|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-338 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 575.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 241 VRQISQ-EGADDAFDPTLAGELNGAVIKLTFVGHSTHQPVVGELTLRYGLPFNILHGKMTQTAHGVFGQLWLHVVATPEQ 319
Cdd:COG1135 241 LPTVLNdELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*....
gi 495163008 320 LENILADLRLHEIHCEVIK 338
Cdd:COG1135 321 IDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-339 |
8.26e-176 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 490.85 E-value: 8.26e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 241 VRQISQEGADDAFDPTLAGEL---NGAVIKLTFVGHSTHQPVVGELTLRYGLPFNILHGKMTQTAHGVFGQLWLHVVATP 317
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPttgSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|..
gi 495163008 318 EQLENILADLRLHEIHCEVIKH 339
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVEVLGY 342
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
3.56e-151 |
|
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: 424.30 E-value: 3.56e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-337 |
1.04e-119 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 348.80 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 241 VRQISQEGADDAFDPTLAGELNGA---VIKLTFVGHSTHQPVVGELTLRYGLPFNILHGKMTQTAHGVFGQLWLHVVATP 317
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADsvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330 340
....*....|....*....|
gi 495163008 318 EQLENILADLRLHEIHCEVI 337
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVL 340
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
1.01e-101 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 298.83 E-value: 1.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAaRGESLRQA 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFS-MQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 495163008 240 FVRQI 244
Cdd:COG1126 235 FLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
6.82e-101 |
|
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: 306.44 E-value: 6.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQ-GKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQ 79
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLKISMVFQH----FNLLWsrTVSENIAFSMQIAGV-PKAEIKTRVAELIDLVGLKGR-ENAYPSRLSGGQKQRVGIAR 153
Cdd:COG1123 340 LRRRVQMVFQDpyssLNPRM--TVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 495163008 234 QPITRQ 239
Cdd:COG1123 498 HPYTRA 503
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.75e-96 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 285.40 E-value: 1.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RL-KISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRkICDRVAVMENGRVVEE 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
4.22e-92 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 273.85 E-value: 4.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
1.19e-91 |
|
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: 272.83 E-value: 1.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LK-ISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRkICDRVAVMENGRV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
5.84e-91 |
|
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: 271.85 E-value: 5.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSM-QIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVlQVFTHPQQPITRQ 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP-EELLASDDPWVRQ 239
|
..
gi 495163008 240 FV 241
Cdd:COG1127 240 FL 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
1.09e-90 |
|
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: 273.85 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKP---TSGSVTVAGKEISAARGESL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARLK-ISMVFQH----FNLLWsrTVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGL---KGRENAYPSRLSGGQKQR 148
Cdd:COG0444 81 RKIRGReIQMIFQDpmtsLNPVM--TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 149 VGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250
....*....|
gi 495163008 229 FTHPQQPITR 238
Cdd:COG0444 239 FENPRHPYTR 248
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-238 |
4.67e-90 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.04 E-value: 4.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslrqa 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 rlkISMVFQHFNLL-WsRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:COG1116 82 ---RGVVFQEPALLpW-LTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMH-VVRkICDRVAVMEN--GRVVEEGDVlqVFTHPQQPI 236
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVEEIDV--DLPRPRDRE 234
|
..
gi 495163008 237 TR 238
Cdd:COG1116 235 LR 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
8.88e-88 |
|
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: 263.97 E-value: 8.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQa 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 rlKISMVFQH----FNLLWsrTVSENIAFSMQIAGVPkaEIKTRVAELIDLVGLKGRE-NAYPSRLSGGQKQRVGIARAL 155
Cdd:COG1124 80 --RVQMVFQDpyasLHPRH--TVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 156 ANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQP 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*..
gi 495163008 236 ITRQFVR 242
Cdd:COG1124 234 YTRELLA 240
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
9.25e-87 |
|
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: 260.73 E-value: 9.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQAR 81
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
1.46e-86 |
|
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: 260.13 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQH----FNLLWsrTVSENIAFSMQIAGVP--KAEIKTRVAELIDLVGL-KGRENAYPSRLSGGQKQRVGIAR 153
Cdd:cd03257 81 RKEIQMVFQDpmssLNPRM--TIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-242 |
2.71e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 265.04 E-value: 2.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLF-----------HQGKD----------TItAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTS 59
Cdd:COG4175 3 KIEVRNLYKIFgkrperalkllDQGKSkdeilektgqTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 60 GSVTVAGKEISAARGESLRQARL-KISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYP 138
Cdd:COG4175 82 GEVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 139 SRLSGGQKQRVGIARALANRPDVLLCDEATSALDP------QttDQILDLLQDINRrfglTIVLITHEMHVVRKICDRVA 212
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremQ--DELLELQAKLKK----TIVFITHDLDEALRLGDRIA 235
|
250 260 270
....*....|....*....|....*....|
gi 495163008 213 VMENGRVVEEGDVLQVFTHPQQPITRQFVR 242
Cdd:COG4175 236 IMKDGRIVQIGTPEEILTNPANDYVADFVE 265
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-244 |
2.40e-85 |
|
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: 258.34 E-value: 2.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLK-ISMVFQHFNLLWSRT 98
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFVRQI 244
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-225 |
6.03e-84 |
|
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: 253.16 E-value: 6.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslrqar 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHFNLL-WsRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03293 75 --RGYVFQQDALLpW-LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMEN--GRVVEEGDV 225
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-238 |
6.85e-84 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 256.97 E-value: 6.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISK-------LFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARG 74
Cdd:COG4608 8 LEVRDLKKhfpvrggLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 75 ESLRQARLKISMVFQH-FNLLWSR-TVSENIAFSMQIAGV-PKAEIKTRVAELIDLVGLKgRE--NAYPSRLSGGQKQRV 149
Cdd:COG4608 88 RELRPLRRRMQMVFQDpYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLR-PEhaDRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
....*....
gi 495163008 230 THPQQPITR 238
Cdd:COG4608 247 ARPLHPYTQ 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-240 |
4.27e-82 |
|
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: 248.96 E-value: 4.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAR 81
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSM-QIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHpQQPITRQF 240
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-225 |
2.44e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 246.90 E-value: 2.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslRQAR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
3.15e-79 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 242.27 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENI-------------AFSMqiagVPKAEiKTRVAELIDLVGLKGRENAYPSRLSGGQKQ 147
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPED-RERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 148 RVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-261 |
4.99e-79 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 242.74 E-value: 4.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGkdT---ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLR 78
Cdd:TIGR04521 1 IKLKNVSYIYQPG--TpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 79 QARLKISMVFQhF--NLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKgrENAY---PSRLSGGQKQRVGIAR 153
Cdd:TIGR04521 79 DLRKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLD--EEYLersPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 495163008 234 Q--------PITRQFVRQISQEGADDAFDPTLAGEL 261
Cdd:TIGR04521 236 ElekigldvPEITELARKLKEKGLPVPKDPLTVEEA 271
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-233 |
1.37e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 244.24 E-value: 1.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISA----ARGes 76
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppeKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 lrqarlkISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG3842 79 -------VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITH------EMhvvrkiCDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeealAL------ADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 495163008 231 HPQ 233
Cdd:COG3842 226 RPA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
1.40e-77 |
|
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: 236.66 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHqgkdTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAaRGESLRQAR 81
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFS-MQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
2.08e-76 |
|
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: 233.57 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeSLRQAR 81
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-----GVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
2.51e-75 |
|
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: 230.82 E-value: 2.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 3 VLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARL 82
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK---LSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 83 KISMVFQHFNL-LWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
1.40e-73 |
|
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: 235.95 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGkdTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPT---SGSVTVAGKEISAARgESL 77
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS-EAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARlkISMVFQHF-NLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG1123 81 RGRR--IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQ 234
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-239 |
2.06e-73 |
|
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: 236.12 E-value: 2.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKS----TLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQ 79
Cdd:COG4172 9 VEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 AR-LKISMVFQH----FNLLWsrTVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGL---KGRENAYPSRLSGGQKQRVG 150
Cdd:COG4172 89 IRgNRIAMIFQEpmtsLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
....*....
gi 495163008 231 HPQQPITRQ 239
Cdd:COG4172 247 APQHPYTRK 255
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
5.05e-72 |
|
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: 223.60 E-value: 5.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAR 81
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSM--------QIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR 153
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
5.47e-72 |
|
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: 223.33 E-value: 5.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENA--YPSRLSGGQKQRVGIARALANRP 159
Cdd:cd03295 76 -KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdrYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 495163008 240 FVRQ 243
Cdd:cd03295 235 FVGA 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
9.67e-72 |
|
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: 220.52 E-value: 9.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEsLRQAR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFsmqiagvpkaeiktrvaelidlvglkgrenaypsRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-239 |
1.12e-71 |
|
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: 231.50 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 10 LFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEkPTSGSVTVAGKEISAARGESLRQARLKISMVFQ 89
Cdd:COG4172 291 LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 90 H-FNLLWSR-TVSENIAFSMQI--AGVPKAEIKTRVAELIDLVGLKGR-ENAYPSRLSGGQKQRVGIARALANRPDVLLC 164
Cdd:COG4172 370 DpFGSLSPRmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 165 DEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
1.36e-71 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 222.70 E-value: 1.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHqGKDTITAVDdvnLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGES---- 76
Cdd:PRK11264 3 AIEVKNLVKKFH-GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 -LRQARLKISMVFQHFNLLWSRTVSEN-IAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARA 154
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDI--NRRfglTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|.
gi 495163008 233 QQPITRQFVRQ 243
Cdd:PRK11264 236 QQPRTRQFLEK 246
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-241 |
1.47e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 225.80 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeSLRQaR 81
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL--PPRE-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:COG1118 76 -RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
1.50e-71 |
|
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: 222.17 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENI-----AFSMQIAGV----PKAEiKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLlgrfSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 152 ARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
2.58e-71 |
|
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: 222.69 E-value: 2.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeISAARGESLRQAR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTH 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
2.00e-70 |
|
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: 218.43 E-value: 2.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAR 81
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
6.40e-69 |
|
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: 216.06 E-value: 6.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslRQA 80
Cdd:COG0411 4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH--RIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQ----------IAGVPK-----AEIKTRVAELIDLVGLKGRENAYPSRLSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 146 KQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 495163008 226 LQVFTHPQ 233
Cdd:COG0411 238 AEVRADPR 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
2.44e-68 |
|
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: 213.64 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargesLRQAR 81
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-245 |
9.95e-68 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 212.65 E-value: 9.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgESLRQA 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK-VDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFS-MQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*.
gi 495163008 240 FVRQIS 245
Cdd:PRK09493 235 FLQHVS 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
4.68e-67 |
|
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: 210.37 E-value: 4.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISA------ARg 74
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 75 esLRQARlkISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEikTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARA 154
Cdd:COG4181 87 --LRARH--VGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEE 222
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
6.10e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 214.17 E-value: 6.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS----AARGes 76
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppKDRN-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 lrqarlkISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG3839 77 -------IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
24-240 |
1.40e-66 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 210.04 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGES----------LRQARLKISMVFQHFNL 93
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqLQRIRTRLGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 lWS-RTVSENIAFS-MQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:COG4598 107 -WShMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 172 DPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQF 240
Cdd:COG4598 186 DPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
7.64e-66 |
|
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: 207.03 E-value: 7.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEK-----PTSGSVTVAGKEISAaRGES 76
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYD-LDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LRQARLKISMVFQHFNLLWSrTVSENIAFSMQIAGV-PKAEIKTRVAELIDLVGLKGREN--AYPSRLSGGQKQRVGIAR 153
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-240 |
1.17e-64 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 204.48 E-value: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLF--HQgkdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAG------KEISAAR 73
Cdd:PRK11124 3 IQLNGINCFYgaHQ------ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 74 GESLRQarlKISMVFQHFNLLWSRTVSEN-IAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIA 152
Cdd:PRK11124 77 IRELRR---NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 153 RALANRPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVlQVFTHP 232
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
....*...
gi 495163008 233 QqpiTRQF 240
Cdd:PRK11124 232 Q---TEAF 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-240 |
1.41e-64 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 204.48 E-value: 1.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAG------KEISAARGE 75
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 SLRQarlKISMVFQHFNLLWSRTVSEN-IAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARA 154
Cdd:COG4161 79 LLRQ---KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDvLQVFTHPQq 234
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ- 232
|
....*.
gi 495163008 235 piTRQF 240
Cdd:COG4161 233 --TEAF 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-233 |
5.26e-64 |
|
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: 202.67 E-value: 5.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeSLRQARLK 83
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENI----------AFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR 153
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-241 |
7.80e-63 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 200.26 E-value: 7.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL--EKP---TSGSVTVAGKEISAaRGESLRQARLKISMVFQHFNLL 94
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 wSRTVSENIAFSMQIAGV-PKAEIKTRVAELIDLVGL----KGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:COG1117 105 -PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 170 ALDPQTTDQILDLLQDINRRFglTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:COG1117 184 ALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
1.15e-62 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 199.70 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargESLRQA 80
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
5.42e-62 |
|
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: 197.56 E-value: 5.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaarGESLRQAr 81
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT---DVPVQER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLLWSRTVSENIAFSMQI----AGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:cd03296 75 -NVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPIT 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 495163008 238 RQFV 241
Cdd:cd03296 234 YSFL 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
6.29e-62 |
|
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: 195.31 E-value: 6.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslRQAR 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP----EEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIafsmqiagvpkaeiktrvaelidlvglkgrenaypsRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
1.70e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 196.46 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISkLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaargeslRQA 80
Cdd:COG1121 6 AIELENLT-VSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSR--TVSENIAF----SMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARA 154
Cdd:COG1121 74 RRRIGYVPQRAEVDWDFpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMeNGRVVEEGDVLQVFTHP 232
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.78e-60 |
|
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: 193.36 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaaRGESlRQAR 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREP-REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-238 |
2.90e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 193.64 E-value: 2.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 7 ISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLKISM 86
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 87 VFQH-FNLLWSR-TVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGLK----GRenaYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK11308 97 VFQNpYGSLNPRkKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRpehyDR---YPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITR 238
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-234 |
6.54e-59 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 191.00 E-value: 6.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARLKISMVFQH-FNLLWSRT 98
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---ETVWDVRRQVGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHPQQ 234
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
2.03e-58 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 190.26 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsAARGESLRQARLKISMVFQHFNL-LWSRT 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYqLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAGVPKAEIKTRVAELIDLVGLK--GRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163008 177 DQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-242 |
3.69e-58 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 188.64 E-value: 3.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARG----------ESLRQARLKISMVFQHFNL 93
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 LWSRTVSENIAFS-MQIAGVPKAEIKTRVAELIDLVGLKGRENA-YPSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:PRK10619 104 WSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 172 DPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFVR 242
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-238 |
3.83e-58 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 190.69 E-value: 3.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLK 83
Cdd:PRK15079 20 IKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQhfNLLWS----RTVSENIAFSMQI--AGVPKAEIKTRVAELIDLVGLKGRE-NAYPSRLSGGQKQRVGIARALA 156
Cdd:PRK15079 100 IQMIFQ--DPLASlnprMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPI 236
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
..
gi 495163008 237 TR 238
Cdd:PRK15079 258 TK 259
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-227 |
5.63e-57 |
|
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: 184.25 E-value: 5.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslRQAR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR----KAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDInrRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQ 227
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
8.45e-57 |
|
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: 195.82 E-value: 8.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMqiAGVPKAEIKT--RVAELIDLV-----GLKGR--ENAypSRLSGGQKQRVGIA 152
Cdd:COG2274 550 -QIGVVLQD-VFLFSGTIRENITLGD--PDATDEEIIEaaRLAGLHDFIealpmGYDTVvgEGG--SNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 153 RALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
2.05e-56 |
|
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: 183.71 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqA 80
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RlKISMVFQHFNLLWSRTVSENIAFS----MQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG1120 75 R-RIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-240 |
2.53e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 183.03 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTITAvddvNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargesLRQA 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-----LPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA-NRP 159
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 dVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:COG3840 150 -ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
.
gi 495163008 240 F 240
Cdd:COG3840 229 Y 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
2.86e-56 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 190.62 E-value: 2.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQA 80
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR---SPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 -RLKISMVFQHFNLLWSRTVSENIAFSMQIAG---VPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG3845 78 iALGIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
4.42e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 4.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDtitaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMQIAGVPKAEikTRVAELIDLVGLKGRENAYP-SRLSGGQKQRVGIARALANRPD 160
Cdd:COG4619 75 -QVAYVPQE-PALWGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
9.63e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 182.37 E-value: 9.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEI---SAARGesl 77
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADRG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 rqarlkisMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:COG4525 80 --------VVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITH 199
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-241 |
1.22e-55 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 185.81 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeSLRQARLK 83
Cdd:PRK11607 22 IRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLL 163
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 164 CDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-333 |
1.53e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 185.15 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESlRQar 81
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:PRK09452 88 --VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 242 RQIsqegadDAFDPTLAGELNGAVIKLTFVGHsthqpvvgELTLRYGLPFNIlhgkmtqtahgvfGQlWLHVVATPEqle 321
Cdd:PRK09452 246 GEI------NIFDATVIERLDEQRVRANVEGR--------ECNIYVNFAVEP-------------GQ-KLHVLLRPE--- 294
|
330
....*....|..
gi 495163008 322 nilaDLRLHEIH 333
Cdd:PRK09452 295 ----DLRVEEIN 302
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-241 |
3.14e-55 |
|
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: 180.22 E-value: 3.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtitaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeSLRQAR 81
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
6.33e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 181.37 E-value: 6.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAA-RGESLRQARLKISMVFQhF--NLLWS 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLkgrENAYPSR----LSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGL---PEELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 173 PQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQ--------PITRQFVRQI 244
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEleaigldlPETVKFKRAL 257
|
...
gi 495163008 245 SQE 247
Cdd:PRK13634 258 EEK 260
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
1.07e-54 |
|
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: 176.42 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFnLLWSRTVSENIafsmqiagvpkaeiktrvaelidlvglkgrenaypsrLSGGQKQRVGIARALANRPDV 161
Cdd:cd03228 77 -NIAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGR 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.29e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 179.80 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQA 80
Cdd:PRK13632 7 MIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFT 230
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-251 |
2.29e-54 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 179.54 E-value: 2.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQA 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVrKICDRVAVMENGRVVEEGDVLQVFTHPQQ----- 234
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDllqlg 238
|
250 260
....*....|....*....|
gi 495163008 235 ---PITRQFVRQISQEGADD 251
Cdd:PRK13650 239 ldiPFTTSLVQSLRQNGYDL 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
2.52e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 179.12 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 16 DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgESLRQARLKISMVFQHF-NLL 94
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEVRKTVGIVFQNPdDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQ 174
Cdd:PRK13639 92 FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 175 TTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-244 |
1.11e-53 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 181.38 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLK-ISMVFQHFNLLWSRT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFVRQI 244
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
1.21e-53 |
|
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: 175.52 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeSLRQAR 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-229 |
1.53e-53 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 177.20 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDT--ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgESLR 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 79 QARLKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-232 |
5.89e-53 |
|
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: 175.38 E-value: 5.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQG-----KDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGE 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 SLRQARLKISMVFQH----FNLlwSRTVSENIAFSMQ-IAGVPKAEIKTRVAELIDLVGLKGRE-NAYPSRLSGGQKQRV 149
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDspsaVNP--RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
....*
gi 495163008 230 T--HP 232
Cdd:TIGR02769 240 SfkHP 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
7.70e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 183.06 E-value: 7.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:COG1132 340 IEFENVS--FSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFnLLWSRTVSENIAFsmqiaGVPKA---EI-----KTRVAELID--------LVGLKGrenaypSRLSGGQ 145
Cdd:COG1132 415 -QIGVVPQDT-FLFSGTIRENIRY-----GRPDAtdeEVeeaakAAQAHEFIEalpdgydtVVGERG------VNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 146 KQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-241 |
9.42e-53 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 174.64 E-value: 9.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 5 RNISKLFH-----QGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAarGESLRQ 79
Cdd:COG4167 8 RNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--GDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLkISMVFQHFNLlwSRTVSENIAfsmQIAGVP--------KAEIKTRVAELIDLVGLKgRENA--YPSRLSGGQKQRV 149
Cdd:COG4167 86 CKH-IRMIFQDPNT--SLNPRLNIG---QILEEPlrlntdltAEEREERIFATLRLVGLL-PEHAnfYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250
....*....|..
gi 495163008 230 THPQQPITRQFV 241
Cdd:COG4167 239 ANPQHEVTKRLI 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-225 |
1.00e-52 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 180.98 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHqgkdTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQA 80
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR---SPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 -RLKISMVFQHFNLLWSRTVSENIAFSMQIAG---VPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:COG1129 77 qAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-232 |
1.85e-52 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.83 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargESLRQAR 81
Cdd:PRK11432 7 VVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:PRK11432 79 -DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
2.54e-52 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 174.53 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeslrqA 80
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-------D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKI-----------SMvfqhfnllwsrTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRV 149
Cdd:COG4152 70 RRRIgylpeerglypKM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV 228
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-220 |
5.20e-52 |
|
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: 171.18 E-value: 5.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaargeslRQARLKISMVFQHFNLLWSR- 97
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 -TVSENIAF----SMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:cd03235 85 iSVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163008 173 PQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMeNGRVV 220
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-224 |
4.11e-51 |
|
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: 169.15 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 12 HQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslRQARLKISMVFQHF 91
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 92 NLLWSRTVSENIAfsMQIAGVPKAEIKTRVAELIDLV-GLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:cd03224 85 RIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163008 171 LDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGD 224
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-276 |
5.37e-51 |
|
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: 172.98 E-value: 5.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkEI--SAARGESLRQARLKISMVFQHFNLLWSRTVS 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqDSARGIFLPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAFSMQIAgvPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQIL 180
Cdd:COG4148 96 GNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 181 DLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPqqpitrqfvrqisqegaddAFDPTLAGE 260
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP-------------------DLLPLAGGE 234
|
250
....*....|....*.
gi 495163008 261 LNGAVIKLTFVGHSTH 276
Cdd:COG4148 235 EAGSVLEATVAAHDPD 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-232 |
3.18e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 168.33 E-value: 3.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLKISMVFQH----FNLl 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisaVNP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 wSRTVSENIAFSMQ-IAGVPKAEIKTRVAELIDLVGLK-GRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK10419 105 -RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 173 PQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV--LQVFTHP 232
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVgdKLTFSSP 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-222 |
5.37e-50 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 166.53 E-value: 5.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 5 RNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEI----SAARGEsLRQA 80
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAE-LRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLkiSMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:PRK11629 88 KL--GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKIcDRVAVMENGRVVEE 222
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
1.30e-49 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 162.82 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHFNLLWSRTVS 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK---EIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 101 ENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGREN----AYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.31e-49 |
|
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: 173.79 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFsmqiaGVPKAEiKTRVAELIDLVGLKGRENAYP-----------SRLSGGQKQRVG 150
Cdd:COG4988 412 -QIAWVPQN-PYLFAGTIRENLRL-----GRPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRkICDRVAVMENGRVVEEGD 224
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
5.81e-49 |
|
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: 161.44 E-value: 5.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQgkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQA- 80
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA---SPRDAr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQhfnllwsrtvseniafsmqiagvpkaeiktrvaelidlvglkgrenaypsrLSGGQKQRVGIARALANRPD 160
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-223 |
7.98e-49 |
|
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: 161.83 E-value: 7.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISklFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLK 83
Cdd:cd03214 2 VENLS--VGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---SPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQhfnllwsrtvseniafsmqiagvpkaeiktrVAELIDLVGLKGRenaYPSRLSGGQKQRVGIARALANRPDVLL 163
Cdd:cd03214 75 IAYVPQ-------------------------------ALELLGLAHLADR---PFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 164 CDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-232 |
7.98e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 164.98 E-value: 7.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 10 LFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARLKISMVFQ 89
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 90 HFN-LLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEAT 168
Cdd:PRK13652 86 NPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 169 SALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
1.22e-48 |
|
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: 162.46 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVErGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAAR-GESLRQARLKISMVFQHFNLLWSRTVSE 101
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 102 NIAFSMQiaGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILD 181
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495163008 182 LLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-222 |
2.57e-48 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 161.97 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDdvnLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVT---FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINrRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-218 |
4.14e-48 |
|
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: 159.33 E-value: 4.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGkdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARLK 83
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK---LPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQhfnllwsrtvseniafsmqiagvpkaeiktrvaelidlvglkgrenaypsrLSGGQKQRVGIARALANRPDVLL 163
Cdd:cd00267 75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 164 CDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
4.74e-48 |
|
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: 161.00 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslRQA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP----AEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
9.43e-48 |
|
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: 160.71 E-value: 9.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqarlkisMVFQHFNLLWSRTVS 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAFSMQ--IAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV-FTHPQQ 234
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-264 |
1.21e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 164.10 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS--AARGEslrq 79
Cdd:PRK10851 3 IEIANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlHARDR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 arlKISMVFQHFNLLWSRTVSENIAFSMQIagVPK------AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR 153
Cdd:PRK10851 75 ---KVGFVFQHYALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
250 260 270
....*....|....*....|....*....|.
gi 495163008 234 QPITRQFVRQISQegaddafdptLAGELNGA 264
Cdd:PRK10851 230 TRFVLEFMGEVNR----------LQGTIRGG 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
1.62e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 162.95 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISK-----------------LFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVT 63
Cdd:COG4586 1 IIEVENLSKtyrvyekepglkgalkgLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 64 VAGKEISAARGESLRQarlkISMVF-QHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAyPSR-L 141
Cdd:COG4586 81 VLGYVPFKRRKEFARR----IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVRqL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 142 SGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVE 221
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
....
gi 495163008 222 EGDV 225
Cdd:COG4586 236 DGSL 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
2.96e-47 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 159.86 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFH------------------QGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSV 62
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 63 TVAGKeISAargesLrqarLKISMVFqHFNLlwsrTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLS 142
Cdd:COG1134 84 EVNGR-VSA-----L----LELGAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 143 GGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*....
gi 495163008 223 GDVLQVFTH 231
Cdd:COG1134 228 GDPEEVIAA 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
4.60e-47 |
|
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: 158.15 E-value: 4.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHqgkdTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeSLRQAR 81
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKtrvaELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
5.16e-47 |
|
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: 158.13 E-value: 5.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtitAVDDVNLEVERGqIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslrqAR 81
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDI--NRrfglTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELgeDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-223 |
7.99e-47 |
|
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: 158.65 E-value: 7.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 10 LFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlkISMVF- 88
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR----IGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 89 QHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLkGRENAYPSR-LSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPVRqLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 168 TSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-231 |
1.29e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 159.52 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKD-TITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISA-ARGESLRQ 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLKISMVFQhF--NLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKgrENAY---PSRLSGGQKQRVGIARA 154
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIS--ESLFeknPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTH 231
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
3.56e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 159.10 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDT-ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSV------------------ 62
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 63 TVAGKEISAARGESLRQA---RLKISMVFQHFNL-LWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLkgrENAY- 137
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIkeiRRRVGVVFQFAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL---DESYl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 138 ---PSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVM 214
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|
gi 495163008 215 ENGRVVEEGD 224
Cdd:PRK13651 239 KDGKIIKDGD 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-224 |
8.62e-46 |
|
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: 155.91 E-value: 8.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNIsklfHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqA 80
Cdd:COG0410 3 MLEVENL----HAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQH---FNLLwsrTVSENIAFSMQIAGvPKAEIKTRVAELIDL--VgLKGRENAYPSRLSGGQKQRVGIARAL 155
Cdd:COG0410 77 RLGIGYVPEGrriFPSL---TVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 156 ANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGD 224
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
4.59e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 155.39 E-value: 4.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 16 DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgESLRQARLKISMVFQH-FNLL 94
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-KGLMKLRESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQ 174
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 175 TTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-223 |
4.69e-45 |
|
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: 153.21 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeslrqARLK 83
Cdd:cd03269 3 VENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------ARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLL 163
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 164 CDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-201 |
5.81e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 154.09 E-value: 5.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEI---SAARGeslrqarlkisMVFQHFNLLWS 96
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpGAERG-----------VVFQNEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180
....*....|....*....|....*
gi 495163008 177 DQILDLLQDINRRFGLTIVLITHEM 201
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-259 |
7.68e-45 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 156.04 E-value: 7.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 18 ITAVDDVNLEVERGQIYGIIGYSGAGKS----TLIRLL--NGLekpTSGSVTVAGKEISAARGESLRQARL-KISMVFQH 90
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGR---IGGSATFNGREILNLPEKELNKLRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 --FNLLWSRTVSENIA-FSMQIAGVPKAEIKTRVAELIDLVGL---KGRENAYPSRLSGGQKQRVGIARALANRPDVLLC 164
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMeVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 165 DEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFVRQI 244
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
250
....*....|....*
gi 495163008 245 SQEGADDAFDPTLAG 259
Cdd:PRK09473 266 PRLDAEGESLLTIPG 280
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-248 |
1.79e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 153.83 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARG-ESLRQARLKISMVFQhF--NLLWSR 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQ-FpeAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGR-ENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 177 DQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ--------QPITRQFVRQISQEG 248
Cdd:PRK13641 182 KEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSRFASKLEKGG 260
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
3.57e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.81 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargESLRQAR 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
4.37e-44 |
|
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: 150.72 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslrQARLKISMVFQHFNLLWSRTVSEN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL 182
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163008 183 LQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-225 |
5.12e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 152.58 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 7 ISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARLKISM 86
Cdd:PRK13647 7 VEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 87 VFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCD 165
Cdd:PRK13647 84 VFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 166 EATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-229 |
1.09e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 151.86 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKD-TITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISA-ARGESLRQ 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLKISMVFQhF--NLLWSRTVSENIAFSMQIAGVPKAEIKTRVAEL-IDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:PRK13646 83 VRKRIGMVFQ-FpeSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLlMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.45e-43 |
|
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: 157.62 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAr 81
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHfNLLWSRTVSENIAFsmqiaGVPKAEiKTRVAELIDLVGLKGRENAYP-----------SRLSGGQKQRVG 150
Cdd:COG4987 411 --IAVVPQR-PHLFDTTLRENLRL-----ARPDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGD 224
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGT 552
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-223 |
2.55e-43 |
|
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: 149.56 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03252 1 ITFEHVR--FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMQIAGVPKAEIKTRVA---ELI--------DLVGLKGrenaypSRLSGGQKQRVG 150
Cdd:cd03252 77 -QVGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAgahDFIselpegydTIVGEQG------AGLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-239 |
4.32e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 156.02 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKS-TLIRLLNGLEKP----TSGSVTVAGKEISAARGESLR 78
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 79 QAR-LKISMVFQH----FNLLwsRTVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGL---KGRENAYPSRLSGGQKQRV 149
Cdd:PRK15134 88 GVRgNKIAMIFQEpmvsLNPL--HTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250
....*....|
gi 495163008 230 THPQQPITRQ 239
Cdd:PRK15134 246 SAPTHPYTQK 255
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-233 |
5.20e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 149.95 E-value: 5.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGS---VTVAGKEISAargESLRQARLKISMVFQH-FNLLW 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA---KTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 SRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQT 175
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 176 TDQILDLLQDINRRFGLTIVLITHEMHVVrKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-276 |
5.64e-43 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 151.80 E-value: 5.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEI-SAARGESLRQARLKISMVFQHFNLLWSRTVSE 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 102 NIAFSMQIAGVPKAEIktRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILD 181
Cdd:TIGR02142 95 NLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 182 LLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQpitrqfvrqisqegaddafdPTLAGEL 261
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL--------------------PWLARED 232
|
250
....*....|....*
gi 495163008 262 NGAVIKLTFVGHSTH 276
Cdd:TIGR02142 233 QGSLIEGVVAEHDQH 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
6.44e-43 |
|
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: 147.40 E-value: 6.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 7 ISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargeslRQARLKISM 86
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 87 VFQHFNL-LWSRTVSENIAFSMQIAGVPKAEIKTrVAELIDLVGLKGRenaYPSRLSGGQKQRVGIARALANRPDVLLCD 165
Cdd:cd03226 76 VMQDVDYqLFTDSVREELLLGLKELDAGNEQAET-VLKDLDLYALKER---HPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 166 EATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
7.95e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.52 E-value: 7.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL-----EKPTSGSVTVAGKEISAARGES 76
Cdd:PRK14247 4 IEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LRQarlKISMVFQHFNLLWSRTVSENIAFSMQIAGV--PKAEIKTRVAELIDLVGL----KGRENAYPSRLSGGQKQRVG 150
Cdd:PRK14247 80 LRR---RVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 495163008 231 HPQQPITRQFV 241
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-222 |
1.52e-42 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 147.23 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 7 ISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLK-IS 85
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 86 MVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCD 165
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 166 EATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEE 222
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-223 |
1.66e-42 |
|
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: 147.38 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTItavDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAr 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVL---KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHfNLLWSRTVSENIAFSM-------QIAGVPKAEIKTRVAELID----LVGLKGrenaypSRLSGGQKQRVG 150
Cdd:cd03253 77 --IGVVPQD-TVLFNDTIGYNIRYGRpdatdeeVIEAAKAAQIHDKIMRFPDgydtIVGERG------LKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-219 |
2.28e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.52 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGkdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGsvtvagkEISAARGeSLRQAR 81
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTA-PLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMqiagvpKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-220 |
4.39e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 154.50 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLK 83
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 -ISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVL 162
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 163 LCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKiCDRVAVMENGRVV 220
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
4.62e-42 |
|
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: 146.15 E-value: 4.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFH-QGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaaRGESLRQA 80
Cdd:cd03249 1 IEFKNVS--FRyPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHfNLLWSRTVSENIAF-------SMQIAGVPKAEIKTRVAELID----LVGLKGrenaypSRLSGGQKQRV 149
Cdd:cd03249 76 RSQIGLVSQE-PVLFDGTIAENIRYgkpdatdEEVEEAAKKANIHDFIMSLPDgydtLVGERG------SQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQdiNRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGD 224
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
6.03e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 147.06 E-value: 6.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeISAARGESLRQA 80
Cdd:PRK13644 1 MIRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLW-SRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITH---EMHVVrkicDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHnleELHDA----DRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-244 |
3.18e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.02 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargesL--- 77
Cdd:COG1137 3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----Lpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:COG1137 74 KRARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDI-NRRFGltiVLITHemHVVR---KICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLITD--HNVRetlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
250
....*....|.
gi 495163008 234 qpitrqfVRQI 244
Cdd:COG1137 229 -------VRKV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
3.80e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 144.21 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL-----EKPTSGSVTVAGKEISAARGESLRqARLKISMVFQHFNLLW 95
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 SRTVSENIAFSMQIAGV--PKAEIKTRV------AELIDLVglKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVewalkkAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 168 TSALDPQTTDQILDLLQDINRRFglTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-241 |
4.37e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 151.55 E-value: 4.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 8 SKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLKISMV 87
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 88 FQ--HFNLLWSRTVSENIAFSMQIAGVPKAE-IKTRVAELIDLVGLKgRENA--YPSRLSGGQKQRVGIARALANRPDVL 162
Cdd:PRK10261 407 FQdpYASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLL-PEHAwrYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 163 LCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
9.75e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 144.99 E-value: 9.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLR--NISKLFHQGK-DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTV----AGKEISAARG 74
Cdd:PRK13631 20 IILRvkNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 75 ---------ESLRQARLKISMVFQHFNL-LWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKgreNAY----PSR 140
Cdd:PRK13631 100 itnpyskkiKNFKELRRRVSMVFQFPEYqLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD---DSYlersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 141 LSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDiNRRFGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 495163008 221 EEGDVLQVFTHP 232
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.13e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 143.35 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQA 80
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-245 |
3.34e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 142.21 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSM-QIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVlQVFTHPQQPITRQ 239
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA-QALQANPDPRVRQ 241
|
....*.
gi 495163008 240 FVRQIS 245
Cdd:PRK11831 242 FLDGIA 247
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
3.58e-40 |
|
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: 140.31 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQa 80
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 rlkISMVFqHFNLLWSR-TVSENIAFSMQIAGVPKAEIktRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:COG4133 77 ---LAYLG-HADGLKPElTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
8.12e-40 |
|
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: 140.06 E-value: 8.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaaRGESLRQAR 81
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHfNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVglKGRENAYP-------SRLSGGQKQRVGIARA 154
Cdd:cd03251 76 RQIGLVSQD-VFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFI--MELPEGYDtvigergVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDI--NRrfglTIVLITHEMHVVRKIcDRVAVMENGRVVEEGD 224
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLmkNR----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
1.28e-39 |
|
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: 139.60 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgESLRQAR 81
Cdd:cd03218 1 LRAENLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRR-FGltiVLIT-HEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-233 |
1.37e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 143.25 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTITavDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKeisaaRGESLRQAR 81
Cdd:PRK11000 4 VTLRNVTKAY--GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRV---AELIDLVGLKGREnayPSRLSGGQKQRVGIARALANR 158
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 159 PDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-223 |
2.71e-39 |
|
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: 138.43 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKD-TITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGK-----EISAARGESL 77
Cdd:cd03220 20 LKKLGILGRKGEVgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 rqarlkismvfqhfnllwsrTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:cd03220 100 --------------------TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-241 |
3.20e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 139.40 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 16 DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL-----EKPTSGSVTVAGKEISAARgESLRQARLKISMVFQH 90
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERR-VNLNRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 FNLlWSRTVSENIAFSMQIAG-VPKAEIKTRV------AELIDLVGLKGRENAYpsRLSGGQKQRVGIARALANRPDVLL 163
Cdd:PRK14258 97 PNL-FPMSVYDNVAYGVKIVGwRPKLEIDDIVesalkdADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 164 CDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMEN-----GRVVEEGDVLQVFTHPQQPITR 238
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
...
gi 495163008 239 QFV 241
Cdd:PRK14258 254 EYV 256
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
3.73e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 139.45 E-value: 3.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGK-DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGEslRQ 79
Cdd:COG1101 1 MLELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY--KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLkISMVFQH------FNLlwsrTVSENIAFSMQ-------IAGVPKAEI---KTRVAELiDLvGLKGRENAYPSRLSG 143
Cdd:COG1101 79 AKY-IGRVFQDpmmgtaPSM----TIEENLALAYRrgkrrglRRGLTKKRRelfRELLATL-GL-GLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 144 GQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
4.80e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 138.68 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqA 80
Cdd:COG4604 1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RlKISMVFQ--HFNllwSR-TVSENIAF-----SmqiAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIA 152
Cdd:COG4604 75 K-RLAILRQenHIN---SRlTVRELVAFgrfpyS---KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 153 RALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-241 |
5.20e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 138.68 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKP----TSGSVTVAGKEISAArgeSLRQarLKISMVFQH----FN 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC---ALRG--RKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 93 LLwsRTVSENIAFSMQIAGVPKAEikTRVAELIDLVGLKGRE---NAYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:PRK10418 94 PL--HTMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 170 ALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
5.49e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 138.76 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL-----EKPTSGSVTVAGKEISAARGESLrQARLKISMVFQHFNLl 94
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-DLRKEIGMVFQQPNP- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSMQIAGVPKAEIKTRVAELiDLVG------LKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEAT 168
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 169 SALDPQTTDQILDLLQDINRRFglTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFV 241
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
5.59e-39 |
|
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: 137.95 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLF---HQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTV--AGKEISAARGE 75
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 -----SLRqaRLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGR-ENAYPSRLSGGQKQRV 149
Cdd:COG4778 84 preilALR--RRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-240 |
5.62e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 138.75 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RlkiSMVFQHFNLLWSRTVSENIAF---SMQIAGVPKAEIKTRVAELIDLVGLKGRenAYPSrLSGGQKQRVGIARALA- 156
Cdd:PRK13548 78 R---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGR--DYPQ-LSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 157 -----NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTh 231
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT- 230
|
....*....
gi 495163008 232 pQQPITRQF 240
Cdd:PRK13548 231 -PETLRRVY 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
1.20e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 137.94 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISklFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqA 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVfQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKG-RENAYPSrLSGGQKQRVGIARALA--- 156
Cdd:COG4559 75 RRRAVLP-QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 157 ----NRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-250 |
1.91e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 138.22 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDT---ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAA--RGES 76
Cdd:PRK13645 7 IILDNVSYTY--AKKTpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LRQARLKISMVFQHFNL-LWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKgRENA--YPSRLSGGQKQRVGIAR 153
Cdd:PRK13645 85 VKRLRKEIGLVFQFPEYqLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP-EDYVkrSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
250 260
....*....|....*....|....*
gi 495163008 234 --------QPITRQFVRQISQEGAD 250
Cdd:PRK13645 244 lltkieidPPKLYQLMYKLKNKGID 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-239 |
2.44e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 142.92 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKST----LIRLLNglekpTSGSVTVAGKEISAARGESLRQARLKISMVFQHFN-L 93
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 LWSR-TVSENIAFSMQI--AGVPKAEIKTRVAELIDLVGLK-GRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:PRK15134 375 LNPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 170 ALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQ 239
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-250 |
2.62e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 137.53 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 12 HQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQARLKISMVFQH- 90
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAEL---IDLVGLKGREnayPSRLSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEAllaVNMLDFKTRE---PARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 168 TSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHPQQ--------PITRQ 239
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveigldvPFSSN 246
|
250
....*....|.
gi 495163008 240 FVRQISQEGAD 250
Cdd:PRK13642 247 LMKDLRKNGFD 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-229 |
4.32e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 137.17 E-value: 4.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEI-SAARGESLRQARLKISMVFQH-FNLLWSR 97
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKPVRKKVGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFSMQIAGVPKAEIKTRVAELIDLVGL-KGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163008 177 DQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
5.86e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.43 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargeSLRQAR 81
Cdd:PRK13536 42 IDLAGVSKSY-GDK---AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
6.27e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 135.89 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqARLKISMVFQHFNLLWSRTV 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SEN--IAFSMQ-----IAGVPK--------AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLC 164
Cdd:PRK11300 98 IENllVAQHQQlktglFSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 165 DEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
1.01e-37 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 134.66 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTItavDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVL---KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVglKGRENAYP-------SRLSGGQKQRVGIARA 154
Cdd:cd03254 78 -MIGVVLQD-TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFI--MKLPNGYDtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
1.18e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 135.29 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEK--PT---SGSVTVAGKEISAARGESLrQARLKISMVFQHFNLl 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPV-EVRRRIGMVFQKPNP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSMQIAGVPK-----AEIKTRVAELIDLVGLKGRENAypSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:PRK14243 103 FPKSIYDNIAYGARINGYKGdmdelVERSLRQAALWDEVKDKLKQSG--LSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 170 ALDPQTTDQILDLLQDINRRFglTIVLITHEMHVVRKICDRVAVM---------ENGRVVEEGDVLQVFTHPQQPITRQF 240
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDY 258
|
.
gi 495163008 241 V 241
Cdd:PRK14243 259 V 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
1.85e-37 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 140.32 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQ-GKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTV-AGKEI--SAARGES 76
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWvdMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LR-QARLKISMVFQHFNLLWSRTVSENIAFSMQIAgVPKAEIKTRVAELIDLVGL---KGRE--NAYPSRLSGGQKQRVG 150
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFdeeKAEEilDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGD 224
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-249 |
2.08e-37 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 141.53 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKS-TLIRLLNGLEKpTSGSVT-------------VAG 66
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQcdkmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 67 KEISAARGESLRQArlKISMVFQH----FNLLWsrTVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGLKGRE---NAYP 138
Cdd:PRK10261 91 SEQSAAQMRHVRGA--DMAMIFQEpmtsLNPVF--TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 139 SRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270
....*....|....*....|....*....|.
gi 495163008 219 VVEEGDVLQVFTHPQQPITRQFVRQISQEGA 249
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-241 |
3.30e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 6 NISKLFHQGKDTiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL------EKPTSGSVTVAGKEISAARGESLRQ 79
Cdd:PRK14246 12 NISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 arlKISMVFQHFNLLWSRTVSENIAFSMQIAGVP-KAEIKTRVAELIDLVGL----KGRENAYPSRLSGGQKQRVGIARA 154
Cdd:PRK14246 91 ---EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQ 234
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*..
gi 495163008 235 PITRQFV 241
Cdd:PRK14246 246 ELTEKYV 252
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
4.52e-37 |
|
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: 132.71 E-value: 4.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMQIAgvPKAEIkTRVAELIDL--------------VGLKGREnaypsrLSGGQKQ 147
Cdd:cd03245 79 -NIGYVPQD-VTLFYGTLRDNITLGAPLA--DDERI-LRAAELAGVtdfvnkhpngldlqIGERGRG------LSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 148 RVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVrKICDRVAVMENGRVVEEG 223
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-233 |
5.75e-37 |
|
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: 139.96 E-value: 5.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQH---FNllwsRT 98
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---IGIVPQDtvlFN----DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMqiAGVPKAEIKT--RVAELIDLV--------------GLKgrenaypsrLSGGQKQRVGIARALANRPDVL 162
Cdd:COG5265 448 IAYNIAYGR--PDASEEEVEAaaRAAQIHDFIeslpdgydtrvgerGLK---------LSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 163 LCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGdvlqvfTHPQ 233
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG------THAE 578
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-228 |
5.79e-37 |
|
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: 139.17 E-value: 5.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLE--KPTSGSV----------------T 63
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 64 VAGKEISAArGESL---------------RQARLKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDL 127
Cdd:TIGR03269 77 KVGEPCPVC-GGTLepeevdfwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 128 VGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKI 207
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|.
gi 495163008 208 CDRVAVMENGRVVEEGDVLQV 228
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEV 256
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
7.36e-37 |
|
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: 130.41 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLLwSRTVSENIafsmqiagvpkaeiktrvaelidlvglkgrenaypsrLSGGQKQRVGIARALANRPDV 161
Cdd:cd03246 77 -HVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRkICDRVAVMENGRV 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-263 |
8.06e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 134.87 E-value: 8.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKL---FHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL----EKPTSGSVTVAGKEISAARGES 76
Cdd:PRK11022 3 LLNVDKLsvhFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LRQ-ARLKISMVFQH--FNLLWSRTVSENIAFSMQI-AGVPKAEIKTRVAELIDLVGL---KGRENAYPSRLSGGQKQRV 149
Cdd:PRK11022 83 RRNlVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270
....*....|....*....|....*....|....
gi 495163008 230 THPQQPITRQFVRQISQEGADDAFDPTLAGELNG 263
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPG 276
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-224 |
1.14e-36 |
|
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: 131.88 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 6 NISKLfHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeSLRQARLKIS 85
Cdd:TIGR03410 2 EVSNL-NVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP--PHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 86 MVFQH---FNLLwsrTVSENIAFSMQIAGVPKAEIKTRVAELI----DLVGLKGrenaypSRLSGGQKQRVGIARALANR 158
Cdd:TIGR03410 79 YVPQGreiFPRL---TVEENLLTGLAALPRRSRKIPDEIYELFpvlkEMLGRRG------GDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 159 PDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGD 224
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-223 |
2.16e-36 |
|
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: 138.94 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaarGESLRQAR 81
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA---GLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLwSRTVSENIAFSMQIAgvpkaeiKTRVAELIDLVGLKGRENAYP-----------SRLSGGQKQRVG 150
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQdinrRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-232 |
3.85e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.82 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGkdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS----AARGes 76
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelepADRD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 lrqarlkISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:PRK11650 78 -------IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
7.52e-36 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 135.68 E-value: 7.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaaRGESLRQA 80
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAF----SMQIAGVPK---AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
8.41e-36 |
|
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: 130.20 E-value: 8.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISkLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSG-SVTVAGKEIsaaRGESLRQ 79
Cdd:COG1119 3 LLELRNVT-VRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR---GGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLKISMV--FQHFNLLWSRTVSENI--AF--SMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR 153
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLDVVlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-232 |
1.18e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 136.78 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHfNLLWSRTVSEN 102
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR---QVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQIAgvPKAEIKT--RVAELIDLVGlkGRENAYP-------SRLSGGQKQRVGIARALANRPDVLLCDEATSALDP 173
Cdd:TIGR00958 575 IAYGLTDT--PDEEIMAaaKAANAHDFIM--EFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 174 qttdQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-223 |
1.25e-35 |
|
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: 136.00 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaaRGESLRQAR 81
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFnLLWSRTVSENIAFSmQIAGVPKAEIKT--RVAELIDLV-----GLKGRENAYPSRLSGGQKQRVGIARA 154
Cdd:TIGR02203 406 RQVALVSQDV-VLFNDTIANNIAYG-RTEQADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-244 |
4.43e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 130.41 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVL--RNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKP----TSGSVTVAGKEISAARG 74
Cdd:COG4170 1 MPLLdiRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 75 ESLRQ-ARLKISMVFQHFN--LLWSRTVSENIAFSMqiagvPKAEI-----------KTRVAELIDLVGLKGRE---NAY 137
Cdd:COG4170 81 RERRKiIGREIAMIFQEPSscLDPSAKIGDQLIEAI-----PSWTFkgkwwqrfkwrKKRAIELLHRVGIKDHKdimNSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 138 PSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250 260
....*....|....*....|....*..
gi 495163008 218 RVVEEGDVLQVFTHPQQPITRQFVRQI 244
Cdd:COG4170 236 QTVESGPTEQILKSPHHPYTKALLRSM 262
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
5.23e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.39 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITavddvnLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeslrQA 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFD------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGD 224
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-219 |
1.24e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 134.10 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargeSLRQARLKISMVFQHFNLLWSRT 98
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----GDIATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMH-VVRkiCDRVAVMENGRV 219
Cdd:NF033858 436 FWRLLIELSREDGVTIFISTHFMNeAER--CDRISLMHAGRV 475
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-238 |
2.47e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 126.67 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL---EKPTSGSVTVAGKEISAA--RGE 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 SLRQARLKISMVFQHFNLLWSRTVSENIAFSmQIAGVP---------KAEIKTRVAELIDLVGLKGRENAYPSRLSGGQK 146
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 147 QRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVL 226
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
250
....*....|....*.
gi 495163008 227 QV----FTHPQQPITR 238
Cdd:PRK09984 239 QFdnerFDHLYRSINR 254
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
6.00e-34 |
|
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: 123.31 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIsaaRGESLRQA-RLKISMV---FQHFNLLW 95
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV---TRRSPRDAiRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 SRTVSENIAFsmqiagvpkaeiktrvaelidlvglkgrenayPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQT 175
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495163008 176 TDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-241 |
7.74e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 125.29 E-value: 7.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 5 RNISK-------LFHqgKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArGESL 77
Cdd:PRK15112 8 RNLSKtfryrtgWFR--RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG-DYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARlkISMVFQH-FNLLWSRT-VSENIAFSMQI-AGVPKAEIKTRVAELIDLVGLK-GRENAYPSRLSGGQKQRVGIAR 153
Cdd:PRK15112 85 RSQR--IRMIFQDpSTSLNPRQrISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
....*...
gi 495163008 234 QPITRQFV 241
Cdd:PRK15112 243 HELTKRLI 250
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-223 |
2.57e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.70 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQHfNLLWSRTV 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN---IAVVFQD-AGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAFSMQIAGVPKAEIKTRVAELIDLVglKGRENAYP-------SRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK13657 426 EDNIRVGRPDATDEEMRAAAERAQAHDFI--ERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163008 173 PQTTDQILDLLQDInrRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:PRK13657 504 VETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-250 |
3.19e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 124.05 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSG-----SVTVAGKEISAARgeSLRQARLKISMVFQHFNL 93
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR--DVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 LWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGL----KGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 170 ALDPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQPITRQFVRQISQEGA 249
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVK 270
|
.
gi 495163008 250 D 250
Cdd:PRK14271 271 D 271
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.52e-32 |
|
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: 126.63 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqgKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHfNLLWSRTVSENIAFSMqiAGVPKAEIKtrvaELIDLVGLKGRENAYP-----------SRLSGGQKQRVG 150
Cdd:TIGR02857 397 -QIAWVPQH-PFLFAGTIAENIRLAR--PDASDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVM 214
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-219 |
2.28e-32 |
|
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: 120.27 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHfNLLWSRTVSEN 102
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS---KVSLVGQE-PVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQ-------IAGVPKAEIKTRVAELID----LVGLKGrenaypSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:cd03248 108 IAYGLQscsfecvKEAAQKAHAHSFISELASgydtEVGEKG------SQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163008 172 DPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKiCDRVAVMENGRV 219
Cdd:cd03248 182 DAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
5.70e-32 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 117.80 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArGESLRQAr 81
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHFNLlWSRTVSENIafsmqiagvpkaeiktrvaelidlvglkGRenaypsRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03247 77 --ISVLNQRPYL-FDTTLRNNL----------------------------GR------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKIcDRVAVMENGRVVEEG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-235 |
7.20e-32 |
|
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: 125.25 E-value: 7.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQHFNLLwSRTVS 100
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH---IGYLPQDVELF-DGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAFSMQI--AGVPKAEIKTRVAELID--------LVGLKGrenaypSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:COG4618 424 ENIARFGDAdpEKVVAAAKLAGVHEMILrlpdgydtRIGEGG------ARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 171 LDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRkICDRVAVMENGRVVEEG---DVLQVFTHPQQP 235
Cdd:COG4618 498 LDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGprdEVLARLARPAAA 563
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-246 |
8.42e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 119.65 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 5 RNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS----AARGESLRQ- 79
Cdd:PRK11701 10 RGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlYALSEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 -ARLKISMVFQHFNLLWSRTVSE--NIAFSMQIAGVPK-AEIKTRVAELIDLVGL-KGRENAYPSRLSGGQKQRVGIARA 154
Cdd:PRK11701 86 lLRTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQ 234
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
250
....*....|..
gi 495163008 235 PITRQFVRQISQ 246
Cdd:PRK11701 246 PYTQLLVSSVLQ 257
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-225 |
2.94e-31 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 117.50 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGkdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeslRQAR 81
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKtrvaELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-226 |
3.14e-31 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 124.74 E-value: 3.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFH-QGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargeSLRQA 80
Cdd:TIGR01257 929 VCVKNLVKIFEpSGR---PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPD 160
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 161 VLLCDEATSALDPQTTDQILDLLqdINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVL 226
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-233 |
9.63e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.21 E-value: 9.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS-AARGESLRQARLKISMVFQHFNLLWSRTVSE 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 102 NIAFSMQiagvpkaeiKTRVAELIDLVGLKGRE---NAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK11144 96 NLRYGMA---------KSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 179 ILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-223 |
9.83e-31 |
|
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: 115.67 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHfNLLWSRTV 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS---RISIIPQD-PVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAF------SMQIAGVPKAEIKTRVAELIDlvGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDP 173
Cdd:cd03244 95 RSNLDPfgeysdEELWQALERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495163008 174 QTTDQILDLLQdiNRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:cd03244 173 ETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-244 |
1.70e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 117.98 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGlekptsgsVTVAGKEISAARGE-------- 75
Cdd:PRK15093 6 IRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTADRMRfddidllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 -SLRQARL----KISMVFQHFNLLWSRtvSENIAFSMqIAGVPKAEIK-----------TRVAELIDLVGLKGRENA--- 136
Cdd:PRK15093 78 lSPRERRKlvghNVSMIFQEPQSCLDP--SERVGRQL-MQNIPGWTYKgrwwqrfgwrkRRAIELLHRVGIKDHKDAmrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 137 YPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMEN 216
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250 260
....*....|....*....|....*...
gi 495163008 217 GRVVEEGDVLQVFTHPQQPITRQFVRQI 244
Cdd:PRK15093 235 GQTVETAPSKELVTTPHHPYTQALIRAI 262
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-229 |
1.74e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 116.65 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgESLRQARLKISMVFQHFNL-LWSRTVSEN 102
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQDPEQqIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL 182
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495163008 183 LQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVF 229
Cdd:PRK13638 179 IRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-223 |
1.75e-30 |
|
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: 115.45 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL---EKPTSGSVTVAGKEISAArgeslrQARLKISMVFQHFNLLWSRTV 99
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPD------QFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAFSMQIAG---VPKAEIKTRVA-ELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQT 175
Cdd:cd03234 99 RETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163008 176 TDQILDLLQDINRRFglTIVLITheMHVVR----KICDRVAVMENGRVVEEG 223
Cdd:cd03234 179 ALNLVSTLSQLARRN--RIVILT--IHQPRsdlfRLFDRILLLSSGEIVYSG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-222 |
4.65e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKDTITAV-------------DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGK 67
Cdd:COG1129 235 LMVGRELEDLFPKRAAAPGEVvleveglsvggvvRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 68 EISAArgeSLRQA-RLKISMV---FQHFNLLWSRTVSENIAFSMQ----IAG-VPKAEIKTRVAELIDLVGLK-GRENAY 137
Cdd:COG1129 315 PVRIR---SPRDAiRAGIAYVpedRKGEGLVLDLSIRENITLASLdrlsRGGlLDRRRERALAEEYIKRLRIKtPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 138 PSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREG 470
|
....*
gi 495163008 218 RVVEE 222
Cdd:COG1129 471 RIVGE 475
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-225 |
1.40e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.24 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTvagkeisaaRGESLRQA 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---------LGETVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 rlkismVF-QHFNLL-WSRTVSENIAfsmqiAGVPKAeiktRVAELIDLVG---LKGRE-NAYPSRLSGGQKQRVGIARA 154
Cdd:COG0488 382 ------YFdQHQEELdPDKTVLDELR-----DGAPGG----TEQEVRGYLGrflFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDinrrFGLTIVLITHEMHVVRKICDRVAVMENGRVVE-EGDV 225
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDRYFLDRVATRILEFEDGGVREyPGGY 514
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
6.17e-29 |
|
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: 110.64 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITAV-DDVNLEVERGQIYGIIGYSGAGKSTLIR-LLNGLEKpTSGSVTVAGKeisaargeslrq 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 arlkISMVFQhFNLLWSRTVSENIAFSMQIagvpkaeIKTRVAELI-------DL----------VGLKGrenaypSRLS 142
Cdd:cd03250 68 ----IAYVSQ-EPWIQNGTIRENILFGKPF-------DEERYEKVIkacalepDLeilpdgdlteIGEKG------INLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 143 GGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILD-LLQDiNRRFGLTIVLITHEMHVVRKiCDRVAVMENGR 218
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILG-LLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-245 |
6.18e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 116.55 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS-AARGESLRQArl 82
Cdd:PRK11288 7 FDGIGKTFPGVK----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 83 kISMVFQHFNLLWSRTVSENI---AFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK11288 81 -VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQqpITRQ 239
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQ--LVQA 236
|
....*..
gi 495163008 240 FV-RQIS 245
Cdd:PRK11288 237 MVgREIG 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.14e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.08 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAr 81
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHFNLLwSRTVSENiafsMQIAGvPKA------EIKTRVaELIDLV----GLK------GREnaypsrLSGGQ 145
Cdd:PRK11160 416 --ISVVSQRVHLF-SATLRDN----LLLAA-PNAsdealiEVLQQV-GLEKLLeddkGLNawlgegGRQ------LSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 146 KQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKIcDRVAVMENGRVVEEGD 224
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-223 |
1.23e-28 |
|
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: 109.56 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFH--QGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL--EKPTSGSVTVAGKEISaargesL 77
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARLKISMVFQHFNLLWSRTVSENIAFSmqiagvpkAEIKtrvaelidlvglkgrenaypsRLSGGQKQRVGIARALAN 157
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFA--------AKLR---------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITH----EMHvvrKICDRVAVMENGRVVEEG 223
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHqpssEIF---ELFDKLLLLSQGRVIYFG 194
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
3.86e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.58 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKlfHQGKdtITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaaRGESLRQA 80
Cdd:PRK11614 5 MLSFDKVSA--HYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFSMQIAgvPKAEIKTRVAELIDLVG-LKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEE--GDVL 226
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEdtGDAL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
7.26e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeisaargeslrqaRLK 83
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENI---------------AFSMQIAGVPKA-----------------EIKTRVAELIDLVGLK 131
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEDlerlaelqeefealggwEAEARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 132 GRE-NAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTdqilDLLQDINRRFGLTIVLITHEMHVVRKICDR 210
Cdd:COG0488 143 EEDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI----EWLEEFLKNYPGTVLVVSHDRYFLDRVATR 218
|
....*....
gi 495163008 211 VAVMENGRV 219
Cdd:COG0488 219 ILELDRGKL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-232 |
9.33e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.86 E-value: 9.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 18 ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLKISMVFQHFNLLWSR 97
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL---SARAASRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFSM-----QIAGVPKAEiKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK09536 93 DVRQVVEMGRtphrsRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 173 PQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK09536 172 INHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-230 |
3.04e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 14 GKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLKISMVFQH--- 90
Cdd:PRK11231 13 GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML---SSRQLARRLALLPQHhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 ----------------FNLLWSRTVSENIAFsmqiagVPKAEIKTRVAELID-LVglkgrenaypSRLSGGQKQRVGIAR 153
Cdd:PRK11231 88 pegitvrelvaygrspWLSLWGRLSAEDNAR------VNQAMEQTRINHLADrRL----------TDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-224 |
4.73e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRnISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQA- 80
Cdd:COG3845 256 VVLE-VENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 -------RLKISMV--FqhfnllwsrTVSENIAFSMQIAG-------VPKAEIKTRVAELIDLVGLKGRENAYPSR-LSG 143
Cdd:COG3845 335 vayipedRLGRGLVpdM---------SVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 144 GQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEV 484
|
.
gi 495163008 224 D 224
Cdd:COG3845 485 P 485
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-223 |
1.39e-26 |
|
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: 110.60 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQHfNLLWSRTV 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAF--------SMQIAGVPKAEIKTRVAELidLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:TIGR01193 565 LENLLLgakenvsqDEIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163008 172 DPQTTDQILDLLQDINRRfglTIVLITHEMHVVRKIcDRVAVMENGRVVEEG 223
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-223 |
1.41e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.11 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISkLFHQGKDTiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:PRK11176 342 IEFRNVT-FTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLlWSRTVSENIAFSMQiAGVPKAEIKT--RVAELIDLV-----GLK---GrENAypSRLSGGQKQRVGI 151
Cdd:PRK11176 418 -QVALVSQNVHL-FNDTIANNIAYART-EQYSREQIEEaaRMAYAMDFInkmdnGLDtviG-ENG--VLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 152 ARALANRPDVLLCDEATSALDPQTTDQI---LDLLQDiNRrfglTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIqaaLDELQK-NR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-218 |
2.27e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.25 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLeKPT---SGSVTVAGKEISAArgeSLRQA 80
Cdd:PRK13549 8 MKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQAS---NIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 -RLKISMVFQHFNLLWSRTVSENIAFSMQI--AGVPK-AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:PRK13549 80 eRAGIAIIHQELALVKELSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
3.83e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKdtiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLeKPTSGSVTVAGKEISAArgeSLRQAR 81
Cdd:PRK11174 350 IEAEDLEILSPDGK---TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHFNLLWSrTVSENIAF---SMQIAGVPKAEIKTRVAELIDLV--GLKG--RENAypSRLSGGQKQRVGIARA 154
Cdd:PRK11174 423 KHLSWVGQNPQLPHG-TLRDNVLLgnpDASDEQLQQALENAWVSEFLPLLpqGLDTpiGDQA--AGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 155 LANRPDVLLCDEATSALDPQTTDQILDLLQDINRrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGD 224
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGD 566
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.07e-25 |
|
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: 107.22 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL--EKPTSGSVTVAGKEISAargESLR 78
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKA---SNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 79 QARLK-ISMVFQHFNLLWSRTVSENIAFSMQI----AGVPKAEIKTRVAELIDLVGLKGRENAYP-SRLSGGQKQRVGIA 152
Cdd:TIGR02633 74 DTERAgIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 153 RALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-228 |
4.05e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.17 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqARlKISMVFQHFNLLWSRTVSENIAfsmqIA 110
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--AR-KVAYLPQQLPAAEGMTVRELVA----IG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 111 GVP--------KAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL 182
Cdd:PRK10575 110 RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495163008 183 LQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQV 228
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
1.51e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.98 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFhQGKDTITAVDdvnLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKeiSAARGESLRQA 80
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQHFNLLWSRTVSENIAFsmqiaGVPK-AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENILF-----GLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 160 DVLLCDEATSALDPQTTD----QILDLLQDinrrfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG 223
Cdd:PRK15439 160 RILILDEPTASLTPAETErlfsRIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
2.28e-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: 103.59 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQ--HfnlLWSR 97
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQdaH---LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFSMqiAGVPKAEIKT--RVAELIDLV-----GLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:TIGR02868 424 TVRENLRLAR--PDATDEELWAalERVGLADWLralpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*....
gi 495163008 171 LDPQTTDQILDLLQDINRrfGLTIVLITH 199
Cdd:TIGR02868 502 LDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-222 |
2.50e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISA-ARGESLRQARLKISMVFQHFNLLWSRTV 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrSPQDGLANGIVYISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIA------FSMQIAGVPKAEIKTRVAELIDLVGLKGrenayPSR------LSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 168 TSALDPQTTDQILDLlqdINrRF---GLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:PRK10762 423 TRGVDVGAKKEIYQL---IN-QFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-223 |
6.46e-24 |
|
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: 97.10 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHFNLLwSRTV 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS---SLTIIPQDPTLF-SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENI-AFSMQiagvPKAEIKT--RVAElidlvglkGRENaypsrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:cd03369 99 RSNLdPFDEY----SDEEIYGalRVSE--------GGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163008 177 DQILDLlqdINRRF-GLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:cd03369 162 ALIQKT---IREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
9.76e-24 |
|
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: 94.82 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHqGKDTItavDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAgkeisaargeslrqAR 81
Cdd:cd03221 1 IELENLSKTYG-GKLLL---KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--------------ST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKIsmvfqhfnllwsrtvseniafsmqiagvpkaeiktrvaelidlvglkgrenAYPSRLSGGQKQRVGIARALANRPDV 161
Cdd:cd03221 63 VKI---------------------------------------------------GYFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 162 LLCDEATSALDPQTTDQILDLLQDINRrfglTIVLITHEMHVVRKICDRVAVMENGR 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-199 |
1.42e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 96.57 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEK--PTSGSVTVAGKEISaaRGESLrqarlkismvfqhfnllws 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG--REASL------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 rtvseniafsmqIAGVPKAEIKTRVAELIDLVGLKgreNAY-----PSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:COG2401 103 ------------IDAIGRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*...
gi 495163008 172 DPQTTDQILDLLQDINRRFGLTIVLITH 199
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-200 |
2.37e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 16 DTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHfNLLW 95
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQT-PTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 SRTVSENIAFSMQIAGV---PKAEIKTRVAELIDLVGLKGRENAypsrLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK10247 94 GDTVYDNLIFPWQIRNQqpdPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180
....*....|....*....|....*...
gi 495163008 173 PQTTDQILDLLQDINRRFGLTIVLITHE 200
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-225 |
3.81e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 99.86 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLeKPT---SGSVTVAGKEisaARGESLRQA 80
Cdd:NF040905 4 MRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEV---CRFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 -RLKISMVFQHFNLLWSRTVSENIAFSMQIA--GVPK-AEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALA 156
Cdd:NF040905 76 eALGIVIIHQELALIPYLSIAENIFLGNERAkrGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 157 NRPDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDC 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-230 |
1.24e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 95.33 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLrqarlkISMVFQHFNLLWSRT 98
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 V-SENIAF-----SMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PRK15056 95 VlVEDVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 173 PQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDrVAVMENGRVVEEGDVLQVFT 230
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-207 |
1.35e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.72 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRqarlkismvfqhfNLLW------ 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ-------------DLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 ---SRTVSENIAFSMQIAGVPKAEiktRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIAR-ALANRPDVLLcDEATSAL 171
Cdd:PRK13538 85 iktELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163008 172 DPQTTDQILDLLQDINRRFGLtIVLITH-EMHV----VRKI 207
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGM-VILTTHqDLPVasdkVRKL 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-233 |
1.86e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVtvagkeisaargesLRQA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RLKISMVFQ--HFNLLWSRTVSEniaFSMQIAGVPKAEI-----KTRVAELIDlvglkgrenAYPSRLSGGQKQRVGIAR 153
Cdd:PRK09544 66 KLRIGYVPQklYLDTTLPLTVNR---FLRLRPGTKKEDIlpalkRVQAGHLID---------APMQKLSGGETQRVLLAR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 154 ALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMeNGRVVEEGDVLQVFTHPQ 233
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
11-234 |
2.65e-22 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 94.50 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 11 FHQGKdTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeisaargeslrqarlKISMVFQH 90
Cdd:PRK13546 31 KHKNK-TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 171 LDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQQ 234
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-232 |
6.46e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.32 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 11 FHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRqARLKismVFQH 90
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR-SRLA---VVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 FNLLWSRTVSENIAFsmqiaGVPKA---EIKtRVAELI----DLVGL-KGRENAYPSR---LSGGQKQRVGIARALANRP 159
Cdd:PRK10789 397 TPFLFSDTVANNIAL-----GRPDAtqqEIE-HVARLAsvhdDILRLpQGYDTEVGERgvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLqdinRRFG--LTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHP 232
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNL----RQWGegRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-251 |
7.03e-22 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 96.50 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQARLKIsmvfqhfnllwsrtv 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 sENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQI 179
Cdd:PRK13545 104 -ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 180 LDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHpqqpiTRQFVRQISQEGADD 251
Cdd:PRK13545 183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKYNQMSVEE 248
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-199 |
1.21e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISkLFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTV-AGKEISAA------- 72
Cdd:COG4178 362 ALALEDLT-LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLpqrpylp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 73 RGeSLRQArlkismvfqhfnLLWSRTVSEniafsmqiagVPKAEIKT--RVAELIDLVGLKGRENAYPSRLSGGQKQRVG 150
Cdd:COG4178 439 LG-TLREA------------LLYPATAEA----------FSDAELREalEAVGLGHLAERLDEEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDinRRFGLTIVLITH 199
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-220 |
1.87e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 94.80 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEIS-AARGESLRQArl 82
Cdd:PRK10982 1 MSNISKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 83 kISMVFQHFNLLWSRTVSENI---AFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK10982 75 -ISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-217 |
2.02e-21 |
|
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: 95.47 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 20 AVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargeslrqarlKISMVFQHF-------- 91
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----------NISDVHQNMgycpqfda 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 92 --NLLWSRtvsENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATS 169
Cdd:TIGR01257 2023 idDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163008 170 ALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
2.70e-21 |
|
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: 89.89 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLE--KPTSGSVTVAGKEISAARGESlrQARLKISMVFQHfnllwsrt 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 vseniafSMQIAGVpkaeiktRVAELIDLVGLKgrenaypsrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:cd03217 86 -------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163008 179 ILDLLQDInRRFGLTIVLITHEMHVVRKI-CDRVAVMENGRVVEEGDV 225
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
3.18e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.27 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTItAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQar 81
Cdd:PRK10522 323 LELRNVT--FAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lKISMVFQHFNLlwsrtvseniaFSMQIAGVPKAEIKTRVAELIDLVGLKGR---ENAYPS--RLSGGQKQRVGIARALA 156
Cdd:PRK10522 398 -LFSAVFTDFHL-----------FDQLLGPEGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 157 NRPDVLLCDEATSALDPQTT----DQILDLLQDInrrfGLTIVLITHEMHVVRKiCDRVAVMENGRVVE 221
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRrefyQVLLPLLQEM----GKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-244 |
3.34e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaaRGESLRQARlKISMVFQHFNLLWSRT 98
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVAR-RIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMqiagVPKAEIKTR--------VAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:PRK10253 98 VQELVARGR----YPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 171 LDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGdvlqvftHPQQPITRQFVRQI 244
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERI 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-223 |
9.24e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.27 E-value: 9.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklfHQGKDTiTAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARgeSLRQAR 81
Cdd:NF033858 2 ARLEGVS---HRYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR--HRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQHF--NLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLKgrenAYPSR----LSGGQKQRVGIARAL 155
Cdd:NF033858 76 PRIAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA----PFADRpagkLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 156 ANRPDVLLCDEATSALDPQTTDQILDLLQDI-NRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATG 219
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
262-337 |
1.06e-20 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 84.48 E-value: 1.06e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 262 NGAVIKLTFVGHSTHQPVVGELTLRYGLPFNILHGKMTQTAHGVFGQLWLHVVATPEQLENILADLRLHEIHCEVI 337
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-227 |
1.77e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLI-----RLLNGLEKptSGSVTVAGKEISAargeslRQARLKISMVFQHFNLLWSR 97
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDA------KEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFS----MQiAGVPKAEIKTRVAELIDLVGLK-------GRENAYPSrLSGGQKQRVGIARALANRPDVLLCDE 166
Cdd:TIGR00955 115 TVREHLMFQahlrMP-RRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 167 ATSALDPQTTDQILDLLQDINRRfGLTIVLITHE--MHVVRkICDRVAVMENGRVVEEGDVLQ 227
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpsSELFE-LFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-225 |
2.86e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.22 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKdtitAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlK 83
Cdd:PRK10762 7 LKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENI----AFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRP 159
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDV 225
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREV 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-233 |
4.86e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESlrQARLKISMVFQHFNLLWSRT 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQI-AGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTD 177
Cdd:PRK10895 95 VYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 178 QILDLLQDInRRFGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-216 |
1.01e-19 |
|
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: 84.90 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVtvagkeisaargeslrqarlkismvfqhfnllwSRTVS 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------------------GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAFSMQIAGVPkaeiktrVAELIDLVglkgrenAYP--SRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQ 178
Cdd:cd03223 64 EDLLFLPQRPYLP-------LGTLREQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 495163008 179 ILDLLQDinrrFGLTIVLITHEmHVVRKICDRVAVMEN 216
Cdd:cd03223 130 LYQLLKE----LGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-199 |
1.79e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.10 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlkiSMVFQHFNLLWSR-TVSEN 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-----ILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQIAGVPKAEIKtrvaELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL 182
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*..
gi 495163008 183 LQDINRRFGLTIvLITH 199
Cdd:TIGR01189 170 LRAHLARGGIVL-LTTH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-212 |
1.95e-19 |
|
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: 89.22 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFhqGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVagkeisaarGESlrqar 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GET----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQ-HFNLLWSRTVSENIAFSMQIAGVPKAEIKTRvaelidlvglkgrenAYPSR--------------LSGGQK 146
Cdd:TIGR03719 385 VKLAYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSR---------------AYVGRfnfkgsdqqkkvgqLSGGER 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 147 QRVGIARALANRPDVLLCDEATSALDPQTtdqiLDLLQDINRRFGLTIVLITHEmhvvRKICDRVA 212
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHD----RWFLDRIA 507
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-222 |
2.53e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAAR-GESLRQA-------RLKISMVFQHfnllw 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGimlcpedRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 srTVSENIAFSMQIAGVPKAEIKTRVAElidlvglkgRENA----------YPSR------LSGGQKQRVGIARALANRP 159
Cdd:PRK11288 347 --SVADNINISARRHHLRAGCLINNRWE---------AENAdrfirslnikTPSReqlimnLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 160 DVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-230 |
4.94e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEkPTSGSVTVAGKEISAARGESLRQARlkiSMVFQHFNLLWSRTVSENI 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 104 AFSMQiAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARAL-----ANRPD--VLLCDEATSALD---P 173
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDvaqQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 174 QTTDQILdllqdinRRF---GLTIVLITHEM-HVVRKiCDRVAVMENGRVVEEGDVLQVFT 230
Cdd:COG4138 170 AALDRLL-------RELcqqGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-199 |
5.06e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAAR-GESL-----RQArLKISMvfqhfnllws 96
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEAChylghRNA-MKPAL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 rTVSENIAFSMQIAGVPKaeikTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARAL-ANRPdVLLCDEATSALDPQT 175
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....
gi 495163008 176 TDQILDLLQDINRRFGLtIVLITH 199
Cdd:PRK13539 163 VALFAELIRAHLAQGGI-VIAATH 185
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-233 |
2.51e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.93 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITavdDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAr 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQ---NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 lkISMVFQHFNLLwSRTVSENIAFSMQI--AGVPKAEIKTRVAELIDLV--GLKGRENAYPSRLSGGQKQRVGIARALAN 157
Cdd:PRK10790 417 --VAMVQQDPVVL-ADTFLANVTLGRDIseEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 158 RPDVLLCDEATSALDPQTTDQILDLLQDINRRfgLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGdvlqvfTHPQ 233
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG------THQQ 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-199 |
3.02e-18 |
|
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: 81.77 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGeSLRQARLKISmvfqHFNLLWSR-TVSEN 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG----HAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFSMQIAGvpkaeiKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL 182
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 495163008 183 LQDINRRFGLtIVLITH 199
Cdd:cd03231 168 MAGHCARGGM-VVLTTH 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-221 |
6.37e-18 |
|
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: 84.46 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlKISMVFQHFNLlwsrtvseni 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ---LFSAVFSDFHL---------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 104 aFSmQIAGVPKAEIKTRVAELIDLVGLKG----RENAYPSR-LSGGQKQRVGIARALA-NRPdVLLCDEATSALDPQ--- 174
Cdd:COG4615 418 -FD-RLLGLDGEADPARARELLERLELDHkvsvEDGRFSTTdLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEfrr 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163008 175 ---TTdqildLLQDINRRfGLTIVLITHE---MHVvrkiCDRVAVMENGRVVE 221
Cdd:COG4615 495 vfyTE-----LLPELKAR-GKTVIAISHDdryFDL----ADRVLKMDYGKLVE 537
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-217 |
6.61e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.22 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 18 ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLR-QARLKISMVFQHFNLLwS 96
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAFsmqiaGVPKAeiKTRVAELIDLVGLK--------GRENAYPSR---LSGGQKQRVGIARALANRPDVLLCD 165
Cdd:cd03290 93 ATVEENITF-----GSPFN--KQRYKAVTDACSLQpdidllpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 166 EATSALDPQTTDQ-----ILDLLQDINRrfglTIVLITHEMHVVRKiCDRVAVMENG 217
Cdd:cd03290 166 DPFSALDIHLSDHlmqegILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
265-336 |
3.35e-17 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 74.79 E-value: 3.35e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 265 VIKLTFVGHSTHQPVVGELTLRYGLPFNILHGKMTQTAHGVFGQLWLHVVATPEQLENILADLRLHEIHCEV 336
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-222 |
4.90e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAargESLRQaRLKISMVF-----QHFNLLWSR 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA---LSTAQ-RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENI--------AFSMQiagvPKAEiKTRVAELIDLVGLKGRENAYPSR-LSGGQKQRVGIARALANRPDVLLCDEAT 168
Cdd:PRK15439 357 PLAWNVcalthnrrGFWIK----PARE-NAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163008 169 SALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-212 |
6.42e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.32 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVagkeisaarGESlrqarLKISMVFQ-HFNLLWSRTV 99
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GET-----VKLAYVDQsRDALDPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAFSMQIAGVPKAEIKTRvaelidlvglkgrenAYPSR--------------LSGGQKQRVGIARALANRPDVLLCD 165
Cdd:PRK11819 406 WEEISGGLDIIKVGNREIPSR---------------AYVGRfnfkggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495163008 166 EATSALDPQTtdqiLDLLQDINRRFGLTIVLITHEmhvvRKICDRVA 212
Cdd:PRK11819 471 EPTNDLDVET----LRALEEALLEFPGCAVVISHD----RWFLDRIA 509
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-220 |
1.41e-16 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 76.92 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPT---SGSVTVAGKEISaargESLR 78
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK----EFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 79 QARLKISMVFQ---HFNLLwsrTVSENIAFSmqiagvpkaeiktrvaelidlvgLKGRENAYPSRLSGGQKQRVGIARAL 155
Cdd:cd03233 80 KYPGEIIYVSEedvHFPTL---TVRETLDFA-----------------------LRCKGNEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 156 ANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHV-VRKICDRVAVMENGRVV 220
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-229 |
1.51e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 15 KDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIR-LLNGLEKPTSGSVTVAGKEISAArgeslrqarlKISMVFqhfnl 93
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVP----------QVSWIF----- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 lwSRTVSENIAFSMQIAgvpkaeiKTRVAELIDLVGLKGRENAYPSR-----------LSGGQKQRVGIARALANRPDVL 162
Cdd:PLN03232 692 --NATVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 163 LCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKIcDRVAVMENGRVVEEGDVLQVF 229
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-224 |
1.05e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.28 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTvagkeisAARgeslrqarlKISMVFQHfnlLW--SRTVS 100
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AER---------SIAYVPQQ---AWimNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAF--SMQIAGVPKAeikTRVAEL-IDLVGLK-GRENAYPSR---LSGGQKQRVGIARAL-ANRpDVLLCDEATSALD 172
Cdd:PTZ00243 739 GNILFfdEEDAARLADA---VRVSQLeADLAQLGgGLETEIGEKgvnLSGGQKARVSLARAVyANR-DVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163008 173 PQTTDQIL-DLLqdINRRFGLTIVLITHEMHVVRKiCDRVAVMENGRVVEEGD 224
Cdd:PTZ00243 815 AHVGERVVeECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-230 |
1.37e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 12 HQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNG--LEKPTSGSVTVAGkEISA-----ARGESLRQARLKI 84
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTG-DVTLngeplAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 85 SMvfqhfnllwSRTVSENIAFSMQ----IAGVPKA-----------EIKTRVAELIDLVGLKGREnayPSRLSGGQKQRV 149
Cdd:PRK13547 87 VL---------PQAAQPAFAFSAReivlLGRYPHArragalthrdgEIAWQALALAGATALVGRD---VTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 150 GIARALAN---------RPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:PRK13547 155 QFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
250
....*....|
gi 495163008 221 EEGDVLQVFT 230
Cdd:PRK13547 235 AHGAPADVLT 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-222 |
2.02e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARG-ESLRQARLKISMVFQHFNLLWSRTV 99
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAFSMQI--AGV--------PKAEIKTRVAELiDLVGLKGRE-NAYPSRLSGGQKQRVGIARALANRPDVLLCDEAT 168
Cdd:PRK09700 359 AQNMAISRSLkdGGYkgamglfhEVDEQRTAENQR-ELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163008 169 SALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-223 |
3.24e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTS-GSVTVAGKEISAArgeslrqarlKISMVFqhfnllwSRTVSE 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVP----------QVSWIF-------NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 102 NIAFsmqiaGVPKAeiKTRVAELIDLVGLKGRENAYPSR-----------LSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:PLN03130 698 NILF-----GSPFD--PERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163008 171 LDPQTTDQILD-LLQDINRrfGLTIVLITHEMHVVRKIcDRVAVMENGRVVEEG 223
Cdd:PLN03130 771 LDAHVGRQVFDkCIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-205 |
3.74e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKL------FHQgkDTITAVD---DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVagKEISAARG 74
Cdd:PTZ00265 377 LKDIKKIqfknvrFHY--DTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 75 ESLRQARLKISMVFQHfNLLWSRTVSENIAFSM--------------------------------QIAGVPKAEIKTRVA 122
Cdd:PTZ00265 453 INLKWWRSKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDMSNTTDS 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 123 -ELI------------DLVGLKGRE------NAYP-----------SRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PTZ00265 532 nELIemrknyqtikdsEVVDVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
250 260 270
....*....|....*....|....*....|...
gi 495163008 173 PQTTDQILDLLQDINRRFGLTIVLITHEMHVVR 205
Cdd:PTZ00265 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-216 |
4.06e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 76 SLRQARLKISMVFQHfNLLWSRTVSENIAFSMQIA---GVPKAEIKTRVAELIDLVGLKGRENA--YPSRLSGGQKQRVG 150
Cdd:PTZ00265 1290 NLKDLRNLFSIVSQE-PMLFNMSIYENIKFGKEDAtreDVKRACKFAAIDEFIESLPNKYDTNVgpYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKiCDRVAVMEN 216
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-219 |
5.12e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.54 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLF----HQGKDTITAVD-----------DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVA 65
Cdd:PRK10982 229 MMVGRSLTQRFpdkeNKPGEVILEVRnltslrqpsirDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 66 GKEI-------SAARGESLRQARLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLK--GRENA 136
Cdd:PRK10982 309 GKKInnhnaneAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKtpGHRTQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 137 YPSrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMEN 216
Cdd:PRK10982 389 IGS-LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSN 466
|
...
gi 495163008 217 GRV 219
Cdd:PRK10982 467 GLV 469
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-230 |
8.87e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.39 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 18 ITAVDDVNLEVERGQIYGIIGYSGAG--KSTLIRLLNGlekPTSGSVTVAGKEISAARgESLRQArlkismVFQHFNLLW 95
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANR-RALRRT------IG*HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 96 SRTVS----ENIAFSMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:NF000106 96 GRRESfsgrENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 172 DPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEGDVLQVFT 230
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-219 |
9.82e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 1 MIVLRNISKLF----HQGKDTI------TA----------VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEK-PTS 59
Cdd:PRK13549 238 MMVGRELTALYprepHTIGEVIlevrnlTAwdpvnphikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 60 GSVTVAGKEISAargESLRQA-RLKISMVFQ---HFNLLWSRTVSENIAFSM--QIAGVPK----AEIKTrVAELIDLVG 129
Cdd:PRK13549 318 GEIFIDGKPVKI---RNPQQAiAQGIAMVPEdrkRDGIVPVMGVGKNITLAAldRFTGGSRiddaAELKT-ILESIQRLK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 130 LKGRENAYP-SRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKIC 208
Cdd:PRK13549 394 VKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLS 472
|
250
....*....|.
gi 495163008 209 DRVAVMENGRV 219
Cdd:PRK13549 473 DRVLVMHEGKL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-223 |
1.19e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLKISMVFQHfNLLWSRTVSENI 103
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQFSMIPQD-PVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 104 -----AFSMQI-AGVPKAEIKTRVA---ELIDLVGLKGRENaypsrLSGGQKQRVGIARALANR-PDVLLCDEATSALDP 173
Cdd:PTZ00243 1405 dpfleASSAEVwAALELVGLRERVAsesEGIDSRVLEGGSN-----YSVGQRQLMCMARALLKKgSGFILMDEATANIDP 1479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495163008 174 QTTDQILDLLQDINRRFglTIVLITHEMHVVRKiCDRVAVMENGRVVEEG 223
Cdd:PTZ00243 1480 ALDRQIQATVMSAFSAY--TVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-233 |
2.04e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLeKPTSGSVTVAGKEISAARGESL--------RQARLKISM-VFQHFNLl 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELarhraylsQQQTPPFAMpVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 wsrtvseniafsMQIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARAL-----ANRPD--VLLCDEA 167
Cdd:PRK03695 93 ------------HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 168 TSALDpQTTDQILDLLQDINRRFGLTIVLITHEM-HVVRKiCDRVAVMENGRVVEEGDVLQVFTHPQ 233
Cdd:PRK03695 161 MNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-223 |
2.07e-14 |
|
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: 74.60 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLK 83
Cdd:TIGR00957 1287 FRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQ---------HFNL-LWSRTVSENIAFSMQIAgvpkaEIKTRVAEL---IDLVGLKGRENaypsrLSGGQKQRVG 150
Cdd:TIGR00957 1362 ITIIPQdpvlfsgslRMNLdPFSQYSDEEVWWALELA-----HLKTFVSALpdkLDHECAEGGEN-----LSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 151 IARALANRPDVLLCDEATSALDPQTTdqilDLLQD-INRRF-GLTIVLITHEMHVVRKICdRVAVMENGRVVEEG 223
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETD----NLIQStIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-252 |
2.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 35 GIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQHfNLLWSRTVSENI-AFSMQ-IAGV 112
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV---LSIIPQS-PVLFSGTVRFNIdPFSEHnDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 113 PKAEIKTRVAELIDL--VGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRrf 190
Cdd:PLN03232 1342 WEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK-- 1419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 191 GLTIVLITHEMHVVRKiCDRVAVMENGRVVEegdvlqvFTHPQQPITRQ---FVRQISQEGADDA 252
Cdd:PLN03232 1420 SCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQELLSRDtsaFFRMVHSTGPANA 1476
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-212 |
2.21e-14 |
|
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: 73.82 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDTItavDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGsvtvagkeisaargESLRQARLK 83
Cdd:TIGR03719 7 MNRVSKVVPPKKEIL---KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 84 ISMVFQHFNLLWSRTVSENI---------------AFSMQIAGvPKAEI------KTRVAELIDLVGLKGREN------- 135
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVeegvaeikdaldrfnEISAKYAE-PDADFdklaaeQAELQEIIDAADAWDLDSqleiamd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 136 --------AYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDinrrFGLTIVLITHEmhvvRKI 207
Cdd:TIGR03719 149 alrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVTHD----RYF 220
|
....*
gi 495163008 208 CDRVA 212
Cdd:TIGR03719 221 LDNVA 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-219 |
8.77e-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: 71.78 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 18 ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGL-EKPTSGSVTVAGKEISAArgESLRQARLKISMV---FQHFNL 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIR--NPAQAIRAGIAMVpedRKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 LWSRTVSENIAFSM-----QIAGVPKAEIKTRVAELIDLVGLKGRENAYP-SRLSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:TIGR02633 351 VPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163008 168 TSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-215 |
2.09e-13 |
|
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: 70.97 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIY-----GIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAgkeisaargeslrqarLKISMVFQHFNLLWS 96
Cdd:COG1245 352 GGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----------------LKISYKPQYISPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIafsmqiagvpKAEIKTRV------AELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:COG1245 416 GTVEEFL----------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495163008 171 LDPQTTDQILDLLQDINRRFGLTIVLITHEMHVVRKICDRVAVME 215
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-215 |
2.39e-13 |
|
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: 68.59 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVE-----RGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKeisaargeslrqarlKISMVFQHFNLLWS 96
Cdd:cd03237 11 GEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---------------TVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAFSMQIAGVpKAEIKTRVAELIDLVGLKGREnayPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDpqtT 176
Cdd:cd03237 76 GTVRDLLSSITKDFYT-HPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD---V 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495163008 177 DQILdLLQDINRRFGL----TIVLITHEMHVVRKICDRVAVME 215
Cdd:cd03237 149 EQRL-MASKVIRRFAEnnekTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-223 |
2.58e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISklFHQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQAR 81
Cdd:TIGR00957 637 ITVHNAT--FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 82 LKISMVFQH-FNLLWSRTVSENIAFSMQIAGVPKAEiKTRVAElidlvglKGrenaypSRLSGGQKQRVGIARALANRPD 160
Cdd:TIGR00957 715 LRENILFGKaLNEKYYQQVLEACALLPDLEILPSGD-RTEIGE-------KG------VNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 161 VLLCDEATSALDPQTTDQILD-LLQDINRRFGLTIVLITHEMHVVRKIcDRVAVMENGRVVEEG 223
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-219 |
2.65e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGsvtvagkEISAARGeslrqarLKISMVFQHfNLLWSRT 98
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKG-------IKLGYFAQH-QLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENIAFSMQIAgvPKaEIKTRVAELIDLVGLKGRENAYPS-RLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTD 177
Cdd:PRK10636 391 DESPLQHLARLA--PQ-ELEQKLRDYLGGFGFQGDKVTEETrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495163008 178 QILDLLQDinrrFGLTIVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:PRK10636 468 ALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-225 |
2.69e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 12 HQGKDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLE--KPTSGSVTVAGKEISAARGEslRQARLKISMVFQ 89
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPE--ERAHLGIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 90 H-------FNLLWSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLVGLkgrENAYPSR-----LSGGQKQRVGIARALAN 157
Cdd:CHL00131 92 YpieipgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGM---DPSFLSRnvnegFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 158 RPDVLLCDEATSALDpqttdqiLDLLQDINRRFGL------TIVLITHEMHVVRKIC-DRVAVMENGRVVEEGDV 225
Cdd:CHL00131 169 DSELAILDETDSGLD-------IDALKIIAEGINKlmtsenSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
1.07e-11 |
|
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: 64.49 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeisaargeslrqarlKISMVFQhFNLLWSRTVSEN 102
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQ-FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFsmqiaGVPKAEIktRVAELIDLVGLKGRENAYPSR-----------LSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:cd03291 118 IIF-----GVSYDEY--RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163008 172 DPQTTDQILD-----LLQDINRrfgltiVLITHEMHVVRKiCDRVAVMENG 217
Cdd:cd03291 191 DVFTEKEIFEscvckLMANKTR------ILVTSKMEHLKK-ADKILILHEG 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-223 |
1.21e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPTS--GSVTVAGKEISaargeslRQARLKISMVFQHFNLLWSRTVSENIAFsMQ 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRETLVF-CS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 109 IAGVPKA---EIKTRVAE-LIDLVGLKGRE-----NAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQI 179
Cdd:PLN03211 166 LLRLPKSltkQEKILVAEsVISELGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495163008 180 LDLLQDINRRfGLTIVLITHE-MHVVRKICDRVAVMENGRVVEEG 223
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-219 |
1.32e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 36 IIGYSGAGKSTLIRLLNGLEKPTSGSVtvagkeisaargesLRQARLKISMVFQHFNLLWSRTVSENIAFSMQIAGVPKA 115
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 116 EIKTRVAELidlvGLKGRENAYPS-RLSGGQKQRVGIARALANRPDVLLCDEATSALDpqtTDQILDLLQDInRRFGLTI 194
Cdd:PLN03073 606 KLRAHLGSF----GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGL-VLFQGGV 677
|
170 180
....*....|....*....|....*
gi 495163008 195 VLITHEMHVVRKICDRVAVMENGRV 219
Cdd:PLN03073 678 LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-221 |
1.68e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 35 GIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAArgeSLRQARLKISMVFQHfNLLWSRTVSENIAFSMQIAGVPK 114
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQA-PVLFSGTVRFNLDPFNEHNDADL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 115 AEIKTRvAELIDLV-----GL-----KGRENaypsrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQtTDQILDllQ 184
Cdd:PLN03130 1345 WESLER-AHLKDVIrrnslGLdaevsEAGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQ--K 1415
|
170 180 190
....*....|....*....|....*....|....*...
gi 495163008 185 DINRRF-GLTIVLITHEMHVVRKiCDRVAVMENGRVVE 221
Cdd:PLN03130 1416 TIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-172 |
1.74e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIY-----GIIGYSGAGKSTLIRLLNGLEKPTSGSVTvagkeisaargeslrqARLKISMVFQHFNLLWS 96
Cdd:PRK13409 351 GDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVD----------------PELKISYKPQYIKPDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIafsmqiagvpkAEIKTRVA------ELIDLVGLkgrENAYPSR---LSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:PRK13409 415 GTVEDLL-----------RSITDDLGssyyksEIIKPLQL---ERLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEP 480
|
....*
gi 495163008 168 TSALD 172
Cdd:PRK13409 481 SAHLD 485
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-199 |
3.64e-11 |
|
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: 64.00 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAgkeisaargeslrqARLKISMVFQ--HFNLlwsRT 98
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------------AKGKLFYVPQrpYMTL---GT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 99 VSENI-----AFSMQIAGVPKAEIKtRVAELIDLVGLKGRENAYPS------RLSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:TIGR00954 531 LRDQIiypdsSEDMKRRGLSDKDLE-QILDNVQLTHILEREGGWSAvqdwmdVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 495163008 168 TSALDPQTTDQILDLLqdinRRFGLTIVLITH 199
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-220 |
5.78e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAgKEISAARgesLRQ--ARLKISMVFQHfnllwsrtV 99
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVAR---LQQdpPRNVEGTVYDF--------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIA-----------FSMQIAGVPK-------AEIK------------TRVAELIDLVGLKGreNAYPSRLSGGQKQRV 149
Cdd:PRK11147 88 AEGIEeqaeylkryhdISHLVETDPSeknlnelAKLQeqldhhnlwqleNRINEVLAQLGLDP--DAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 150 GIARALANRPDVLLCDEATSALDPQTTDQILDLLQDinrrFGLTIVLITHEMHVVRKICDRVAVMENGRVV 220
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-217 |
1.18e-10 |
|
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: 63.01 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGkeisaargeslrqarlKISMVFQhFNLLWSRTVSEN 102
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 103 IAFsmqiaGVPKAEIktRVAELIDLVGLKGRENAYPSR-----------LSGGQKQRVGIARALANRPDVLLCDEATSAL 171
Cdd:TIGR01271 507 IIF-----GLSYDEY--RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163008 172 DPQTTDQILD-----LLQDINRrfgltiVLITHEMHVVRKiCDRVAVMENG 217
Cdd:TIGR01271 580 DVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-200 |
1.59e-10 |
|
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: 59.56 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKP--TSGSVTVAGKEisaaRGESLRQarlKISMVFQHFNLLWSRTV 99
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRP----LDKNFQR---STGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 100 SENIAFSMQIAGvpkaeiktrvaelidlvglkgrenaypsrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQI 179
Cdd:cd03232 97 REALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180
....*....|....*....|.
gi 495163008 180 LDLLQDINRRfGLTIVLITHE 200
Cdd:cd03232 148 VRFLKKLADS-GQAILCTIHQ 167
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-200 |
2.11e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 15 KDTITAVDDVNLEVERGQIYGIIGYSGAGKSTlirLLNGL-EKPTSGSVTvAGKEISAARGESLRQARlKISMVFQHFNL 93
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLaERVTTGVIT-GGDRLVNGRPLDSSFQR-SIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 94 LWSRTVSENIAFSM---QIAGVPKAEIKTRVAELIDLVGLKGRENAY----PSRLSGGQKQRVGIARALANRPDVLL-CD 165
Cdd:TIGR00956 848 LPTSTVRESLRFSAylrQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*
gi 495163008 166 EATSALDPQTTDQILDLLQDINRRfGLTIVLITHE 200
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQ 961
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-172 |
3.17e-10 |
|
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: 59.69 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVtvaGKE------ISAARG-------ESLRQARLKISMVFQHFNLLwSR 97
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPpdwdeiLDEFRGselqnyfTKLLEGDVKVIVKPQYVDLI-PK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163008 98 TVSENIafsmqIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:cd03236 102 AVKGKV-----GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-227 |
3.44e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 25 NLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQArlkISMVFQHFN--LL------WS 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDEWQRNNtdMLspgeddTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAfsmqiAGVPKAEIKTRVAELIDLVGLKGRENAYpsrLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTT 176
Cdd:PRK10938 100 RTTAEIIQ-----DEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163008 177 DQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEEG---DVLQ 227
Cdd:PRK10938 172 QQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGereEILQ 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-199 |
3.58e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 3 VLRNISKlFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGsvtvagkEISAARGeslrqarL 82
Cdd:PRK11819 8 TMNRVSK-VVPPKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPG-------I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 83 KISMVFQHFNLLWSRTVSENIafsmqIAGVpkAEIKTRVAELIDLVGLKGRENAY------------------------- 137
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENV-----EEGV--AEVKAALDRFNEIYAAYAEPDADfdalaaeqgelqeiidaadawdlds 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 138 -----------P------SRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDinrrFGLTIVLITH 199
Cdd:PRK11819 144 qleiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVTH 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-172 |
3.85e-10 |
|
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: 60.95 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 29 ERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTV-AGKE--ISAARG-------ESLRQARLKISMVFQHFNLL---W 95
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWDevLKRFRGtelqdyfKKLANGEIKVAHKPQYVDLIpkvF 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 96 SRTVSENIAfsmqiagvpKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:COG1245 177 KGTVRELLE---------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
4.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISAARGESLRQarlkISMVFQHFNLLWSRTVS 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ----LCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 101 ENIAFSMQIAGVpkaeiKTRVAELIDLVGLkGRENAYP-SRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQI 179
Cdd:PRK13540 93 ENCLYDIHFSPG-----AVGITELCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 495163008 180 LDLLQDiNRRFGLTIVLITHE 200
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQ 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-224 |
4.69e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLE--KPTSGSVTVAGKEISAARGESlrQARLKISMVFQH-------FNLL 94
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQYpveipgvSNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSMQIAGVPKAEIKTRVAELIDLvgLKGRENAYPSRL----SGGQKQRVGIARALANRPDVLLCDEATSA 170
Cdd:PRK09580 98 FLQTALNAVRSYRGQEPLDRFDFQDLMEEKIAL--LKMPEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 171 LDP---QTTDQILDLLQDINRRFgltiVLITHEMHVVRKI-CDRVAVMENGRVVEEGD 224
Cdd:PRK09580 176 LDIdalKIVADGVNSLRDGKRSF----IIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
24-242 |
5.33e-10 |
|
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: 59.15 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTL----IRLLNGLEkptsGSVTVAGKEISAARGESLRQarlKISMVFQ---------H 90
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTLRS---RLSIILQdpilfsgsiR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 91 FNLLWSRTVSENIAF-SMQIAgvpkaEIKTRVAEL---IDLVGLKGRENaypsrLSGGQKQRVGIARALANRPDVLLCDE 166
Cdd:cd03288 113 FNLDPECKCTDDRLWeALEIA-----QLKNMVKSLpggLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 167 ATSALDpQTTDQILD--LLQDINRRfglTIVLITHEMHVVRKiCDRVAVMENGRVVEEGDVLQVFTHPQQPITrQFVR 242
Cdd:cd03288 183 ATASID-MATENILQkvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA-SLVR 254
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-222 |
6.06e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLE--KPTSGSVTVAGKEISAArgeSLRQA-RLKISMVFQ---HFNLL 94
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVS---TVSDAiDAGLAYVTEdrkGYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 95 WSRTVSENIAFSM--QIA--GVPKAEIKTRVAElidlvGLKGREN-AYPS------RLSGGQKQRVGIARALANRPDVLL 163
Cdd:NF040905 353 LIDDIKRNITLANlgKVSrrGVIDENEEIKVAE-----EYRKKMNiKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 164 CDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENGRVVEE 222
Cdd:NF040905 428 LDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-210 |
1.24e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 30 RGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVtvagKEISAargeslrqarlkismvfqhfnllwsrtvseniafsmqi 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----IYIDG-------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 110 agvpkaeikTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDL-----LQ 184
Cdd:smart00382 39 ---------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|....*.
gi 495163008 185 DINRRFGLTIVLITHEMHVVRKICDR 210
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-219 |
2.39e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTItaVDDVNLEVERGQIYGIIGYSGAGKSTL----IRLLNglekpTSGSVTVAGKEISAArgeSL 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSV---PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 78 RQARLKISMVFQHFnLLWSRTVSENiafsMQIAGVPKAEIKTRVAELidlVGLKGRENAYPSRL-----------SGGQK 146
Cdd:cd03289 73 QKWRKAFGVIPQKV-FIFSGTFRKN----LDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163008 147 QRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQdinRRF-GLTIVLITHEMHVVRKiCDRVAVMENGRV 219
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK---QAFaDCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-227 |
4.56e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 21 VDDVNLEVERGQIYGIIGYSGAGKSTLI----RLLNglekpTSGSVTVAGKEISAArgeSLRQARLKISMVFQHFnLLWS 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS-----TEGEIQIDGVSWNSV---TLQTWRKAFGVIPQKV-FIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 97 RTVSENIAFSMQIAgvpKAEIkTRVAELidlVGLKGRENAYPSRL-----------SGGQKQRVGIARALANRPDVLLCD 165
Cdd:TIGR01271 1306 GTFRKNLDPYEQWS---DEEI-WKVAEE---VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163008 166 EATSALDPqTTDQILDllQDINRRFG-LTIVLITHEMHVVRKiCDRVAVMEnGRVVEEGDVLQ 227
Cdd:TIGR01271 1379 EPSAHLDP-VTLQIIR--KTLKQSFSnCTVILSEHRVEALLE-CQQFLVIE-GSSVKQYDSIQ 1436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-172 |
6.81e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 28 VERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAG---KEISAARG-------ESLRQARLKISMVFQHFNLLwsr 97
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFRGtelqnyfKKLYNGEIKVVHKPQYVDLI--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 tvseniafsmqiagvPKAeIKTRVAELIDLVGLKGRENAYPSR-------------LSGGQKQRVGIARALANRPDVLLC 164
Cdd:PRK13409 173 ---------------PKV-FKGKVRELLKKVDERGKLDEVVERlglenildrdiseLSGGELQRVAIAAALLRDADFYFF 236
|
....*...
gi 495163008 165 DEATSALD 172
Cdd:PRK13409 237 DEPTSYLD 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-200 |
8.80e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 19 TAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKeisaargeslrqarLKISMVFQHFNLL-WSR 97
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK--------------LEVAYFDQHRAELdPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIAFSMQ---IAGVPKAEIktrvAELIDLVglkgrenAYPSR-------LSGGQKQRVGIARALANRPDVLLCDEA 167
Cdd:PRK11147 399 TVMDNLAEGKQevmVNGRPRHVL----GYLQDFL-------FHPKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 495163008 168 TSALDPQTtdqiLDLLQDINRRFGLTIVLITHE 200
Cdd:PRK11147 468 TNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-217 |
1.02e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEisaaRGESLRQARLK------ISMVFQHFNLLWSRTVSENIA 104
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE----RLGKLRQDQFAfeeftvLDTVIMGHTELWEVKQERDRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 105 FSMQIA----GVPKAEIKTRVAELiD-----------LVGL---KGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDE 166
Cdd:PRK15064 103 YALPEMseedGMKVADLEVKFAEM-DgytaearagelLLGVgipEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163008 167 ATSALDPQTtdqILDLLQDINRRfGLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:PRK15064 182 PTNNLDINT---IRWLEDVLNER-NSTMIIISHDRHFLNSVCTHMADLDYG 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-223 |
1.61e-08 |
|
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: 54.19 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 23 DVNLEVERGQIYGIIGYSGAGKSTLI---------------------RLLNGLEKP-----TSGSVTVAGKEISAARgeS 76
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPdvdsiEGLSPAIAIDQKTTSR--N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 77 LRQARLKISMVFQHFNLLWSRtvseniafsmqiagvpkAEIKTRVAELIDlVGLkgrENAYPSR----LSGGQKQRVGIA 152
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFAR-----------------VGIRERLGFLVD-VGL---GYLTLSRsaptLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 153 RAL-ANRPDVL-LCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRkICDRV------AVMENGRVVEEG 223
Cdd:cd03270 150 TQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR-AADHVidigpgAGVHGGEIVAQG 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-174 |
2.03e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 24 VNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKeiSAARGESLRQarlkISMVFQHFNLLWSRTVSENI 103
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRF----MAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 104 AFsmqIAGVPKAEIKTRVAELIDLVGLKGRENAYPSRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQ 174
Cdd:PRK13543 104 HF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-173 |
6.68e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 22 DDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGlEKPT--SGSVTVAGKEisAARGESLRQARLKISMVFQHFNLLW--SR 97
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRR--RGSGETIWDIKKHIGYVSSSLHLDYrvST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 98 TVSENIafsmqIAG----------VPKAEIKtRVAELIDLVGLKGRENAYPSR-LSGGQKQRVGIARALANRPDVLLCDE 166
Cdd:PRK10938 354 SVRNVI-----LSGffdsigiyqaVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDE 427
|
....*..
gi 495163008 167 ATSALDP 173
Cdd:PRK10938 428 PLQGLDP 434
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-207 |
1.83e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 36 IIGYSGAGKSTLIRLLN-GL--EKPTSGSVTVAGKEIsAARGESlrqaRLKISMVFQHFN---LLWSRTVS--ENIAFsm 107
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyALtgELPPNSKGGAHDPKL-IREGEV----RAQVKLAFENANgkkYTITRSLAilENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 108 qiagVPKAEIKTRVAELIDlvglkgrenaypsRLSGGQKQ------RVGIARALANRPDVLLCDEATSALDPQTTD-QIL 180
Cdd:cd03240 100 ----CHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLA 162
|
170 180
....*....|....*....|....*..
gi 495163008 181 DLLQDINRRFGLTIVLITHEMHVVRKI 207
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
56-243 |
2.25e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 56 KPTSGSVTVAGKEISAARGESLRQArlkisMVFqhFNLLWSRTVSEniafsmQIAGVPKAEIKTRVAELIDlVGLkgrEN 135
Cdd:TIGR00630 417 KPEALAVTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEK------KIAEEVLKEIRERLGFLID-VGL---DY 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 136 AYPSR----LSGGQKQRVGIARALANR-PDVL-LCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVRKiCD 209
Cdd:TIGR00630 480 LSLSRaagtLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-AD 557
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495163008 210 RV------AVMENGRVVEEGDVLQVFTHPQQpITRQFVRQ 243
Cdd:TIGR00630 558 YVidigpgAGEHGGEVVASGTPEEILANPDS-LTGQYLSG 596
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-224 |
3.41e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 4 LRNISKLFHQGKDT--ITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLL----NGLEKPTSGSVTVAG---KEISAA-R 73
Cdd:TIGR00956 58 LTRGFRKLKKFRDTktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKHyR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 74 GESLRQARLKIsmvfqHFNLLwsrTVSENIAFSM-------QIAGVPKAEIKTRVAELIDLV-GLKGRENA-----YPSR 140
Cdd:TIGR00956 138 GDVVYNAETDV-----HFPHL---TVGETLDFAArcktpqnRPDGVSREEYAKHIADVYMATyGLSHTRNTkvgndFVRG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 141 LSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDINRRFGLT-IVLITHEMHVVRKICDRVAVMENGRV 219
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQ 289
|
....*
gi 495163008 220 VEEGD 224
Cdd:TIGR00956 290 IYFGP 294
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-183 |
4.54e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 36 IIGYSGAGKSTLIRLLNGLEKPTSGSVTVAGKEISaargeslRQARLKISMVFQHFNLLWSRTVSENIAFSMQI----AG 111
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-------NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIynsaET 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 112 VPKAEIKTRVAELIDlvglkgrENAYpsRLSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLL 183
Cdd:PRK13541 104 LYAAIHYFKLHDLLD-------EKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-205 |
9.18e-07 |
|
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: 48.47 E-value: 9.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 139 SRLSGGQKQRVGIARALANRPD--VLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVR 205
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLS 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-211 |
1.16e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 1.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163008 139 SRLSGGQKQRVGIARALAN---RPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVrKICDRV 211
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV-KVADYV 881
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-209 |
4.15e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 4.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163008 141 LSGGQKQRVGIARALANR---PDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITHEMHVVrKICD 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVI-KCAD 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-243 |
7.52e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 117 IKTRVAELIDLvglkGRENAYPSR----LSGGQKQRVGIARALANRPD--VLLCDEATSALDPQTTDQILDLLQDInRRF 190
Cdd:PRK00635 453 LKSRLSILIDL----GLPYLTPERalatLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQ 527
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 191 GLTIVLITHEMHVVrKICDRVAVMENGRVVEEGDVL-----QVFTHPQQPITRQFVRQ 243
Cdd:PRK00635 528 GNTVLLVEHDEQMI-SLADRIIDIGPGAGIFGGEVLfngspREFLAKSDSLTAKYLRQ 584
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-62 |
1.98e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163008 2 IVLRNISKLFhqgkDTITAVDDVNLEVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGSV 62
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-215 |
2.16e-05 |
|
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: 44.49 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 27 EVERGQIYGIIGYSGAGKSTLIRLLNGLEKPTSGsvtvagkeisaargeslrqarlkismvfqhfNLLWSRTvseNIAFS 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------------------------------NDEWDGI---TPVYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 107 MQIAgvpkaeiktrvaelidlvglkgrenaypsRLSGGQKQRVGIARALANRPDVLLCDEATSALDpqtTDQILDLLQDI 186
Cdd:cd03222 67 PQYI-----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD---IEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|...
gi 495163008 187 nRRFGL----TIVLITHEMHVVRKICDRVAVME 215
Cdd:cd03222 115 -RRLSEegkkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-172 |
6.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 14 GKDTITavdDVNLEVERGQIYGIIGYSGAGKSTLIRLL-----NGL---------EKPTSGSVTVAGKEISAARGESLRQ 79
Cdd:PLN03073 189 GRDLIV---DASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaiDGIpkncqilhvEQEVVGDDTTALQCVLNTDIERTQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 80 ARLKISMVFQHFNLLWSRTVSENIafSMQIAGVPKAEIKTRVA------ELIDLVGLKGRENAYPSRLS----------- 142
Cdd:PLN03073 266 LEEEAQLVAQQRELEFETETGKGK--GANKDGVDKDAVSQRLEeiykrlELIDAYTAEARAASILAGLSftpemqvkatk 343
|
170 180 190
....*....|....*....|....*....|...
gi 495163008 143 ---GGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PLN03073 344 tfsGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
1.85e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163008 141 LSGGQKQRVGIARALANR---PDVLLCDEATSALDPQTTDQILDLLQDInRRFGLTIVLITHEMHVVR 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 896
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-172 |
2.27e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 31 GQIYGIIGYSGAGKSTLIRLLNGLEKP--TSGSVTVAG---KEISAARGESL--------RQARLKISMVFQHFnLLWSR 97
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkKQETFARISGYceqndihsPQVTVRESLIYSAF-LRLPK 984
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163008 98 TVS--ENIAFSMQiagvpkaeiktrVAELIDLVGLKGRENAYP--SRLSGGQKQRVGIARALANRPDVLLCDEATSALD 172
Cdd:PLN03140 985 EVSkeEKMMFVDE------------VMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-199 |
1.13e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKlfHQGKDTITAVDDVNLevergqiygIIGYSGAGKSTLIRLLN-GLEkptsGSVTVAGKEISAARGESLRQA 80
Cdd:COG0419 5 LRLENFRS--YRDTETIDFDDGLNL---------IVGPNGAGKSTILEAIRyALY----GKARSRSKLRSDLINVGSEEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 81 RlkISMVFQH-------------FNLLWSRTVSENIAFSMQIAGVP------------KAEIKTRVAELIDLVGLKGR-- 133
Cdd:COG0419 70 S--VELEFEHggkryrierrqgeFAEFLEAKPSERKEALKRLLGLEiyeelkerlkelEEALESALEELAELQKLKQEil 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 134 ----ENAYPSRLSGGQKQRVGIARALAnrpdvLLCDeaTSALDPQTTDQILDLLQDinrrfgltIVLITH 199
Cdd:COG0419 148 aqlsGLDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
141-186 |
2.89e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 2.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 495163008 141 LSGGQKQRVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQDI 186
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
141-199 |
3.65e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.40 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163008 141 LSGGQKQRVGIARALA--------NRPDVLLCDEATSALDPQTTDQILDLLQDINRRfGLTIVLITH 199
Cdd:PRK10246 950 LSGGESFLVSLALALAlsdlvshkTRIDSLFLDEGFGTLDSETLDTALDALDALNAS-GKTIGVISH 1015
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-185 |
7.25e-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: 35.29 E-value: 7.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 139 SRLSGGQKQ-------------RVGIARALANRPDVLLCDEATSALDPQTTDQILDLLQD 185
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YlqF_related_GTPase |
cd01849 |
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
2-59 |
8.66e-03 |
|
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.
Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 36.21 E-value: 8.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163008 2 IVLRNISKLFHQGKDTITAVDDVNLEVERGQI-YGIIGYSGAGKSTLIR-LLNGLEKPTS 59
Cdd:cd01849 61 TFFISATNGQGILKLKAEITKQKLKLKYKKGIrVGVVGLPNVGKSSFINaLLNKFKLKVG 120
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