLlSLKKSEQLARasEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:cd03291 113 TIKEniifgVSYDEYRYK-SVVKACQLEE--DITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
...
gi 16131352 182 LDL 184
Cdd:cd03291 190 LDV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-245 |
2.60e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGL-ESPAQGNISWRGEPLAKLNRAQ---------------------R 84
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQdyqgdeeqnvgmknvnefsltK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 85 KAFRRDIQMVFQDS----ISAVN----PRKTVREIL----REPMRHLLSLKKSEQLARASEMLKAVDLD------DSVLD 146
Cdd:PTZ00265 1263 EGGSGEDSTVFKNSgkilLDGVDicdyNLKDLRNLFsivsQEPMLFNMSIYENIKFGKEDATREDVKRAckfaaiDEFIE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 147 KRPPQ-----------LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
Cdd:PTZ00265 1343 SLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
250 260 270
....*....|....*....|....*....|....
gi 16131352 216 ERfCQRVMVMDN----GQIVETQVVGEKLTFSSD 245
Cdd:PTZ00265 1423 KR-SDKIVVFNNpdrtGSFVQAHGTHEELLSVQD 1455
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-211 |
3.15e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGE-PLAKLNRAQRKAFRRDIQMV---------FQ 96
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEYVidgdreyrqLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 DSISAVNPRKTVREIlrePMRH--LLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
Cdd:PRK10636 96 AQLHDANERNDGHAI---ATIHgkLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131352 175 LDEAVSNLDLvlqAGVIRLLKKLQQQFGTACLfITHD 211
Cdd:PRK10636 173 LDEPTNHLDL---DAVIWLEKWLKSYQGTLIL-ISHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-211 |
3.50e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNIswRGEPLAKlnraqrkafrrdIQMVFQDSisAVNPRK 106
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--RPAPGIK------------VGYLPQEP--QLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILREPMRHLLSLKK-----SEQLAR--------ASEM------LKAVDLDDsvLDKR----------PP------Q 151
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDrfneiYAAYAEpdadfdalAAEQgelqeiIDAADAWD--LDSQleiamdalrcPPwdakvtK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHD 211
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-233 |
8.42e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLE--SPAQGNISWRGEPLAKLNRAQRKAfrRDIQMVFQDSISAv 102
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG--EGIFMAFQYPVEI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 103 nPRKTVREILREPMRHLLSLKKSEQLARasemlkaVDLDDSVLDK-----RPPQL---------SGGQLQRVCLARALAV 168
Cdd:PRK09580 91 -PGVSNQFFLQTALNAVRSYRGQEPLDR-------FDFQDLMEEKiallkMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 169 EPKLLILDEAVSNLD---LVLQAGVIRLLKKLQQQFgtacLFITHDLRLVERF-CQRVMVMDNGQIVET 233
Cdd:PRK09580 163 EPELCILDESDSGLDidaLKIVADGVNSLRDGKRSF----IIVTHYQRILDYIkPDYVHVLYQGRIVKS 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-231 |
1.05e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 22 HQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLE--SPAQGNISWRGEPLAklNRAQRKAFRRDIQMVFQDsi 99
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVD--VSTVSDAIDAGLAYVTED-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 savnpRKTVREILREPMRHLLSLKKSEQLARAS------EMLKAVDLDDSVLDKRPP------QLSGGQLQRVCLARALA 167
Cdd:NF040905 346 -----RKGYGLNLIDDIKRNITLANLGKVSRRGvideneEIKVAEEYRKKMNIKTPSvfqkvgNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-185 |
1.24e-08 |
|
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: 55.69 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGeplaklnraqrkafrrdiQMVFQDSISAVNPrK 106
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------------RISFSPQTSWIMP-G 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrepmrhLLSLKKSEqlARASEMLKAVDL----------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
Cdd:TIGR01271 502 TIKDNI------IFGLSYDE--YRYTSVIKACQLeedialfpekDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
....*....
gi 16131352 177 EAVSNLDLV 185
Cdd:TIGR01271 574 SPFTHLDVV 582
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
28-251 |
1.94e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLArLLVGLESPAQGNISWRGEPLAKLNRAQRKAF--RRDIQMVFQDSISAvnpR 105
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIg*HRPVR*GRRESFSG---R 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 106 KTVREILREpmrhlLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
Cdd:NF000106 105 ENLYMIGR*-----LDLSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLTfsSDAGRVLQ 251
Cdd:NF000106 179 TRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT--KVGGRTLQ 241
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-232 |
2.34e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRaqrKAFRRDIQMVFQDSI------- 99
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL---RELRRQFSMIPQDPVlfdgtvr 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SAVNP--RKTVREILREpmRHLLSLKksEQLARASEmlkavDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLIL-D 176
Cdd:PTZ00243 1402 QNVDPflEASSAEVWAA--LELVGLR--ERVASESE-----GIDSRVLEG-GSNYSVGQRQLMCMARALLKKGSGFILmD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131352 177 EAVSNLDLVLQagvirllKKLQQQFGTA-----CLFITHDLRLVERfCQRVMVMDNGQIVE 232
Cdd:PTZ00243 1472 EATANIDPALD-------RQIQATVMSAfsaytVITIAHRLHTVAQ-YDKIIVMDHGAVAE 1524
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-224 |
3.84e-08 |
|
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: 51.80 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 35 LKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklnraqrkafrrdiqmvfqdsisaVNPRKTvreilre 114
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------YKPQYI------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 115 pmrhllslkkseqlarasemlkavdlddsvldkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLL 194
Cdd:cd03222 71 ------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|
gi 16131352 195 KKLQQQFGTACLFITHDLRLVERFCQRVMV 224
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-184 |
7.08e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.22 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLnraQRKAFRRDIQMVFQDSISAVNprk 106
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPILFSG--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 107 TVREILrEPMRHLL--SLKKSEQLARASEMLKAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
Cdd:cd03288 110 SIRFNL-DPECKCTddRLWEALEIAQLKNMVKSLPGGlDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
.
gi 16131352 184 L 184
Cdd:cd03288 189 M 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-184 |
7.95e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 26 AVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDsISAVnpr 105
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKAD-LSTL--- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 106 ktvreilrEPMRHLLSLKKSEQLARASEMLKAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:PRK13543 101 --------ENLHFLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-210 |
9.48e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLeSPAQGNISWRGEPLAKLNRAQRKAFRRdiqmvfqdsisavnp 104
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAKGKLFYVPQRPYMTL--------------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLD---------DSVLDKRPpQLSGGQLQRVCLARALAVEPKLLIL 175
Cdd:TIGR00954 529 -GTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLThilereggwSAVQDWMD-VLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 16131352 176 DEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITH 210
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-184 |
1.44e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLL---------------------VG-----LESPAQGNISWRG--EPLAK 78
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqilhveqevVGddttaLQCVLNTDIERTQllEEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 79 LNRAQRKAfrrDIQMVFQDSISAVN---PRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGG 155
Cdd:PLN03073 272 LVAQQREL---EFETETGKGKGANKdgvDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGG 348
|
170 180
....*....|....*....|....*....
gi 16131352 156 QLQRVCLARALAVEPKLLILDEAVSNLDL 184
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-211 |
1.91e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISwRGeplAKLNRAQRKAFRrdiqmvfqdsiSAVNPRKT 107
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CG---TKLEVAYFDQHR-----------AELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREIL----REPM-----RHLLSLkkseqL-------ARASEMLKAvdlddsvldkrppqLSGGQLQRVCLARALAVEPK 171
Cdd:PRK11147 400 VMDNLaegkQEVMvngrpRHVLGY-----LqdflfhpKRAMTPVKA--------------LSGGERNRLLLARLFLKPSN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131352 172 LLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
Cdd:PRK11147 461 LLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-231 |
3.33e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHhyahgGFNGKhqhqAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRgeplaklNRAQ 83
Cdd:PRK15064 320 LEVENLTK-----GFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-------ENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIQMVFQDSISavnprktvreiLREPMRHLLSLKKSEQLARAS--EMLkaVDLDDsvLDKRPPQLSGGQLQRVC 161
Cdd:PRK15064 384 IGYYAQDHAYDFENDLT-----------LFDWMSQWRQEGDDEQAVRGTlgRLL--FSQDD--IKKSVKVLSGGEKGRML 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 162 LARALAVEPKLLILDEAVSNLDL----VLQAGvirlLKKLQqqfGTaCLFITHDLRLVERFCQRVMVMDNGQIV 231
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMesieSLNMA----LEKYE---GT-LIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
30-230 |
8.17e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 30 NVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISW-RGEPLAKLNRAQRkAFR--RDIQMVFQ---------- 96
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQF-AFEefTVLDTVIMghtelwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 97 --DSISAvNPRKTVREILR--EpmrhlLSLKKSE-----QLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
Cdd:PRK15064 98 erDRIYA-LPEMSEEDGMKvaD-----LEVKFAEmdgytAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 168 VEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:PRK15064 172 SNPDILLLDEPTNNLDI----NTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-183 |
1.02e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQdsisavnp 104
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 rKTVREilrepmrhllSLKKSEQLARASEMLKAV----DLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
Cdd:PRK13541 85 -MTVFE----------NLKFWSEIYNSAETLYAAihyfKLHD-LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
...
gi 16131352 181 NLD 183
Cdd:PRK13541 153 NLS 155
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-230 |
1.05e-06 |
|
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: 49.63 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLaklnRAQRKAFRRDIQMVFQDSIsaVNPRKT 107
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI--LFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREilrepmrHLL---SLKKSEQLARASEMlKAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSN 181
Cdd:TIGR01257 1020 VAE-------HILfyaQLKGRSWEEAQLEM-EAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131352 182 LDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
Cdd:TIGR01257 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
4-217 |
1.05e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 4 LNISGLSHHYahggfngkhqhqavLNNVSLTLKSGETVALLGRSGCGKSTLarLLVGLESPAQgniswrgeplAKLNRAQ 83
Cdd:cd03238 1 LTVSGANVHN--------------LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK----------ARLISFL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 84 RKAFRRDIqmVFQDSISAvnprktvreilrepmrhllslkkseqlarasemLKAVDLDDSVLDKRPPQLSGGQLQRVCLA 163
Cdd:cd03238 55 PKFSRNKL--IFIDQLQF---------------------------------LIDVGLGYLTLGQKLSTLSGGELQRVKLA 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131352 164 RALAVEPK--LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVER 217
Cdd:cd03238 100 SELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS 154
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-195 |
1.58e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPA--QGNISWRGEPlaklnrAQRKAFRRDIQMVFQDSISAvnP 104
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP------KKQETFARISGYCEQNDIHS--P 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 105 RKTVRE--ILREPMRHLLSLKKSEQLARASEMLKAVDLD---DSVLDkRP--PQLSGGQLQRVCLARALAVEPKLLILDE 177
Cdd:PLN03140 967 QVTVREslIYSAFLRLPKEVSKEEKMMFVDEVMELVELDnlkDAIVG-LPgvTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170
....*....|....*...
gi 16131352 178 AVSNLDLVLQAGVIRLLK 195
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVR 1063
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-253 |
5.98e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQ-GNISWRGEplaklnraqrKAFRRDIQMVFQDSI------- 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGS----------VAYVPQVSWIFNATVrenilfg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 100 SAVNPRKTVREILREPMRHLLSLKKSEQLARASEmlkavdlddsvldkRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
Cdd:PLN03232 703 SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGE--------------RGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFcQRVMVMDNGQIVETQVVGEKLTFSSDAGRVLQNA 253
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA 840
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-224 |
6.84e-06 |
|
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: 45.06 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 37 SGETVALLGRSGCGKSTLARLLVGLESPAQGNISwrgeplaklnraqrkafrrdiqmvfqdSISAVNPRKTVREILREPM 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------YIDGEDILEEVLDQLLLII 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 117 RHllslkkseqlarasemlkavdlddsvldKRPPQLSGGQLQRVCLARALAVEPKLLILDEA-----VSNLDLVLQAGVI 191
Cdd:smart00382 54 VG----------------------------GKKASGSGELRLRLALALARKLKPDVLILDEItslldAEQEALLLLLEEL 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131352 192 RLLKKLQQQFGTACLFITHDLR------LVERFCQRVMV 224
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVL 144
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-211 |
8.95e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 28 LNNVSLTLKSGETVALLGRSGCGKSTLA----------RLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDiqmvfQD 97
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAID-----QK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 98 SISaVNPRKTVREI--LREPMRHLLSLkksEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK--LL 173
Cdd:cd03270 86 TTS-RNPRSTVGTVteIYDYLRLLFAR---VGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLY 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131352 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHD 211
Cdd:cd03270 162 VLDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHD 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-183 |
1.34e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 29 NNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWrGEplaklnraqrkafrrDIQMVFQD-SISAVNPRKT 107
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE---------------TVKLAYVDqSRDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 108 VREILREPMRHLLsLKKSEQLARA---------SEMLKAVDlddsvldkrppQLSGGQLQRVCLARALAVEPKLLILDEA 178
Cdd:PRK11819 405 VWEEISGGLDIIK-VGNREIPSRAyvgrfnfkgGDQQKKVG-----------VLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
....*
gi 16131352 179 VSNLD 183
Cdd:PRK11819 473 TNDLD 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-233 |
1.91e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 25 QAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAklNRAQRKAFRRDIQMV---------- 94
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN--NHNANEAINHGFALVteerrstgiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 95 ------FQDSISAVNPRKTvreilrePMRhLLSLKKSEqlaraSEMLKAVDlddSVLDKRPPQ------LSGGQLQRVCL 162
Cdd:PRK10982 339 ayldigFNSLISNIRNYKN-------KVG-LLDNSRMK-----SDTQWVID---SMRVKTPGHrtqigsLSGGNQQKVII 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131352 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ---IVET 233
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDT 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
127-210 |
4.61e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 127 QLARASEMLKAVDLDDSVLDKRPPQLSGGQlQRVCL-ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAC 205
Cdd:PRK10938 377 QQKLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQL 455
|
....*
gi 16131352 206 LFITH 210
Cdd:PRK10938 456 LFVSH 460
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
150-218 |
1.94e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131352 150 PQLSGGQLQRVCLARALAVEPK----LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERF 218
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQV-IVITHLPELAELA 147
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
22-69 |
2.28e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 16131352 22 HQHQAVLNNVsltLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNI 69
Cdd:PRK01889 182 GEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
27-76 |
2.05e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 38.50 E-value: 2.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 16131352 27 VLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGN-ISWRGEPL 76
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDAL 52
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
152-229 |
4.97e-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: 37.25 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131352 152 LSGGQLQRVCLARALAVEPKL----------LILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQR 221
Cdd:cd03279 124 LSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTE-NRMVGVISHVEELKERIPQR 202
|
....*...
gi 16131352 222 VMVMDNGQ 229
Cdd:cd03279 203 LEVIKTPG 210
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
37-81 |
6.80e-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: 6.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 16131352 37 SGETVALLGRSGCGKSTLARLLVGLESPAQGNISwrgeplAKLNR 81
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS------EKLGR 122
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
151-196 |
8.49e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 8.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131352 151 QLSGGQLQR---VCLARALA----------VEPKLLILDEAVSNLDLVLQAGVIRLLKK 196
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| |
