|
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: 574.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 241 VRQVSQYAEEETFNTELANDLE-GTVIRLTFTGHSTHKPIVGELTLRYGLPFNILHGKMTQTAHGVFGQLWVHVAASDEQ 319
Cdd:COG1135 241 LPTVLNDELPEELLARLREAAGgGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*....
gi 695703442 320 LNNILADLQHSDIEGEVIK 338
Cdd:COG1135 321 IDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-339 |
7.22e-175 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 488.54 E-value: 7.22e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 241 VRQVSQYAEEETFNTELANDL---EGTVIRLTFTGHSTHKPIVGELTLRYGLPFNILHGKMTQTAHGVFGQLWVHVAASD 317
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPttgSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|..
gi 695703442 318 EQLNNILADLQHSDIEGEVIKH 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 |
2.69e-153 |
|
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: 429.69 E-value: 2.69e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 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 |
4.55e-118 |
|
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: 344.56 E-value: 4.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 241 VRQVSQYAEEETFNTELANDLEGT---VIRLTFTGHSTHKPIVGELTLRYGLPFNILHGKMTQTAHGVFGQLWVHVAASD 317
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADsvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330 340
....*....|....*....|
gi 695703442 318 EQLNNILADLQHSDIEGEVI 337
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVL 340
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
5.61e-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: 306.83 E-value: 5.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFD-NGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQ 79
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQH----FNLLWsrTVRENIAFSMQIAGV-PKAKIAARVAELVELVGLkGREHA--YPSQLSGGQKQRVGIA 152
Cdd:COG1123 340 LRRRVQMVFQDpyssLNPRM--TVGDIIAEPLRLHGLlSRAERRERVAELLERVGL-PPDLAdrYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
....*..
gi 695703442 233 QQPITQQ 239
Cdd:COG1123 497 QHPYTRA 503
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
7.08e-100 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 294.21 E-value: 7.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAaKGEALRQA 80
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFS-MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQ 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 695703442 240 FVRQV 244
Cdd:COG1126 235 FLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
4.84e-98 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 289.25 E-value: 4.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RL-KISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRkICDRVAVMENGKVVEE 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
2.49e-93 |
|
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: 277.63 E-value: 2.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVL---DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSM-QIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVlSVFTHPQQPITQQ 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP-EELLASDDPWVRQ 239
|
..
gi 695703442 240 FV 241
Cdd:COG1127 240 FL 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
8.69e-93 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 275.78 E-value: 8.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:COG2884 1 MIRFENVSKRYPGGREAL---SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 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 |
1.18e-92 |
|
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: 275.14 E-value: 1.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LK-ISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRkICDRVAVMENGKV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
8.75e-91 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 271.96 E-value: 8.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalrqa 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlkISMVFQHFNLL-WsRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG1116 82 ---RGVVFQEPALLpW-LTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMH-VVRkICDRVAVMEN--GKVVEEGDV 225
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVEEIDV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
2.79e-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: 272.70 E-value: 2.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKP---STGSVTVNGQDISAAKGEAL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 78 RQARLK-ISMVFQH----FNLLWsrTVRENIAFSMQI-AGVPKAKIAARVAELVELVGL---KGREHAYPSQLSGGQKQR 148
Cdd:COG0444 81 RKIRGReIQMIFQDpmtsLNPVM--TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 149 VGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSV 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250
....*....|
gi 695703442 229 FTHPQQPITQ 238
Cdd:COG0444 239 FENPRHPYTR 248
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-250 |
1.79e-89 |
|
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: 268.21 E-value: 1.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQa 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlKISMVFQH----FNLLWsrTVRENIAFSMQIAGVPKakIAARVAELVELVGLkGREHA--YPSQLSGGQKQRVGIARA 154
Cdd:COG1124 80 --RVQMVFQDpyasLHPRH--TVDRILAEPLRIHGLPD--REERIAELLEQVGL-PPSFLdrYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|....*.
gi 695703442 235 PITQQFVRQVSQYAEE 250
Cdd:COG1124 233 PYTRELLAASLAFERA 248
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-244 |
3.10e-89 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 272.75 E-value: 3.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVF-DNGKVALT-------------------AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTG 60
Cdd:COG4175 3 KIEVRNLYKIFgKRPERALKlldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 61 SVTVNGQDISAAKGEALRQARL-KISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPS 139
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 140 QLSGGQKQRVGIARALANNPDVLLCDEATSALDP------QttdqilDLLLDINRRFNLTIVLITHEMHVVRKICDRVAV 213
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremQ------DELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
|
250 260 270
....*....|....*....|....*....|....
gi 695703442 214 MENGKVVEEG---DVLsvfTHPQQPITQQFVRQV 244
Cdd:COG4175 237 MKDGRIVQIGtpeEIL---TNPANDYVADFVEDV 267
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
3.64e-88 |
|
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: 263.98 E-value: 3.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQH----FNLLWsrTVRENIAFSMQIAGVP--KAKIAARVAELVELVGL-KGREHAYPSQLSGGQKQRVGIAR 153
Cdd:cd03257 81 RKEIQMVFQDpmssLNPRM--TIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-244 |
8.99e-88 |
|
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: 264.51 E-value: 8.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVF-DNGKVALT-------------------AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGS 61
Cdd:cd03294 1 IKIKGLYKIFgKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 62 VTVNGQDISAAKGEALRQARLK-ISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQ 140
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 141 LSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....
gi 695703442 221 EEGDVLSVFTHPQQPITQQFVRQV 244
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGV 264
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
7.94e-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: 7.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQAR 81
Cdd:COG1122 1 IELENLSFSYPGGTPAL---DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-225 |
1.52e-86 |
|
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: 259.71 E-value: 1.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsaakgealRQAR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV--------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLL-WsRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03293 73 PDRGYVFQQDALLpW-LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMEN--GKVVEEGDV 225
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-238 |
1.12e-84 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 258.89 E-value: 1.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 10 VFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKISMVFQ 89
Cdd:COG4608 23 LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 90 H-FNLLWSR-TVRENIAFSMQIAGV-PKAKIAARVAELVELVGLKgREHA--YPSQLSGGQKQRVGIARALANNPDVLLC 164
Cdd:COG4608 103 DpYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLR-PEHAdrYPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 165 DEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQ 238
Cdd:COG4608 182 DEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-240 |
6.37e-83 |
|
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: 250.88 E-value: 6.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAR 81
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSM-QIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHpQQPITQQF 240
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
2.27e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 249.97 E-value: 2.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPAL---DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENI-------------AFSMqiagVPKAKIAaRVAELVELVGLKGREHAYPSQLSGGQKQ 147
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 148 RVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-225 |
2.24e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 247.28 E-value: 2.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsaakGEALRQAR 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-233 |
3.04e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 245.78 E-value: 3.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEAlRQa 80
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlkISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG3842 79 ---VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITH------EMhvvrkiCDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeealAL------ADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
1.03e-77 |
|
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: 237.03 E-value: 1.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQAR 81
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
2.07e-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: 236.27 E-value: 2.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQAR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHV----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFS-MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-246 |
2.82e-77 |
|
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: 238.12 E-value: 2.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFD-NGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQhF--NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLkgrEHAY----PSQLSGGQKQRVGIARA 154
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGL---DEEYlersPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
250 260
....*....|....*....|
gi 695703442 235 --------PITQQFVRQVSQ 246
Cdd:TIGR04521 237 lekigldvPEITELARKLKE 256
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
2.86e-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: 2.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 3 VLSNISKVFDNGKVAltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeaLRQARL 82
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 KISMVFQHFNL-LWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
5.28e-75 |
|
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: 239.81 E-value: 5.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPS---TGSVTVNGQDISAAkGEAL 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 78 RQARlkISMVFQHF-NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:COG1123 81 RGRR--IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-241 |
6.31e-75 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 234.66 E-value: 6.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgeaLRQAR 81
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----LPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
4.33e-74 |
|
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: 228.61 E-value: 4.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAR 81
Cdd:cd03256 1 IEVENLSKTYPNGKKAL---KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSM--------QIAG-VPKAKIAaRVAELVELVGLKGREHAYPSQLSGGQKQRVGIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGlFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
5.46e-74 |
|
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: 228.72 E-value: 5.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHA--YPSQLSGGQKQRVGIARALANNP 159
Cdd:cd03295 76 -KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdrYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQ 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 695703442 240 FVRQ 243
Cdd:cd03295 235 FVGA 238
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
1.67e-73 |
|
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: 227.18 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQAL---KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENI-----AFSMQIAGV----PKAKIAaRVAELVELVGLKGREHAYPSQLSGGQKQRVGI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLlgrfSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 152 ARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-239 |
6.45e-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: 234.96 E-value: 6.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEkPSTGSVTVNGQDISAAKGEALRQARLKISMVFQH-FNLLWS 96
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFGSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 R-TVRENIAFSMQI--AGVPKAKIAARVAELVELVGLKGR-EHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:COG4172 378 RmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 173 PQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQ 239
Cdd:COG4172 458 VSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-239 |
1.50e-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: 231.11 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLS--NISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKS----TLIRLL-NGLEKPStGSVTVNGQDISAAK 73
Cdd:COG4172 4 MPLLSveDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLpDPAAHPS-GSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 74 GEALRQAR-LKISMVFQH----FNLLWsrTVRENIAFSMQI-AGVPKAKIAARVAELVELVGL---KGREHAYPSQLSGG 144
Cdd:COG4172 83 ERELRRIRgNRIAMIFQEpmtsLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 145 QKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250
....*....|....*
gi 695703442 225 VLSVFTHPQQPITQQ 239
Cdd:COG4172 241 TAELFAAPQHPYTRK 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
8.57e-71 |
|
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: 218.21 E-value: 8.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFdNGKvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsAAKGEALRQAR 81
Cdd:cd03229 1 LELKNVSKRY-GQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSmqiagvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPDV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
7.12e-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: 216.89 E-value: 7.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAR 81
Cdd:cd03292 1 IEFINVTKTYPNGTAAL---DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.49e-69 |
|
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: 216.92 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqA 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDAR--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RL---KISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKiaARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALAN 157
Cdd:COG4181 86 RLrarHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEE 222
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.52e-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: 217.60 E-value: 1.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqA 80
Cdd:COG0411 4 LLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQ----------IAGVPKAK-----IAARVAELVELVGLKGREHAYPSQLSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRARreereARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 695703442 226 LSVFTHPQ 233
Cdd:COG0411 238 AEVRADPR 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
1.34e-68 |
|
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: 215.76 E-value: 1.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgEALRQAR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE--ENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFTH 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
2.84e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 217.63 E-value: 2.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQA 80
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
5.94e-66 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 208.45 E-value: 5.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdNGKVALTAVDnvnLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKG-----E 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 76 ALRQARLKISMVFQHFNLLWSRTVREN-IAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARA 154
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLL--LDINRRfnlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIrqLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|.
gi 695703442 233 QQPITQQFVRQ 243
Cdd:PRK11264 236 QQPRTRQFLEK 246
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-241 |
7.06e-66 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 208.35 E-value: 7.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL--EKPS---TGSVTVNGQDISAAKG--EALRQarlKISMVFQHFN 92
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDVdvVELRR---RVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 93 LLwSRTVRENIAFSMQIAGV-PKAKIAARVAELVELVGL----KGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:COG1117 103 PF-PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 168 TSALDPQTTDQILDLLLDINRRFnlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:COG1117 182 TSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-225 |
2.02e-65 |
|
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: 205.88 E-value: 2.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEK-----PSTGSVTVNGQDISAAKGEA 76
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRqARLKISMVFQHFNLLWSrTVRENIAFSMQIAGV-PKAKIAARVAELVELVGLKGREH--AYPSQLSGGQKQRVGIAR 153
Cdd:cd03260 77 LE-LRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfnLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
5.58e-65 |
|
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: 205.16 E-value: 5.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQAR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-233 |
1.45e-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: 204.21 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeALRQARLK 83
Cdd:cd03219 3 VRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWSRTVRENI----------AFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIAR 153
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-245 |
1.46e-64 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 204.56 E-value: 1.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEaLRQA 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFS-MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQ 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*.
gi 695703442 240 FVRQVS 245
Cdd:PRK09493 235 FLQHVS 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
7.58e-64 |
|
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: 202.40 E-value: 7.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgEALRQA 80
Cdd:COG4555 1 MIEVENLSKKY--GKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
24-240 |
1.88e-63 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 201.95 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDI---SAAKGEA-------LRQARLKISMVFQHFNL 93
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkPDRDGELvpadrrqLQRIRTRLGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 lWS-RTVRENIAFS-MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:COG4598 107 -WShMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 172 DPQTTDQILDL---LLDINRrfnlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQF 240
Cdd:COG4598 186 DPELVGEVLKVmrdLAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
4.73e-63 |
|
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: 198.01 E-value: 4.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRqar 81
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLWSRTVRENIafsmqiagvpkakiaarvaelvelvglkgrehaypsQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03230 74 -RIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-240 |
2.98e-62 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 198.31 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQ--DISAAKGE-ALR 78
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 QARLKISMVFQHFNLLWSRTVREN-IAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVlSVFTHPQqpiT 237
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ---T 233
|
...
gi 695703442 238 QQF 240
Cdd:PRK11124 234 EAF 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-240 |
3.12e-62 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 198.31 E-value: 3.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNG------QDISAAKGE 75
Cdd:COG4161 3 IQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 76 ALRQarlKISMVFQHFNLLWSRTVREN-IAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARA 154
Cdd:COG4161 79 LLRQ---KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDvLSVFTHPQq 234
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ- 232
|
....*.
gi 695703442 235 piTQQF 240
Cdd:COG4161 233 --TEAF 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
6.65e-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: 6.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGealrQAR 81
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV----QER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLWSRTVRENIAFSMQI----AGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALAN 157
Cdd:cd03296 75 -NVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPIT 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 695703442 238 QQFV 241
Cdd:cd03296 234 YSFL 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
1.02e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.08 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalrqa 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RlkiSMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:COG4525 78 R---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
2.42e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.77 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDnGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsaakgealRQA 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVL---EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSR--TVRENIAF----SMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARA 154
Cdd:COG1121 74 RRRIGYVPQRAEVDWDFpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMeNGKVVEEGDVLSVFTHP 232
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
7.32e-59 |
|
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: 201.22 E-value: 7.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVAltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:COG2274 474 IELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFSMqiAGVPKAKI--AARVAELVELV-----GLKGR--EHAypSQLSGGQKQRVGIA 152
Cdd:COG2274 550 -QIGVVLQD-VFLFSGTIRENITLGD--PDATDEEIieAARLAGLHDFIealpmGYDTVvgEGG--SNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-238 |
1.79e-58 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 191.33 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKISMVFQH-FNLLWSR- 97
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYGSLNPRk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQI-AGVPKAKIAARVAELVELVGLKGrEHA--YPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK11308 110 KVGQILEEPLLInTSLSAAERREKALAMMAKVGLRP-EHYdrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 175 TTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQ 238
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
4.14e-58 |
|
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: 187.19 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEAlRQAR 81
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EP-REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
8.17e-58 |
|
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: 186.17 E-value: 8.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFdnGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealRQAR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR----KAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDInrRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-229 |
9.54e-58 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 188.33 E-value: 9.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGK-VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsAAKGEALRQA 80
Cdd:PRK13637 3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNL-LWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHA--YPSQLSGGQKQRVGIARALAN 157
Cdd:PRK13637 82 RKKVGLVFQYPEYqLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
1.37e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFSMQIAGvpKAKIAARVAELVELVGLkgrEHAY----PSQLSGGQKQRVGIARALAN 157
Cdd:COG4619 75 -QVAYVPQE-PALWGGTVRDNLPFPFQLRE--RKFDRERALELLERLGL---PPDIldkpVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
1.47e-57 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 183.74 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFnLLWSRTVRENIafsmqiagvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPDV 161
Cdd:cd03228 77 -NIAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGK 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-240 |
8.45e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 184.19 E-value: 8.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISkvFDNGKVALTAvdnvNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQA 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-----LPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQiagvPKAKIAA----RVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLGLR----PGLKLTAeqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPI 236
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
....
gi 695703442 237 TQQF 240
Cdd:COG3840 226 LAAY 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-254 |
9.95e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 185.04 E-value: 9.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 5 SNISKVFDN-----GKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaaKGEALRQ 79
Cdd:COG4167 8 RNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE--YGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLkISMVFQHFNLlwSRTVRENIAfsmQIAGVP--------KAKIAARVAELVELVGLKgREHA--YPSQLSGGQKQRV 149
Cdd:COG4167 86 CKH-IRMIFQDPNT--SLNPRLNIG---QILEEPlrlntdltAEEREERIFATLRLVGLL-PEHAnfYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 150 GIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250 260
....*....|....*....|....*
gi 695703442 230 THPQQPITQQFVRqvSQYAEEETFN 254
Cdd:COG4167 239 ANPQHEVTKRLIE--SHFGEALTAD 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-247 |
1.96e-56 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 187.74 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQARLKIS 85
Cdd:PRK11607 24 NLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 86 MVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCD 165
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 166 EATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVRQVS 245
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
..
gi 695703442 246 QY 247
Cdd:PRK11607 255 VF 256
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
2.24e-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: 2.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqA 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RlKISMVFQHFNLLWSRTVRENIAFS----MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:COG1120 75 R-RIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFT 230
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-241 |
3.28e-56 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 183.73 E-value: 3.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLS--NISKVFDNGKV-----ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK 73
Cdd:PRK10419 1 MTLLNvsGLSHHYAHGGLsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 74 GEALRQARLKISMVFQH----FNLlwSRTVRENIAFSMQ-IAGVPKAKIAARVAELVELVGLKGrEHA--YPSQLSGGQK 146
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDsisaVNP--RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDD-SVLdkRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 147 QRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEE---G 223
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvG 237
|
250
....*....|....*...
gi 695703442 224 DVLSvFTHPQQPITQQFV 241
Cdd:PRK10419 238 DKLT-FSSPAGRVLQNAV 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
1.72e-55 |
|
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: 180.14 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQAR 81
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-----LPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-232 |
1.93e-55 |
|
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: 181.93 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNG-----KVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGE 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 76 ALRQARLKISMVFQH----FNLlwSRTVRENIAFSMQ-IAGVPKAKIAARVAELVELVGLKGrEHA--YPSQLSGGQKQR 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDspsaVNP--RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRS-EDAdkLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 149 VGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV--L 226
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVaqL 238
|
....*.
gi 695703442 227 SVFTHP 232
Cdd:TIGR02769 239 LSFKHP 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-242 |
5.01e-55 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 180.55 E-value: 5.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS----------AAKGEALRQARLKISMVFQHFNL 93
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 LWSRTVRENIAFS-MQIAGVPKAKIAARVAELVELVGLKGREHA-YPSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:PRK10619 104 WSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 172 DPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVR 242
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
5.52e-55 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 187.16 E-value: 5.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEALrq 79
Cdd:COG3845 5 ALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 aRLKISMVFQHFNLLWSRTVRENIAFSMQIAG---VPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:COG3845 79 -ALGIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQildlLLDINRRF---NLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADE----LFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-244 |
5.63e-55 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 184.47 E-value: 5.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLK-ISMVFQHFNLLWSRT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVRQV 244
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-241 |
1.54e-54 |
|
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: 178.30 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalrqaR 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-----KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
2.44e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 186.91 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVL---KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFnLLWSRTVRENIAFsmqiaGVPKA-----KIAARVAELVE-----------LVGLKGrehaypSQLSGGQ 145
Cdd:COG1132 415 -QIGVVPQDT-FLFSGTIRENIRY-----GRPDAtdeevEEAAKAAQAHEfiealpdgydtVVGERG------VNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-234 |
1.57e-53 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 177.13 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQARLKISMVFQH-FNLLWSRT 98
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---ETVWDVRRQVGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-246 |
2.15e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 177.13 E-value: 2.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEA-LRQARLKISMVFQhF--NLLWS 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKkLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAFSMQIAGVPKAKIAARVAELVELVGL--KGREHAyPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpeELLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 175 TTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ--------PITQQFVRQVSQ 246
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEleaigldlPETVKFKRALEE 259
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
4.11e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 178.99 E-value: 4.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEAlRQar 81
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:PRK09452 88 --VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-232 |
4.59e-53 |
|
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: 178.37 E-value: 4.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNG---QDisAAKGEALRQARLKISMVFQHFNLLWSRTV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD--SARGIFLPPHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAgvPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQI 179
Cdd:COG4148 95 RGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 180 LDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
9.02e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 175.18 E-value: 9.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQA 80
Cdd:PRK13632 7 MIKVENVSFSYPNSE--NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFT 230
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
9.87e-53 |
|
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: 172.76 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvaltAVDNVNLTIAQGqIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAaKGEALRQar 81
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03264 73 -RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
2.89e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 181.11 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:COG4988 337 IELEDVSFSYPGGRPAL---DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFsmqiaGVPKAKiAARVAELVELVGLKGREHAYP-----------SQLSGGQKQRVG 150
Cdd:COG4988 412 -QIAWVPQN-PYLFAGTIRENLRL-----GRPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRkICDRVAVMENGKVVEEGD 224
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-220 |
3.17e-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: 171.56 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsaakgealRQARLKISMVFQHFNLLWSR- 97
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 -TVRENIAF----SMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:cd03235 85 iSVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695703442 173 PQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMeNGKVV 220
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
1.51e-51 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 167.82 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHFNLLWSRTVR 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK---EIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 101 ENIAFSMQIAGVPKAKIAARVAELVELVGLKGREH----AYPSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-232 |
2.16e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 173.75 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgEALRQAR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:PRK11432 79 -DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-224 |
3.33e-50 |
|
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: 166.84 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 17 ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalRQARLKISMVFQHFNLLWS 96
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAfsMQIAGVPKAKIAARVAELVELV-GLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:cd03224 90 LTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695703442 176 TDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:cd03224 168 VEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
4.92e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 167.95 E-value: 4.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQA 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEAL---KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHF-NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-238 |
8.88e-50 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 169.12 E-value: 8.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 17 ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKISMVFQhfNLLWS 96
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ--DPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 ----RTVRENIAFSMQI--AGVPKAKIAARVAELVELVGLK----GRehaYPSQLSGGQKQRVGIARALANNPDVLLCDE 166
Cdd:PRK15079 111 lnprMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpnliNR---YPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 167 ATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQ 238
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-223 |
1.07e-49 |
|
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: 165.16 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDI-SAAKGEALRQARLKISMVFQHFNLLWSRTVRENIAFSMQI 109
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 110 AGVPKAKIaaRVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRR 189
Cdd:cd03297 103 KRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 695703442 190 FNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-225 |
1.12e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 172.90 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS-AAKGEALrq 79
Cdd:COG1129 4 LLEMRGISKSF--GGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 aRLKISMVFQHFNLLWSRTVRENIAFSMQIAG---VPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:COG1129 78 -AAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-223 |
2.10e-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: 163.38 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQhfnllwsrt 98
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR---KIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 vreniafsmqiagvpkakiaarVAELVELVGLKGREHaypSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:cd03214 81 ----------------------ALELLGLAHLADRPF---NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-250 |
3.68e-49 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 167.95 E-value: 3.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgealrQAR 81
Cdd:PRK10851 3 IEIANIKKSFGRTQV----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL------HAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 -LKISMVFQHFNLLWSRTVRENIAFSMQIagVPK------AKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARA 154
Cdd:PRK10851 73 dRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
250
....*....|....*.
gi 695703442 235 PITQQFVRQVSQYAEE 250
Cdd:PRK10851 231 RFVLEFMGEVNRLQGT 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-267 |
3.71e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 166.03 E-value: 3.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGK--VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgEALR 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 QARLKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGL-KGREHAyPSQLSGGQKQRVGIARALA 156
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMyEYRRHA-PHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFthPQQPI 236
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEM 237
|
250 260 270
....*....|....*....|....*....|...
gi 695703442 237 TQQFVRQVSQYaeeetfnTELANDL--EGTVIR 267
Cdd:PRK13633 238 MKKIGLDVPQV-------TELAYELkkEGVDIP 263
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
3.92e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 166.44 E-value: 3.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgealrqA 80
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-------D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKI-----------SMvfqhfnllwsrTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRV 149
Cdd:COG4152 70 RRRIgylpeerglypKM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 150 GIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-218 |
5.37e-49 |
|
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: 161.26 E-value: 5.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlK 83
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQhfnllwsrtvreniafsmqiagvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPDVLL 163
Cdd:cd00267 75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 164 CDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
1.89e-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: 162.64 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqarlkisMVFQHFNLLWSRTVR 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMQ--IAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSV-FTHPQQ 234
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
3.79e-48 |
|
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: 160.85 E-value: 3.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQ-- 79
Cdd:cd03268 1 LKTNDLTKTYGKKRV----LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRig 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQHfnllwsRTVRENIAFSMQIAGVPKakiaARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:cd03268 76 ALIEAPGFYPN------LTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-222 |
6.94e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 161.14 E-value: 6.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 5 SNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDI----SAAKGEaLRQA 80
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAE-LRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLkiSMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK11629 88 KL--GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKIcDRVAVMENGKVVEE 222
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
9.57e-48 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.41 E-value: 9.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDnGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEAlrqa 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPAL---EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlkiSMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK11248 73 ----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEM 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
1.22e-47 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 160.23 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealRQA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP----AEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-222 |
2.44e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 159.27 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDnvnLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVT---FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINrRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEE 222
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-223 |
4.02e-47 |
|
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: 158.43 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 26 LTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealrQARLKISMVFQHFNLLWSRTVRENIAF 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 106 SMqiagVPKAKIAA----RVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILD 181
Cdd:cd03298 94 GL----SPGLKLTAedrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695703442 182 LLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.19e-46 |
|
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: 166.09 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:COG4987 334 LELEDVSFRYPGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHfNLLWSRTVRENIAFsmqiaGVPKAKiAARVAELVELVGLKGREHAYP-----------SQLSGGQKQRVG 150
Cdd:COG4987 411 --IAVVPQR-PHLFDTTLRENLRL-----ARPDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGD 224
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGT 552
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-244 |
2.57e-46 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 166.18 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 8 SKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKISMV 87
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 88 FQ--HFNLLWSRTVRENIAFSMQIAGVPKAKIAA-RVAELVELVGLKgREHA--YPSQLSGGQKQRVGIARALANNPDVL 162
Cdd:PRK10261 407 FQdpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLL-PEHAwrYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVR 242
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
..
gi 695703442 243 QV 244
Cdd:PRK10261 566 AV 567
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
6.21e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 156.61 E-value: 6.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-----EKPSTGSVTVNGQDISAAKGEA 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEV----LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRQarlKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAK--IAARVAELVELVGL----KGREHAYPSQLSGGQKQRVG 150
Cdd:PRK14247 80 LRR---RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkeLQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFT 230
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 695703442 231 HPQQPITQQFV 241
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-229 |
7.07e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 157.63 E-value: 7.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGK-VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISA-AKGEALRQ 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQhF--NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGL-KGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK13646 83 VRKRIGMVFQ-FpeSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-223 |
1.29e-45 |
|
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: 155.47 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVL---KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHfNLLWSRTVRENIAFSMQIAG---VPKAKIAARVAELVE--------LVGLKGrehaypSQLSGGQKQRVG 150
Cdd:cd03253 77 --IGVVPQD-TVLFNDTIGYNIRYGRPDATdeeVIEAAKAAQIHDKIMrfpdgydtIVGERG------LKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.37e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 157.56 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNG-KVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQD------------ 68
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 69 ------ISAAKGEALRQA---RLKISMVFQHFNL-LWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLkgrEHAY- 137
Cdd:PRK13651 83 vleklvIQKTRFKKIKKIkeiRRRVGVVFQFAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL---DESYl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 138 ---PSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVM 214
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....
gi 695703442 215 ENGKVVEEGDVLSV 228
Cdd:PRK13651 239 KDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
1.55e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 156.43 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQA 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGL---KGREhayPSQLSGGQKQRVGIARALA 156
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMqdfKERE---PARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVrKICDRVAVMENGKV 219
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-224 |
3.01e-45 |
|
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: 154.62 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIsaaKGEALRQARLKISMVFQHfNLLWSRTVRE 101
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRSQIGLVSQE-PVLFDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 102 NIAFSMQIAGVPKAKIAARVAELVE-----------LVGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATSA 170
Cdd:cd03249 96 NIRYGKPDATDEEVEEAAKKANIHDfimslpdgydtLVGERG------SQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 171 LDPQTTDQI---LDllldiNRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGD 224
Cdd:cd03249 170 LDAESEKLVqeaLD-----RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
3.09e-45 |
|
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: 151.81 E-value: 3.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS-AAKGEALRqa 80
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rLKISMVFQhfnllwsrtvreniafsmqiagvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPD 160
Cdd:cd03216 75 -AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-223 |
1.34e-44 |
|
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: 152.64 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRTV 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---QVGVVLQE-NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAGVPKAKIAARVA-------ELVE----LVGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEAT 168
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAgahdfisELPEgydtIVGEQG------AGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 169 SALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
1.45e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 153.81 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQARLKISMVFQHFN-LLWSRT 98
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRKFVGLVFQNPDdQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-224 |
1.51e-44 |
|
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: 152.44 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 17 ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqARLKISMVFQH---FNL 93
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLGIGYVPEGrriFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 LwsrTVRENIAFSMQIAGvPKAKIAARVAELVEL--VgLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:COG0410 93 L---TVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 172 DPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:COG0410 168 APLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
6.31e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 152.06 E-value: 6.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTavdNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDisAAKGEALRQA 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALE---NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLW-SRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITH---EMHVVrkicDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHnleELHDA----DRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-252 |
6.68e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 153.74 E-value: 6.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL----EKPSTGSVTVNGQDISAAKGEALRQ 79
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 -ARLKISMVFQH--FNLLWSRTVRENIAFSMQI-AGVPKAKIAARVAELVELVGL---KGREHAYPSQLSGGQKQRVGIA 152
Cdd:PRK11022 86 lVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
250 260
....*....|....*....|
gi 695703442 233 QQPITQQFVRQVSQYAEEET 252
Cdd:PRK11022 246 RHPYTQALLRALPEFAQDKA 265
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-241 |
1.08e-43 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 151.08 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 10 VFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-----EKPSTGSVTVNGQDISAAKGEALrQARLKI 84
Cdd:PRK14239 13 VYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-DLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 85 SMVFQHFNLlWSRTVRENIAFSMQIAGVpkaKIAARVAELVE--LVG------LKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK14239 89 GMVFQQPNP-FPMSIYENVVYGLRLKGI---KDKQVLDEAVEksLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFnlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPI 236
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
....*
gi 695703442 237 TQQFV 241
Cdd:PRK14239 243 TEDYI 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
1.20e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 152.70 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 5 SNISKVFDNGKV-ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTV----NGQDISAA------- 72
Cdd:PRK13631 25 KNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHelitnpy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 73 --KGEALRQARLKISMVFQHFNL-LWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKgreHAY----PSQLSGGQ 145
Cdd:PRK13631 105 skKIKNFKELRRRVSMVFQFPEYqLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD---DSYlersPFGLSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDiNRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
....*..
gi 695703442 226 LSVFTHP 232
Cdd:PRK13631 261 YEIFTDQ 267
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-281 |
1.39e-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: 153.34 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDI-SAAKGEALRQARLKISMVFQHFNLLWSRTVREN 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGVPKAKIaaRVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDL 182
Cdd:TIGR02142 96 LRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 183 LLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGdvlsvfthpqqPITQQFVRQVSQYAEEEtfntELANDLE 262
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG-----------PIAEVWASPDLPWLARE----DQGSLIE 238
|
250
....*....|....*....
gi 695703442 263 GTVIRLTFTGHSTHKPIVG 281
Cdd:TIGR02142 239 GVVAEHDQHYGLTALRLGG 257
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
1.43e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 151.54 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS-AAKGeaLRQARLKISMVFQH-FNLLWSR 97
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKG--LMKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD 177
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695703442 178 QILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
1.54e-43 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 150.23 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVF------------------DNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSV 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 63 TVNGQdISaakgeALrqarLKISMVFqHFNLlwsrTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHA----YP 138
Cdd:COG1134 84 EVNGR-VS-----AL----LELGAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQpvktYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 139 SqlsgGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:COG1134 149 S----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|...
gi 695703442 219 VVEEGDVLSVFTH 231
Cdd:COG1134 224 LVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-231 |
1.96e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 151.05 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGK-VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISA-AKGEALRQ 79
Cdd:PRK13649 3 INLQNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQhF--NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKgrEHAY---PSQLSGGQKQRVGIARA 154
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIS--ESLFeknPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTH 231
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
2.18e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 152.16 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVF-----DNG------------KVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVT 63
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGlkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 64 VNGQDISAAKGEALRQarlkISMVF-QHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKG------Reha 136
Cdd:COG4586 81 VLGYVPFKRRKEFARR----IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGElldtpvR--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 137 ypsQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMEN 216
Cdd:COG4586 154 ---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
....*....
gi 695703442 217 GKVVEEGDV 225
Cdd:COG4586 231 GRIIYDGSL 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-223 |
6.75e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 150.34 E-value: 6.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgEALRQARLKISMVFQHFNLLWSRT 98
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695703442 179 ILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK13537 177 MWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-222 |
2.40e-42 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 146.46 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 7 ISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLK-IS 85
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 86 MVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCD 165
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 166 EATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEE 222
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
2.48e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 145.70 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQa 80
Cdd:COG4133 2 MLEAENLSCRRGERLL----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlkISMVFqHFNLLWSR-TVRENIAFSMQIAGVPKAkiAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG4133 77 ---LAYLG-HADGLKPElTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-248 |
2.89e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 147.23 E-value: 2.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISkVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA 80
Cdd:PRK13548 2 MLEARNLS-VRLGGRTLL---DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RlkiSMVFQHFNLLWSRTVRENIAF---SMQIAGVPKAKIAARVAELVELVGLKGRehAYPsQLSGGQKQRVGIARALA- 156
Cdd:PRK13548 78 R---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 157 -----NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGdvlsvftH 231
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG-------T 224
|
250
....*....|....*..
gi 695703442 232 PQQPITQQFVRQVSQYA 248
Cdd:PRK13548 225 PAEVLTPETLRRVYGAD 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-223 |
3.58e-42 |
|
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: 145.50 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalrqarlK 83
Cdd:cd03269 3 VENVTKRF--GRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLL 163
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 164 CDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-220 |
6.44e-42 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 144.71 E-value: 6.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgealRQARLKISMVFQHFNL-LWSR 97
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGYVMQDVDYqLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQIAGVPKAKIAArVAELVELVGLKGRehaYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD 177
Cdd:cd03226 88 SVREELLLGLKELDAGNEQAET-VLKDLDLYALKER---HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695703442 178 QILDLLLDINRRFNlTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:cd03226 164 RVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
1.07e-41 |
|
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: 145.17 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFD-----------------NGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTV 64
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 65 NGQDISAAKGEALRQarlkISMVF-QHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSG 143
Cdd:cd03267 81 AGLVPWKRRKKFLRR----IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 144 GQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-244 |
1.26e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 145.17 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaL--- 77
Cdd:COG1137 3 TLEAENLVKSYGKRTV----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----Lpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 78 RQARLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALAN 157
Cdd:COG1137 74 KRARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTiVLITHemHVVR---KICDRVAVMENGKVVEEGDVLSVFTHPQq 234
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIG-VLITD--HNVRetlGICDRAYIISEGKVLAEGTPEEILNNPL- 228
|
250
....*....|
gi 695703442 235 pitqqfVRQV 244
Cdd:COG1137 229 ------VRKV 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
1.37e-41 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 144.68 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVL---KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVglKGREHAYPSQ-------LSGGQKQRVGIARA 154
Cdd:cd03254 78 -MIGVVLQD-TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFI--MKLPNGYDTVlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-224 |
1.52e-41 |
|
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: 144.68 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeaLRQARLKISMVFQHfNLLWSRTV 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQD-VFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAGVPKAKIAARVAELVEL-----------VGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEAT 168
Cdd:cd03251 93 AENIAYGRPGATREEVEEAARAANAHEFimelpegydtvIGERG------VKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 169 SALDPQTTDQILDLL--LDINRrfnlTIVLITHEMHVVRKIcDRVAVMENGKVVEEGD 224
Cdd:cd03251 167 SALDTESERLVQAALerLMKNR----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-255 |
2.34e-41 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 147.18 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKS----TLIRLL--NGLekpSTGSVTVNGQDISAAKGEALRQARL-KISMVFQ-- 89
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGR---IGGSATFNGREILNLPEKELNKLRAeQISMIFQdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 90 --HFNLlWSRTVRENIAFSMQIAGVPKAKI---AARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLC 164
Cdd:PRK09473 107 mtSLNP-YMRVGEQLMEVLMLHKGMSKAEAfeeSVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 165 DEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVRQV 244
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
250
....*....|..
gi 695703442 245 SQY-AEEETFNT 255
Cdd:PRK09473 266 PRLdAEGESLLT 277
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-220 |
2.56e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 152.57 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLK 83
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 -ISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVL 162
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVRKiCDRVAVMENGKVV 220
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-265 |
4.07e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 146.20 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 13 NGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTgSVTV-----NGQDISAAKGEALRQ-ARLKISM 86
Cdd:COG4170 17 QGRV--KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVTAdrfrwNGIDLLKLSPRERRKiIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 87 VFQHFN--LLWSRTVRENIAFSM---QIAG----VPKAKIaARVAELVELVGLKGREH---AYPSQLSGGQKQRVGIARA 154
Cdd:COG4170 94 IFQEPSscLDPSAKIGDQLIEAIpswTFKGkwwqRFKWRK-KRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHH 252
|
250 260 270
....*....|....*....|....*....|.
gi 695703442 235 PITQQFVRQVSQYAEEETFNTELaNDLEGTV 265
Cdd:COG4170 253 PYTKALLRSMPDFRQPLPHKSRL-NTLPGSI 282
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-239 |
4.25e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 150.63 E-value: 4.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKST----LIRLLNglekpSTGSVTVNGQDISAAKGEALRQARLKISMVFQHFN-L 93
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 LWSR-TVRENIAFSMQI--AGVPKAKIAARVAELVELVGLK-GREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PRK15134 375 LNPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 170 ALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQ 239
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
6.41e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 144.12 E-value: 6.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdNGKVALTaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQa 80
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13648 84 --HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-239 |
6.79e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 149.86 E-value: 6.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKS----TLIRLLnglekPS------TGSVTVNGQDISAAKGE 75
Cdd:PRK15134 10 NLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 76 ALRQAR-LKISMVFQH----FNLLwsRTVRENIAFSMQI-AGVPKAKIAARVAELVELVGL---KGREHAYPSQLSGGQK 146
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmvsLNPL--HTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 147 QRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVL 226
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250
....*....|...
gi 695703442 227 SVFTHPQQPITQQ 239
Cdd:PRK15134 243 TLFSAPTHPYTQK 255
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-231 |
7.83e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 144.38 E-value: 7.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGK-VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAA--KGEALR 78
Cdd:PRK13645 7 IILDNVSYTYAKKTpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 QARLKISMVFQHFNL-LWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKgREHA--YPSQLSGGQKQRVGIARAL 155
Cdd:PRK13645 87 RLRKEIGLVFQFPEYqLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP-EDYVkrSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTH 231
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
9.97e-41 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 142.91 E-value: 9.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqA 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVV----LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RlKISMVFQ--HFNllwSR-TVRENIAF-----SmqiAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIA 152
Cdd:COG4604 75 K-RLAILRQenHIN---SRlTVRELVAFgrfpyS---KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFT 230
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
1.06e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 143.30 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKV-ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeALRQ 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP--EYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLkISMVFQH------FNLlwsrTVRENIAFSMQ-------IAGVPKAKIA---ARVAELvELvGLKGREHAYPSQLSG 143
Cdd:COG1101 79 AKY-IGRVFQDpmmgtaPSM----TIEENLALAYRrgkrrglRRGLTKKRRElfrELLATL-GL-GLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 144 GQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
1.47e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 142.67 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-----EKPSTGSVTVNGQDISAAKGEALRqARLKISMVFQHFNLLW 95
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SRTVRENIAFSMQIAGVPKAKI--------AARVAELVELVglKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSKKeldervewALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 168 TSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-244 |
1.51e-40 |
|
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: 141.91 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaaKGEALRQAR 81
Cdd:cd03218 1 LRAENLSKRYGKRKV----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTiVLIT-HEMHVVRKICDRVAVMENGKVVEEGDvlsvfthPQQPITQQF 240
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGT-------PEEIAANEL 225
|
....
gi 695703442 241 VRQV 244
Cdd:cd03218 226 VRKV 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
2.19e-40 |
|
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: 141.19 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVAltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYP-----SQLSGGQKQRVGIARALA 156
Cdd:cd03245 79 -NIGYVPQD-VTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQigergRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLldinRRF--NLTIVLITHEMHVVrKICDRVAVMENGKVVEEG 223
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
3.71e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 144.20 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealRQAR 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAV----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----RLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-244 |
2.05e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.87 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISkVFDNGKvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqA 80
Cdd:COG4559 1 MLEAENLS-VRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVfQHFNLLWSRTVRENIAF---SMQIAGVPKAKIAARVAELVELVGLKGRehAYPsQLSGGQKQRVGIARALA- 156
Cdd:COG4559 75 RRRAVLP-QHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGR--SYQ-TLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 157 ------NNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGdvlsvft 230
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG------- 222
|
250
....*....|....
gi 695703442 231 HPQQPITQQFVRQV 244
Cdd:COG4559 223 TPEEVLTDELLERV 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-263 |
2.24e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 140.73 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALT-AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKG-EALRQ 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQhF--NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGR--EHAyPSQLSGGQKQRVGIARAL 155
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKS-PFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ-- 233
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwl 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695703442 234 ------QPITQQFVRQVS----QYAEE----ETFNTELANDLEG 263
Cdd:PRK13641 240 kkhyldEPATSRFASKLEkggfKFSEMpltiDELVDGIKNNLKG 283
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-233 |
2.66e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 140.32 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKP---STGSVTVNGQDISAakgEALRQARLKISMVFQH-FNLLW 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTA---KTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 176 TDQILDLLLDINRRFNLTIVLITHEMHVVrKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-261 |
2.73e-39 |
|
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: 145.33 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDnGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLE--KPSTGSVTVN-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVL---KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 66 --GQDISAAKG-------------EALRQA-RLKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELV 128
Cdd:TIGR03269 77 kvGEPCPVCGGtlepeevdfwnlsDKLRRRiRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 129 GLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 209 DRVAVMENGKVVEEGDVLSVfthpqqpiTQQFVRQVSQYAEEETFntELANDL 261
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEV--EVGEPI 279
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-233 |
5.00e-39 |
|
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: 145.73 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQH---FNllwsRT 98
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---IGIVPQDtvlFN----DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMqiAGVPKAKI--AARVAELVELV--------------GLKgrehaypsqLSGGQKQRVGIARALANNPDVL 162
Cdd:COG5265 448 IAYNIAYGR--PDASEEEVeaAARAAQIHDFIeslpdgydtrvgerGLK---------LSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGdvlsvfTHPQ 233
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG------THAE 578
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-223 |
5.35e-39 |
|
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: 146.25 E-value: 5.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISkvF---DNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALR 78
Cdd:TIGR03797 452 IEVDRVT--FryrPDGPLIL---DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 QarlKISMVFQHFNLLwSRTVRENIAFSMQIaGVPKAKIAARVAELVELV-----GLkgreHAYPSQ----LSGGQKQRV 149
Cdd:TIGR03797 527 R---QLGVVLQNGRLM-SGSIFENIAGGAPL-TLDEAWEAARMAGLAEDIrampmGM----HTVISEgggtLSGGQRQRL 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 150 GIARALANNPDVLLCDEATSALDPQTTDQILDLLldinRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-219 |
1.02e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.89 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTvngqdisaAKGEALRQAR 81
Cdd:PRK11247 13 LLLNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMqiagvpKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-232 |
2.17e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.59 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgeaLRQA 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE-----LEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAE---LVELVGLKGREhayPSQLSGGQKQRVGIARALAN 157
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMeNGKVVEE-GDVLSVFTHP 232
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM-NGGVAEQiGTPVEVYEKP 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-228 |
3.10e-38 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 142.63 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVF---DNGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVN-GQD-ISAAKGE 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVV--KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 76 ALRQARLK--ISMVFQHFNLLWSRTVRENI--AFSMQIA---GVPKAKIAARVAELVELvglKGRE--HAYPSQLSGGQK 146
Cdd:TIGR03269 357 PDGRGRAKryIGILHQEYDLYPHRTVLDNLteAIGLELPdelARMKAVITLKMVGFDEE---KAEEilDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 147 QRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVL 226
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 695703442 227 SV 228
Cdd:TIGR03269 514 EI 515
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
8.69e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 135.93 E-value: 8.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-----EKPSTGSVTVNGQDISAAKGEa 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRQARLKISMVFQHFNLlWSRTVRENIAFSMQIAG-VPKAKI------AARVAELVELVglKGREHAYPSQLSGGQKQRV 149
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNL-FPMSVYDNVAYGVKIVGwRPKLEIddivesALKDADLWDEI--KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 150 GIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMEN-----GKVVEEGD 224
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
250
....*....|....*..
gi 695703442 225 VLSVFTHPQQPITQQFV 241
Cdd:PRK14258 240 TKKIFNSPHDSRTREYV 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-241 |
1.07e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 135.66 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKISMVFQHFNLLWSRTVRE 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 102 NIAFSM-QIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQIL 180
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 181 DLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPqQPITQQFV 241
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFL 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
1.68e-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: 132.34 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHFNLLwSRTVRENIafsmqiagvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPDV 161
Cdd:cd03246 77 -HVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRkICDRVAVMENGKV 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
2.50e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.86 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQARLKISMVFQH-FNLLWSRT 98
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVRSKVGLVFQDpDDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695703442 179 ILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:PRK13647 177 LMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-223 |
3.32e-37 |
|
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: 133.04 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgealrqarLK 83
Cdd:cd03220 23 LGILGRKGEVGEF--WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL----------LG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHfnllwSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLL 163
Cdd:cd03220 91 LGGGFNP-----ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 164 CDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-223 |
4.73e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 141.01 E-value: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRTVREN 102
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR---QVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGVPKAKIAARVAELVELVGlkGREHAYP-------SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPqt 175
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA-- 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695703442 176 tdQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:TIGR00958 651 --ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-241 |
1.07e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 132.52 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKP----STGSVTVNGQDISAAkgeALRQarLKISMVFQH----FN 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC---ALRG--RKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 93 LLwsRTVRENIAFSMQIAGVPKAkiAARVAELVELVGLKGRE---HAYPSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PRK10418 94 PL--HTMHTHARETCLALGKPAD--DATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 170 ALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-224 |
1.56e-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: 131.49 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEalRQARLKISMVFQH---FNLLw 95
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAYVPQGreiFPRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 srTVRENIAFSMQIAGVPKAKIAARVAELV----ELVGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:TIGR03410 91 --TVEENLLTGLAALPRRSRKIPDEIYELFpvlkEMLGRRG------GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 172 DPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
2.24e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 131.24 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTavdnvnLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealrQA 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFD------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQiagvPKAKIAA----RVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALA 156
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNIGLGLN----PGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 157 NNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-223 |
2.56e-36 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 138.17 E-value: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:PRK13657 335 VEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHfNLLWSRTVRENIAFSMQIAG---VPKAKIAARVAELVE--------LVGLKGRehaypsQLSGGQKQRVG 150
Cdd:PRK13657 411 --IAVVFQD-AGLFNRSIEDNIRVGRPDATdeeMRAAAERAQAHDFIErkpdgydtVVGERGR------QLSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDInrRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.09e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 135.49 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQar 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPAL---RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lKISMVFQHfNLLWSRTVRENIAFsmqiaGVPKAKiAARVAELVELVGLKGREHAYP-----------SQLSGGQKQRVG 150
Cdd:TIGR02857 397 -QIAWVPQH-PFLFAGTIAENIRL-----ARPDAS-DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 151 IARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVM 214
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-229 |
1.23e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 130.60 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAakgEALRQARLKISMVFQH-FNLLWSRTV 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAGVPKAKIAARVAEL---VELVGLKGREhayPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTT 176
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEAllaVNMLDFKTRE---PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 177 DQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-219 |
3.10e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 136.02 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealRQARLKISMVFQHFNLLWSRT 98
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----IATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695703442 179 ILDLLLDINRRFNLTIVLITHEMH-VVRkiCDRVAVMENGKV 219
Cdd:NF033858 436 FWRLLIELSREDGVTIFISTHFMNeAER--CDRISLMHAGRV 475
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-239 |
3.77e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.15 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTI-AQGqIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS-AAKGEALRQARLKISMVFQHFNLLWSRTVR 100
Cdd:PRK11144 16 TVNLTLpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPEKRRIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMqiagvpKAKIAARVAELVELVGLkgrEH---AYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD 177
Cdd:PRK11144 95 GNLRYGM------AKSMVAQFDKIVALLGI---EPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 178 QILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFT----HPQQPITQQ 239
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAssamRPWLPKEEQ 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-223 |
4.06e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 128.57 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqARLKISMVFQHFNLLWSR 97
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVREN--IAFSMQ-----IAGVPK--------AKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVL 162
Cdd:PRK11300 96 TVIENllVAQHQQlktglFSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-233 |
5.13e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.92 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVAltavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQ---DISAAKGEalr 78
Cdd:PRK11000 4 VTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 qarlkISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARV---AELVELVGLKGREhayPSQLSGGQKQRVGIARAL 155
Cdd:PRK11000 77 -----VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
9.79e-35 |
|
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: 126.78 E-value: 9.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFD----NGKVaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVN--GQDISAAKG 74
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 75 E-----ALRqaRLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGR-EHAYPSQLSGGQKQR 148
Cdd:COG4778 83 SpreilALR--RRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 149 VGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
1.49e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 127.21 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEK--PS---TGSVTVNGQDISAAKGEALrQARLKISMVFQHFNLl 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPV-EVRRRIGMVFQKPNP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 95 WSRTVRENIAFSMQIAGVPK-----AKIAARVAELVELVGLKGREHAypSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PRK14243 103 FPKSIYDNIAYGARINGYKGdmdelVERSLRQAALWDEVKDKLKQSG--LSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 170 ALDPQTTDQILDLLLDINRRFnlTIVLITHEMHVVRKICDRVAVM---------ENGKVVEEGDVLSVFTHPQQPITQQF 240
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDY 258
|
.
gi 695703442 241 V 241
Cdd:PRK14243 259 V 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-241 |
1.65e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 127.21 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQARlkISMVFQHFNLlwSR 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-YSYRSQR--IRMIFQDPST--SL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAfsmQIAGVP--------KAKIAARVAELVELVGLKgREHA--YPSQLSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:PRK15112 101 NPRQRIS---QILDFPlrlntdlePEQREKQIIETLRQVGLL-PDHAsyYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 168 TSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFV 241
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
1.78e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.64 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:PRK11160 339 LTLNNVSFTYPDQ--PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLwSRTVRENIAFsmqiagvpkAKIAARVAELVEL---VGLK----------------GRehaypsQLS 142
Cdd:PRK11160 416 --ISVVSQRVHLF-SATLRDNLLL---------AAPNASDEALIEVlqqVGLEklleddkglnawlgegGR------QLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 143 GGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKIcDRVAVMENGKVVEE 222
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
250
....*....|....*..
gi 695703442 223 GDvlsvftHpQQPITQQ 239
Cdd:PRK11160 555 GT------H-QELLAQQ 564
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
2.24e-34 |
|
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: 124.35 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISkvFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQAr 81
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLlWSRTVRENIafsmqiagvpkakiaarvaelvelvglkGRehaypsQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03247 77 --ISVLNQRPYL-FDTTLRNNL----------------------------GR------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKIcDRVAVMENGKVVEEG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-219 |
2.95e-34 |
|
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: 125.28 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRTVREN 102
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS---KVSLVGQE-PVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGVPKAKIAARVAE----LVEL-------VGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHahsfISELasgydteVGEKG------SQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695703442 172 DPQTTDQILDLLLDINRRfnLTIVLITHEMHVVRKiCDRVAVMENGKV 219
Cdd:cd03248 182 DAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-241 |
3.18e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 126.32 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVF--DNGKVALTavdNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKG----EALRq 79
Cdd:PRK14246 12 NISRLYlyINDKAILK---DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqiDAIK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMVFQHFNLLWSRTVRENIAFSMQIAGVP-KAKIAARVAELVELVGL----KGREHAYPSQLSGGQKQRVGIARA 154
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfnLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQ 234
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*..
gi 695703442 235 PITQQFV 241
Cdd:PRK14246 246 ELTEKYV 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-229 |
4.03e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.77 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFD-NGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqDI---SAAKGEA 76
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRQARLKISMVFQH-FNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGL-KGREHAYPSQLSGGQKQRVGIARA 154
Cdd:PRK13643 79 IKPVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-223 |
5.24e-34 |
|
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: 131.38 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeaLRQARLKISMVFQHFnLLWSRTV 99
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVSQDV-VLFNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSmQIAGVPKAKI--AARVAELVELV-----GLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:TIGR02203 423 ANNIAYG-RTEQADRAEIerALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695703442 173 PQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:TIGR02203 502 NESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-223 |
7.56e-34 |
|
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: 124.14 E-value: 7.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRTV 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS---RISIIPQD-PVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAF------SMQIAGVPKAKIAARVAELVElvGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDP 173
Cdd:cd03244 95 RSNLDPfgeysdEELWQALERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695703442 174 QTTDQILDLlldINRRF-NLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:cd03244 173 ETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
7.62e-34 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 130.29 E-value: 7.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaaKGEALRQA 80
Cdd:PRK09700 5 YISMAGIGKSF--GPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAF----SMQIAGVPK---AKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILdLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
3.70e-33 |
|
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: 123.27 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISkVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTG-SVTVNGQDISaakGEALRQ 79
Cdd:COG1119 3 LLELRNVT-VRRGGKTIL---DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG---GEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 80 ARLKISMV--FQHFNLLWSRTVRENI--AF--SMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIAR 153
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLDVVlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFT 230
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
6.72e-33 |
|
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: 120.23 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRqaRLKISMV---FQHFNLLWS 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--RAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAFsmqiagvpkakiaarvaelvelvglkgrehayPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTT 176
Cdd:cd03215 93 LSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695703442 177 DQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-249 |
8.05e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 128.43 E-value: 8.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKS----TLIRLLNG-----------LEKPSTGSVTVN 65
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQagglvqcdkmlLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 66 GQdiSAAKGEALRQArlKISMVFQH----FNLLWsrTVRENIAFSM---QIAGVPKAKIAA-RVAELVELVGLKGREHAY 137
Cdd:PRK10261 92 EQ--SAAQMRHVRGA--DMAMIFQEpmtsLNPVF--TVGEQIAESIrlhQGASREEAMVEAkRMLDQVRIPEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 138 PSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260 270
....*....|....*....|....*....|..
gi 695703442 218 KVVEEGDVLSVFTHPQQPITQQFVRQVSQYAE 249
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-235 |
9.18e-33 |
|
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: 127.56 E-value: 9.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLwSRTVRENIA-FsmqiAGVPKAKI--AARVAELVEL-----------VGLKGrehaypSQLSGGQKQ 147
Cdd:COG4618 408 --IGYLPQDVELF-DGTIAENIArF----GDADPEKVvaAAKLAGVHEMilrlpdgydtrIGEGG------ARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 148 RVGIARALANNPDVLLCDEATSALDPQtTDQILDLLLDINRRFNLTIVLITHEMHVVRkICDRVAVMENGKVVEEG---D 224
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDE-GEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGprdE 552
|
250
....*....|.
gi 695703442 225 VLSVFTHPQQP 235
Cdd:COG4618 553 VLARLARPAAA 563
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
1.68e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 121.66 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKvALTAVDnvnLTIAQGQIYGIIGYSGAGKSTLIRLLNGL---EKPSTGSVTVNGQDISAAKGEA- 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ-ALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 -LRQARLKISMVFQHFNLLWSRTVRENIAFSmQIAGVPKAKIA---------ARVAELVELVGLKGREHAYPSQLSGGQK 146
Cdd:PRK09984 80 dIRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFWRTCfswftreqkQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 147 QRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-247 |
2.58e-32 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 122.99 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTgSVTVNG---QDISAAKGEALRQARL 82
Cdd:PRK15093 8 NLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNW-RVTADRmrfDDIDLLRLSPRERRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 ---KISMVFQHFNLLWSRTvrENIAFSMqIAGVP----KAKIAARVA-------ELVELVGLKGRE---HAYPSQLSGGQ 145
Cdd:PRK15093 87 vghNVSMIFQEPQSCLDPS--ERVGRQL-MQNIPgwtyKGRWWQRFGwrkrraiELLHRVGIKDHKdamRSFPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
250 260
....*....|....*....|..
gi 695703442 226 LSVFTHPQQPITQQFVRQVSQY 247
Cdd:PRK15093 244 KELVTTPHHPYTQALIRAIPDF 265
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-244 |
1.96e-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: 117.89 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDNGkvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgealRQARLKIS 85
Cdd:TIGR03740 5 NLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDLHKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 86 MVFQHFNLLWSRTVRENIAFSMQIAGVPKAkiaaRVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCD 165
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 166 EATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVlsvftHPQQPITQQFVRQV 244
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI-----NKSENLEKLFVEVV 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-223 |
5.10e-31 |
|
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: 116.60 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL--EKPST-GSVTVNGQDISAAkgealrQARLKISMVFQHFNLLWSRTV 99
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTTsGQILFNGQPRKPD------QFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAG---VPKAKIAARVAELVEL-VGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:cd03234 99 RETLTYTAILRLprkSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695703442 176 TDQILDLLLDINRRfNlTIVLITheMHVVR----KICDRVAVMENGKVVEEG 223
Cdd:cd03234 179 ALNLVSTLSQLARR-N-RIVILT--IHQPRsdlfRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-218 |
2.01e-30 |
|
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: 114.49 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIR-LLNGLEKPStGSVTVNGQdISAAKGEAlrqarlkismvfqhfnllW--SRTV 99
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLS-GSVSVPGS-IAYVSQEP------------------WiqNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIagvpkakIAARVAELVEL-----------------VGLKGrehaypSQLSGGQKQRVGIARALANNPDVL 162
Cdd:cd03250 83 RENILFGKPF-------DEERYEKVIKAcalepdleilpdgdlteIGEKG------INLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGK 218
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-223 |
3.10e-30 |
|
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: 113.80 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 12 DNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPS--TGSVTVNGQDISaakgeaLRQARLKISMVFQ 89
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD------KRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 90 HFNLLWSRTVRENIAFSmqiagvpkakiaarvAELvelvglkgrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:cd03213 90 DDILHPTLTVRETLMFA---------------AKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 170 ALDPQTTDQILDLLldinRRF---NLTIVLITH----EMHvvrKICDRVAVMENGKVVEEG 223
Cdd:cd03213 141 GLDSSSALQVMSLL----RRLadtGRTIICSIHqpssEIF---ELFDKLLLLSQGRVIYFG 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-225 |
6.07e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 6.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVngqdisaakGEalrqa 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GE----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLL-WSRTVRENIAfsmqiAGVPKAKIaARVAELVELVGLKGRE-HAYPSQLSGGQKQRVGIARALANN 158
Cdd:COG0488 377 TVKIGYFDQHQEELdPDKTVLDELR-----DGAPGGTE-QEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 159 PDVLLCDEATSALDPQTTDQILDLLLDinrrFNLTIVLITHEMHVVRKICDRVAVMENGKVVE-EGDV 225
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDRYFLDRVATRILEFEDGGVREyPGGY 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-226 |
7.20e-30 |
|
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: 120.50 E-value: 7.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDngKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQAr 81
Cdd:TIGR01257 929 VCVKNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL-DAVRQS- 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:TIGR01257 1005 --LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLdiNRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVL 226
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
9.07e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDnGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTvngqdisaakgealRQARLK 83
Cdd:COG0488 1 LENLSKSFG-GRPLL---DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------------IPKGLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWSRTVRENI---------------AFSMQIAGVPK--AKIA---------------ARVAELVELVGLK 131
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEdlERLAelqeefealggweaeARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 132 GREHAYP-SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLldinRRFNLTIVLITHEMHVVRKICDR 210
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRYFLDRVATR 218
|
....*....
gi 695703442 211 VAVMENGKV 219
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
1.15e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.81 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-EKPS----TGSVTVNGQDISAAKGeaLRQARLKISMVFQHFNL 93
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNYRD--VLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 lWSRTVRENIafsmqIAGVPKAKIAAR-------VAELVElVGL----KGREHAYPSQLSGGQKQRVGIARALANNPDVL 162
Cdd:PRK14271 113 -FPMSIMDNV-----LAGVRAHKLVPRkefrgvaQARLTE-VGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 163 LCDEATSALDPQTTDQILDLLLDINRRfnLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQQFVR 242
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
...
gi 695703442 243 QVS 245
Cdd:PRK14271 264 GLS 266
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-229 |
2.93e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 113.56 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgEALRQARLKISMVFQHFNL-LWSRTVREN 102
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQDPEQqIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDL 182
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695703442 183 LLDINRRFNlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVF 229
Cdd:PRK13638 179 IRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-224 |
7.43e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.87 E-value: 7.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 13 NGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLeKPSTGSVTVNGQDISAAkgeALRQARLKISMVFQHFN 92
Cdd:PRK11174 361 DGKTLA---GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 93 LLWSrTVRENIAFSMQIAGVPKAKIA---ARVAELVELVGLkGREHAYPSQ---LSGGQKQRVGIARALANNPDVLLCDE 166
Cdd:PRK11174 434 LPHG-TLRDNVLLGNPDASDEQLQQAlenAWVSEFLPLLPQ-GLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 167 ATSALDPQTTDQILDLLLDINRRfnLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGD 224
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGD 566
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-246 |
9.21e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.56 E-value: 9.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS----AAKGEALRQAR 81
Cdd:PRK11701 11 GLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFN----LLWSRTVRENIAFSMQIAGVPK-AKIAARVAELVELVGLK-GREHAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK11701 87 LRTEWGFVHQHprdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQP 235
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHP 246
|
250
....*....|.
gi 695703442 236 ITQQFVRQVSQ 246
Cdd:PRK11701 247 YTQLLVSSVLQ 257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
1.09e-28 |
|
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: 115.92 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQ--HfnlLWSR 97
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQdaH---LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQIAGVPKAKIAARVAELVELV-----GLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALERVGLADWLralpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*..
gi 695703442 173 PQTTDQILDLLLDINRRfnLTIVLITH 199
Cdd:TIGR02868 504 AETADELLEDLLAALSG--RTVVLITH 528
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
1.10e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdNGKVALTAVDnvnLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQa 80
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rLKISMVFQHFNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELvelvGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK15439 86 -LGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAL----GCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 161 VLLCDEATSALDPQTTD----QILDLLldinrRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK15439 161 ILILDEPTASLTPAETErlfsRIRELL-----AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-224 |
1.18e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQA--------RLKISMV-- 87
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLVpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 88 FqhfnllwsrTVRENIAFSMQIAG-------VPKAKIAARVAELVELVGLKGR-EHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:COG3845 351 M---------SVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPgPDTPARSLSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVP 485
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-222 |
1.30e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEALRQarlKISMV---FQHFNLLW 95
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRA---GIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SRTVRENIAFSMQ----IAG-VPKAKIAARVAELVELVGLK-GREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:COG1129 344 DLSIRENITLASLdrlsRGGlLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 170 ALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEE 222
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-223 |
1.77e-27 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 113.30 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQHfNLLWSRTV 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQiAGVPKAKIAaRVAELVEL--------VGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIW-AACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695703442 172 DPQTTDQILDLLLDINRRfnlTIVLITHEMHVVRKIcDRVAVMENGKVVEEG 223
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-224 |
3.26e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.57 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqARlKISMVFQHFNLLWSRTVRENI 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--AR-KVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 104 AfsmqIAGVP--------KAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:PRK10575 107 A----IGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695703442 176 TDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGD 224
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-244 |
5.57e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALrqARlKISMVFQHFNLLWSRT 98
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--AR-RLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFS----MQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK11231 93 VRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 175 TTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDvlsvfthPQQPITQQFVRQV 244
Cdd:PRK11231 173 HQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-------PEEVMTPGLLRTV 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
6.73e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.55 E-value: 6.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQa 80
Cdd:PRK09536 3 MIDVSDLSVEF--GDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 rlKISMVFQHFNLLWSRTVRENIAFSM-----QIAGVPKAKIAArVAELVELVGLKGREHAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK09536 78 --RVASVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDL---LLDINRrfnlTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHP 232
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELvrrLVDDGK----TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-233 |
7.24e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.39 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDIS-AAKGEALRQArl 82
Cdd:PRK11288 7 FDGIGKTFPGVK----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 kISMVFQHFNLLWSRTVRENI---AFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK11288 81 -VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQ 233
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQ 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
1.75e-26 |
|
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: 102.14 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaakgealrqar 81
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkismvfqhfnllwsrtvreniafsmqiagvPKAKIAarvaelvelvglkgrehaYPSQLSGGQKQRVGIARALANNPDV 161
Cdd:cd03221 61 -------------------------------STVKIG------------------YFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDinrrFNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-223 |
1.24e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.41 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHFNLlWSRTV 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN---QVALVSQNVHL-FNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQ----IAGVPKAKIAARVAELVE--------LVGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:PRK11176 434 ANNIAYARTeqysREQIEEAARMAYAMDFINkmdngldtVIGENG------VLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 168 TSALDPQTTDQILDLLLDINRrfNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
1.86e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.26 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaaKGEALRQA 80
Cdd:PRK11614 5 MLSFDKVSAHY--GKI--QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQHFNLLWSRTVRENIAFSMQIAgvPKAKIAARVAELVELVG-LKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEE--GDVL 226
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEdtGDAL 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-223 |
2.06e-25 |
|
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: 101.33 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHFNLLwSRTV 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS---SLTIIPQDPTLF-SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENI-AFSM----QIAGvpkakiAARVAElvelvglKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:cd03369 99 RSNLdPFDEysdeEIYG------ALRVSE-------GG------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695703442 175 TTDQILDLlldINRRF-NLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:cd03369 160 TDALIQKT---IREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
3.20e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.78 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDngkvALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPST--GSVTVNGQDISAAkgeALRQA-RL 82
Cdd:PRK13549 10 NITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQAS---NIRDTeRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 KISMVFQHFNLLWSRTVRENIAFSMQI--AGVPK-AKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGK 218
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-200 |
1.38e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRTVR 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQT-PTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMQIAG--VPKAKIAARVA--ELVELVGLKGREhaypsQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTT 176
Cdd:PRK10247 99 DNLIFPWQIRNqqPDPAIFLDDLErfALPDTILTKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....
gi 695703442 177 DQILDLLLDINRRFNLTIVLITHE 200
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-230 |
2.14e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 97.65 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKvalTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgEALRQAR 81
Cdd:PRK15056 7 IVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLWSRTVR-ENIAF-----SMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARAL 155
Cdd:PRK15056 80 --VAYVPQSEEVDWSFPVLvEDVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDrVAVMENGKVVEEGDVLSVFT 230
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-257 |
2.65e-23 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 97.19 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGqDISAAKGEALRQARLkismvfqhfnllwsrTV 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQL---------------TG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQI 179
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 180 LDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHPQQPITQqfVRQVSQyAEEETFNTEL 257
Cdd:PRK13546 183 LDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLND--FKKKSK-AEQKEFRNKL 256
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-207 |
2.76e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 95.26 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkGEALRQarlkismvfqhfNLLW------ 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQ------------DLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 ---SRTVRENIAFSMQIAGVPKAkiaARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:PRK13538 85 iktELTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695703442 173 PQTTDQILDLLLDINRRfNLTIVLITH-EMHV----VRKI 207
Cdd:PRK13538 162 KQGVARLEALLAQHAEQ-GGMVILTTHqDLPVasdkVRKL 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-225 |
4.47e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 99.69 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlK 83
Cdd:PRK10762 7 LKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWSRTVRENI----AFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNP 159
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREV 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-245 |
6.90e-23 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 99.13 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNgkvaLTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPST--GSVTVNGQDISAakgEALR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA---SNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 79 QARLK-ISMVFQHFNLLWSRTVRENIAFSMQI----AGVPKAKIAARVAELVELVGLKGREHAYP-SQLSGGQKQRVGIA 152
Cdd:TIGR02633 74 DTERAgIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFThp 232
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE-- 230
|
250
....*....|...
gi 695703442 233 QQPITQQFVRQVS 245
Cdd:TIGR02633 231 DDIITMMVGREIT 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
1.95e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEkPSTGSVTVNGQDISAAKGEALRQARlkiSMVFQHFNLLWSRTVR 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMQiAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARAL-----ANNPD--VLLCDEATSALD- 172
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDv 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 173 -PQTTdqiLDLLLdinRRF---NLTIVLITHEM-HVVRKiCDRVAVMENGKVVEEGDVLSVFT 230
Cdd:COG4138 167 aQQAA---LDRLL---RELcqqGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-220 |
5.11e-22 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 96.34 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDI--SAAKgEALRQAr 81
Cdd:PRK10982 1 MSNISKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSK-EALENG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLWSRTVRENI---AFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANN 158
Cdd:PRK10982 75 --ISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 159 PDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-233 |
7.41e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.87 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqdisaakgeaLRQA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQ--HFNLLWSRTVREniaFSMQIAGVPKAKIA---ARV--AELVElvglkgrehaYPSQ-LSGGQKQRVGIA 152
Cdd:PRK09544 66 KLRIGYVPQklYLDTTLPLTVNR---FLRLRPGTKKEDILpalKRVqaGHLID----------APMQkLSGGETQRVLLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 153 RALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMeNGKVVEEGDVLSVFTHP 232
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
.
gi 695703442 233 Q 233
Cdd:PRK09544 212 E 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-223 |
2.07e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEAlrQAR 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHFNLLWSRTVRENIAFSMQI-AGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPD 160
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 VLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-224 |
3.75e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.39 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRqARLKismVFQHFNLLWSRT 98
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR-SRLA---VVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVE-----------LVGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLASVHDdilrlpqgydtEVGERG------VMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 168 TSALDPQTTDQILDLLldinRRF--NLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGD 224
Cdd:PRK10789 479 LSAVDGRTEHQILHNL----RQWgeGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-199 |
4.17e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEAL-----RQArLKISMvfqhfnllws 96
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEAChylghRNA-MKPAL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 rTVRENIAFSMQIAGVPKAKIAArVAELVELVGLKGREHAYpsqLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTT 176
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAA-ALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|...
gi 695703442 177 DQILDLLLDiNRRFNLTIVLITH 199
Cdd:PRK13539 164 ALFAELIRA-HLAQGGIVIAATH 185
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-279 |
5.63e-21 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 93.80 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQARLKIsmvfqhfnllwsrtv 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 rENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQI 179
Cdd:PRK13545 104 -ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 180 LDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSVFTHpqqpiTQQFVRQVSQYAEEE--TFNTEL 257
Cdd:PRK13545 183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKYNQMSVEErkDFREEQ 256
|
250 260
....*....|....*....|..
gi 695703442 258 ANDLEGTVIRLTFTGHSTHKPI 279
Cdd:PRK13545 257 ISQFQHGLLQEDQTGRERKRKK 278
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
8.79e-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: 88.35 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLE--KPSTGSVTVNGQDISAAKGEalRQARLKISMVFQHfnllwsrt 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE--ERARLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 vreniafSMQIAGVpkakiaaRVAELVELVGLKgrehaypsqLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:cd03217 86 -------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695703442 179 ILDLLLDInRRFNLTIVLITHEMHVVRKI-CDRVAVMENGKVVEEGDV 225
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-183 |
1.23e-20 |
|
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: 88.18 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 17 ALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlkiSMVFQHFNLLWS 96
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-----ILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 R-TVRENIAFSMQIAGVPKAKIAarvaELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
....*...
gi 695703442 176 TDQILDLL 183
Cdd:TIGR01189 163 VALLAGLL 170
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-222 |
1.25e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.86 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 16 VALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEK--PSTGSVTVNGQDISAakgealrqarlkismvfqhfnl 93
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR---------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 lwSRTVRENIAfsmqIAGVPKAKIaarvaELVELVGLKgreHAY-----PSQLSGGQKQRVGIARALANNPDVLLCDEAT 168
Cdd:COG2401 99 --EASLIDAIG----RKGDFKDAV-----ELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 169 SALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKIC-DRVAVMENGKVVEE 222
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-221 |
1.60e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.16 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 6 NISKVFDNGKvaltAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPST--GSVTVNGQ-----DI--SAAKGea 76
Cdd:NF040905 6 GITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIrdSEALG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 lrqarlkISMVFQHFNLLWSRTVRENIAFSMQIA--GVPK-AKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIAR 153
Cdd:NF040905 80 -------IVIIHQELALIPYLSIAENIFLGNERAkrGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 154 ALANNPDVLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVE 221
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
1.83e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaAKGEAL---RQARLKISmvfqhfnllwsr 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP------AGARVLflpQRPYLPLG------------ 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQIAGVPKAKIAArVAELVELVGLKGR---EHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:COG4178 441 TLREALLYPATAEAFSDAELRE-ALEAVGLGHLAERldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....*
gi 695703442 175 TTDQILDLLLDinRRFNLTIVLITH 199
Cdd:COG4178 520 NEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-222 |
1.84e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.99 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEALRQARLKISMVFQHFNLLWSRTV 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIA------FSMQIAGVPKAKIAARVAELVELVGLKGrehayPSQ------LSGGQKQRVGIARALANNPDVLLCDEA 167
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 168 TSALDPQTTDQILDLlldINrRFN---LTIVLITHEMHVVRKICDRVAVMENGKVVEE 222
Cdd:PRK10762 423 TRGVDVGAKKEIYQL---IN-QFKaegLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-244 |
2.17e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISA-AKGEALRqarlKISMVFQHFNLLWSR 97
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVAR----RIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMqiagVPKAKIAAR--------VAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PRK10253 97 TVQELVARGR----YPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 170 ALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGdvlsvftHPQQPITQQFVRQV 244
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERI 240
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-183 |
2.21e-20 |
|
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: 87.55 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEaLRQARLKISmvfqHFNLLWSR-TVREN 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLG----HAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGvpkakiAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDL 182
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
.
gi 695703442 183 L 183
Cdd:cd03231 168 M 168
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-223 |
3.14e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.72 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFdnGKValTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgeALRQAR 81
Cdd:NF033858 2 ARLEGVSHRY--GKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR--HRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQHF--NLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLkgreHAYPS----QLSGGQKQRVGIARAL 155
Cdd:NF033858 76 PRIAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 156 ANNPDVLLCDEATSALDPQTTDQILDLLLDI-NRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATG 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-223 |
4.16e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 31 GQIYGIIGYSGAGKSTLI-----RLLNGLEKpsTGSVTVNGQDISAakgealRQARLKISMVFQHFNLLWSRTVRENIAF 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDA------KEMRAISAYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 106 S----MQiAGVPKAKIAARVAELVELVGLKGREH---AYPSQ---LSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:TIGR00955 123 QahlrMP-RRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695703442 176 TDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEG 223
Cdd:TIGR00955 202 AYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-221 |
4.65e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.80 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQHFNLlwsrtv 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL---FSAVFTDFHL------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 reniaFSMQIAGVPKAKIAARVAELVELVGLKGR---EHAYPS--QLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK10522 409 -----FDQLLGPEGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695703442 175 TTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVE 221
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-230 |
8.72e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.57 E-value: 8.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNG-LEKPS-------TGSVTVNGQDISAAkgEALRQARLKISMvfqhfn 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAI--DAPRLARLRAVL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 93 llwSRTVRENIAFSMQ----IAGVPKAK-----------IAARVAELVELVGLKGREhayPSQLSGGQKQRVGIARALAN 157
Cdd:PRK13547 89 ---PQAAQPAFAFSAReivlLGRYPHARragalthrdgeIAWQALALAGATALVGRD---VTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 158 ---------NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSV 228
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
..
gi 695703442 229 FT 230
Cdd:PRK13547 243 LT 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-212 |
1.20e-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: 89.61 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDnGKVAltaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVngqdisaakGEAlrqar 81
Cdd:TIGR03719 323 IEAENLTKAFG-DKLL---IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GET----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQ-HFNLLWSRTVRENIAFSMQIAGVPKAKIAARVaeLVELVGLKGREHAYP-SQLSGGQKQRVGIARALANNP 159
Cdd:TIGR03719 385 VKLAYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDinrrFNLTIVLITHEmhvvRKICDRVA 212
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHD----RWFLDRIA 507
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-233 |
1.79e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALTavdNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQAr 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQ---NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkISMVFQHFNLLwSRTVRENIAFSMQI--AGVPKAKIAARVAELVELV--GLKGREHAYPSQLSGGQKQRVGIARALAN 157
Cdd:PRK10790 417 --VAMVQQDPVVL-ADTFLANVTLGRDIseEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDInrRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGdvlsvfTHPQ 233
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG------THQQ 560
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-221 |
4.22e-19 |
|
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: 87.93 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQarlKISMVFQHFNLlwsrtvreni 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ---LFSAVFSDFHL---------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 104 aFSmQIAGVPKAKIAARVAELVELVGLKG----REHAYPS-QLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD- 177
Cdd:COG4615 418 -FD-RLLGLDGEADPARARELLERLELDHkvsvEDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRv 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695703442 178 ---QILDLLldinRRFNLTIVLITHE---MHVvrkiCDRVAVMENGKVVE 221
Cdd:COG4615 496 fytELLPEL----KARGKTVIAISHDdryFDL----ADRVLKMDYGKLVE 537
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
262-337 |
7.62e-19 |
|
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: 79.48 E-value: 7.62e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 262 EGTVIRLTFTGHSTHKPIVGELTLRYGLPFNILHGKMTQTAHGVFGQLWVHVAASDEQLNNILADLQHSDIEGEVI 337
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-228 |
1.21e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEAL----------RQA---------RL 82
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLarglvylpedRQSsglyldaplAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 KISMVFQHFNLLWSRTVRENiafsmqiagvpkakiaARVAELVELVGLKGREHAYPSQ-LSGGQKQRVGIARALANNPDV 161
Cdd:PRK15439 361 NVCALTHNRRGFWIKPAREN----------------AVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 162 LLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEE--GDVLSV 228
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGAltGAAINV 492
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-223 |
1.59e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.76 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgeALRQARLKISMVFQHfNLLWSRTVRENI 103
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQFSMIPQD-PVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 104 AFSMQIAgvpkakiAARVAELVELVGLKGREHAYP-----------SQLSGGQKQRVGIARA-LANNPDVLLCDEATSAL 171
Cdd:PTZ00243 1405 DPFLEAS-------SAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILMDEATANI 1477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 172 DPQTTDQILDLLLDInrrF-NLTIVLITHEMHVVRKiCDRVAVMENGKVVEEG 223
Cdd:PTZ00243 1478 DPALDRQIQATVMSA---FsAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-217 |
1.60e-18 |
|
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: 86.99 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNgkVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEAlrQARLK 83
Cdd:TIGR01257 1940 LNELTKVYSG--TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--HQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWsrTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLL 163
Cdd:TIGR01257 2016 YCPQFDAIDDLL--TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695703442 164 CDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENG 217
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-216 |
3.14e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVAltaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqdisaakgealrqar 81
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 lkismvfqhfnllwSRTVRENIAFSMQIAGVPkakiaarVAELVELVglkgrehAYPSQ--LSGGQKQRVGIARALANNP 159
Cdd:cd03223 59 --------------GMPEGEDLLFLPQRPYLP-------LGTLREQL-------IYPWDdvLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLldinRRFNLTIVLITHEmHVVRKICDRVAVMEN 216
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-212 |
3.35e-18 |
|
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: 85.37 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 4 LSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTgsvtvngqdisaakGEALRQARLK 83
Cdd:TIGR03719 7 MNRVSKVVPPKKEIL---KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFN--------------GEARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 84 ISMVFQHFNLLWSRTVRENI---------------AFSMQIAGvPKA---KIAARVAELVELVGLKGrEHAYPSQ----- 140
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVeegvaeikdaldrfnEISAKYAE-PDAdfdKLAAEQAELQEIIDAAD-AWDLDSQleiam 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 141 --------------LSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLldinRRFNLTIVLITHEmhvvRK 206
Cdd:TIGR03719 148 dalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD----RY 219
|
....*.
gi 695703442 207 ICDRVA 212
Cdd:TIGR03719 220 FLDNVA 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-228 |
3.59e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.29 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDN----VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLeKPSTGSVTVNGQDISAAKGEAL--------RQARLKISM- 86
Cdd:PRK03695 7 AVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELarhraylsQQQTPPFAMp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 87 VFQHFNLlwsrtvreniafsMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARAL-----ANNPD- 160
Cdd:PRK03695 86 VFQYLTL-------------HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 161 -VLLCDEATSALDpQTTDQILDLLLDINRRFNLTIVLITHEM-HVVRKiCDRVAVMENGKVVEEG---DVLSV 228
Cdd:PRK03695 153 qLLLLDEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGrrdEVLTP 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-205 |
4.62e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqDISAAKGEALRQARLKISMVFQHfNLLWSRTVREN 102
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSM------------------------QIAGVPKAKIAARVAELV------ELVGLKGREH----------------- 135
Cdd:PTZ00265 480 IKYSLyslkdlealsnyynedgndsqenkNKRNSCRAKCAGDLNDMSnttdsnELIEMRKNYQtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 136 ----AYP-----------SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHE 200
Cdd:PTZ00265 560 dfvsALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
....*
gi 695703442 201 MHVVR 205
Cdd:PTZ00265 640 LSTIR 644
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-223 |
9.21e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 9.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIR-LLNGLEKPSTGSVTVNGqdisaakgealrqarlKISMVFQhFNLLWSRTVRE 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG----------------TVAYVPQ-VSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 102 NIAFsmqiaGVP----KAKIAARVAELV-ELVGLKGREHAYPSQ----LSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:PLN03130 698 NILF-----GSPfdpeRYERAIDVTALQhDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695703442 173 PQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKIcDRVAVMENGKVVEEG 223
Cdd:PLN03130 773 AHVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-222 |
2.85e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-GEALRQA-------RLKISMVFQHfnllw 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGimlcpedRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 srTVRENIAFSMQIAGVP-----KAKIAARVAEL-VELVGLKGREHAYP-SQLSGGQKQRVGIARALANNPDVLLCDEAT 168
Cdd:PRK11288 347 --SVADNINISARRHHLRagcliNNRWEAENADRfIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695703442 169 SALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEE 222
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-216 |
3.10e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 58 STGSVTVNGQDISAAKgeaLRQARLKISMVFQHfNLLWSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREH-- 135
Cdd:PTZ00265 1275 NSGKILLDGVDICDYN---LKDLRNLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYdt 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 136 ---AYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHVVRKiCDRVA 212
Cdd:PTZ00265 1351 nvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIV 1429
|
....
gi 695703442 213 VMEN 216
Cdd:PTZ00265 1430 VFNN 1433
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
264-336 |
1.29e-16 |
|
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: 73.25 E-value: 1.29e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 264 TVIRLTFTGHSTHKPIVGELTLRYGLPFNILHGKMTQTAHGVFGQLWVHVAASDEQLNNILADLQHSDIEGEV 336
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-212 |
1.74e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.16 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDnGKVAltaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVngqdisaakGEAlrqar 81
Cdd:PRK11819 325 IEAENLSKSFG-DRLL---IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GET----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 LKISMVFQ-HFNLLWSRTVRENIAFSMQIAGVPKAKIAAR--VAELvelvGLKGREHAYP-SQLSGGQKQRVGIARALAN 157
Cdd:PRK11819 387 VKLAYVDQsRDALDPNKTVWEEISGGLDIIKVGNREIPSRayVGRF----NFKGGDQQKKvGVLSGGERNRLHLAKTLKQ 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 158 NPDVLLCDEATSALDPQTTDQILDLLLDinrrFNLTIVLITHEmhvvRKICDRVA 212
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLE----FPGCAVVISHD----RWFLDRIA 509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-217 |
2.52e-16 |
|
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: 76.60 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALR-QARLKISMVFQHFNLLwS 96
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAFsmqiaGVPKAKiaARVAELVELVGLKGREHAYPS-----------QLSGGQKQRVGIARALANNPDVLLCD 165
Cdd:cd03290 93 ATVEENITF-----GSPFNK--QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 166 EATSALDPQTTDQ-----ILDLLLDINRrfnlTIVLITHEMHVVRKiCDRVAVMENG 217
Cdd:cd03290 166 DPFSALDIHLSDHlmqegILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-229 |
5.63e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.25 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 15 KVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIR-LLNGLEKPSTGSVTVNGQDISAAKgealrqarlkISMVFqhfnl 93
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVPQ----------VSWIF----- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 94 lwSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQ----LSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PLN03232 692 --NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 170 ALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKIcDRVAVMENGKVVEEGDVLSVF 229
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-224 |
1.10e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.28 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqdisaakgealrQARLKISMVFQHfnlLW--SRTVR 100
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------------WAERSIAYVPQQ---AWimNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMQIAGVPKAKiAARV----AELVEL-------VGLKGrehaypSQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:PTZ00243 739 GNILFFDEEDAARLAD-AVRVsqleADLAQLgggleteIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 170 ALDPQTTDQIL-DLLLdiNRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGD 224
Cdd:PTZ00243 812 ALDAHVGERVVeECFL--GALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-199 |
1.24e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 3 VLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTgsvtvngqdisaakGEALRQARL 82
Cdd:PRK11819 8 TMNRVSKVVPPKKQIL---KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFE--------------GEARPAPGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 KISMVFQHFNLLWSRTVRENI---------------AFSMQIAgVPKA---KIAARVAELVELVglkgrEHA-------- 136
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENVeegvaevkaaldrfnEIYAAYA-EPDAdfdALAAEQGELQEII-----DAAdawdldsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 137 ---------YP------SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD---QILdllldinRRFNLTIVLIT 198
Cdd:PRK11819 145 leiamdalrCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwleQFL-------HDYPGTVVAVT 217
|
.
gi 695703442 199 H 199
Cdd:PRK11819 218 H 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-222 |
3.11e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 12 DNGKValtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAA-------KGEALRQARLKI 84
Cdd:PRK09700 275 DRKKV-----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspldavkKGMAYITESRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 85 SMVFQHFnllwsrTVRENIAFSMQIA--------GVPKAKIAARVAELV-ELVGLKGRE-HAYPSQLSGGQKQRVGIARA 154
Cdd:PRK09700 350 NGFFPNF------SIAQNMAISRSLKdggykgamGLFHEVDEQRTAENQrELLALKCHSvNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEE 222
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-223 |
1.56e-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: 74.98 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgeALRQARLKISMVFQHfNLLWSRTVREN 102
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFKITIIPQD-PVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAgvpkakiAARVAELVELVGLKGREHAYPSQL-----------SGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:TIGR00957 1380 LDPFSQYS-------DEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 172 DPQTTDQILDlllDINRRF-NLTIVLITHEMHVVRKICdRVAVMENGKVVEEG 223
Cdd:TIGR00957 1453 DLETDNLIQS---TIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-220 |
2.26e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgQDISAAKgeaLRQ--ARLKISMVFQHfnllwsrtV 99
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVAR---LQQdpPRNVEGTVYDF--------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIA-----------FSMQIAGVPKAKIAARVAEL-------------------VELVGLKGreHAYPSQLSGGQKQRV 149
Cdd:PRK11147 88 AEGIEeqaeylkryhdISHLVETDPSEKNLNELAKLqeqldhhnlwqlenrinevLAQLGLDP--DAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 150 GIARALANNPDVLLCDEATSALDPQTTDQILDLLLDinrrFNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-241 |
3.79e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 35 GIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQHfNLLWSRTVRENI-AFSMQ-IAGV 112
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV---LSIIPQS-PVLFSGTVRFNIdPFSEHnDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 113 PKAKIAARVAELVEL--VGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTtdqilDLLLD--INR 188
Cdd:PLN03232 1342 WEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-----DSLIQrtIRE 1416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 189 RF-NLTIVLITHEMHVVRKiCDRVAVMENGKVVE----------EGDVLSVFTHPQQPITQQFV 241
Cdd:PLN03232 1417 EFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEydspqellsrDTSAFFRMVHSTGPANAQYL 1479
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-220 |
7.49e-14 |
|
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: 69.21 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 2 IVLSNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL----EKPStGSVTVNGQDISaakgEAL 77
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYK----EFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 78 RQARLKISMVFQ---HFNLLwsrTVRENIAFSmqiagvpkakiaarvaelvelvgLKGREHAYPSQLSGGQKQRVGIARA 154
Cdd:cd03233 79 EKYPGEIIYVSEedvHFPTL---TVRETLDFA-----------------------LRCKGNEFVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 155 LANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVLITHEMHV-VRKICDRVAVMENGKVV 220
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-218 |
9.98e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.85 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFdnGKVALtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqdiSAAKGE---AL 77
Cdd:PRK15064 1 MLSTANITMQF--GAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-------SLDPNErlgKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 78 RQARLK------ISMVFQHFNLLWS-RTVRENIaFS---------MQIAGVpKAKIA--------ARVAELVELVGLKGR 133
Cdd:PRK15064 70 RQDQFAfeeftvLDTVIMGHTELWEvKQERDRI-YAlpemseedgMKVADL-EVKFAemdgytaeARAGELLLGVGIPEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 134 EHAYP-SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLldiNRRfNLTIVLITHEMHVVRKICDRVA 212
Cdd:PRK15064 148 QHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL---NER-NSTMIIISHDRHFLNSVCTHMA 223
|
....*.
gi 695703442 213 VMENGK 218
Cdd:PRK15064 224 DLDYGE 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-223 |
2.83e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQdisaakgealrqarlkISMVFQHfnlLWSR--T 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQ---AWIQndS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQ----LSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695703442 175 TTDQILDLLLDINRRF-NLTIVLITHEMHVVRKIcDRVAVMENGKVVEEG 223
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-215 |
4.90e-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: 67.82 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 27 TIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealrqarlkismvfQHFNLLWSRTVRENIAFS 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---------------QYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 107 MQIAGVpKAKIAARVAELVELVGLKGREhayPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDpqtTDQILdLLLDI 186
Cdd:cd03237 86 TKDFYT-HPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD---VEQRL-MASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 695703442 187 NRRFNL----TIVLITHEMHVVRKICDRVAVME 215
Cdd:cd03237 158 IRRFAEnnekTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-225 |
8.01e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGleKPS----TGSVTVNGQDISAAKGEAlrQARLKISMVFQhfnllwsrt 98
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEE--RAHLGIFLAFQ--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 vreniaFSMQIAGVP---------KAKIAAR-------------VAELVELVGLKgrehayPSQL--------SGGQKQR 148
Cdd:CHL00131 92 ------YPIEIPGVSnadflrlayNSKRKFQglpeldplefleiINEKLKLVGMD------PSFLsrnvnegfSGGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 149 VGIARALANNPDVLLCDEATSALDpqttdqiLDLLLDINRRFNL------TIVLITHEMHVVRKIC-DRVAVMENGKVVE 221
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLD-------IDALKIIAEGINKlmtsenSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
....
gi 695703442 222 EGDV 225
Cdd:CHL00131 233 TGDA 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-252 |
1.52e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.12 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 25 NLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKGEALRQArlkISMVFQHFN--LL------WS 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDEWQRNNtdMLspgeddTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAFSmqiagvpkAKIAARVAELVELVG---LKGREHAYpsqLSGGQKQRVGIARALANNPDVLLCDEATSALDP 173
Cdd:PRK10938 100 RTTAEIIQDE--------VKDPARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 174 QTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGdvlsvfthPQQPITQQFVrqVSQYAEEET 252
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETG--------EREEILQQAL--VAQLAHSEQ 236
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-242 |
1.54e-12 |
|
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: 66.47 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTL----IRLLNGLEkpstGSVTVNGQDISAAKGEALRQarlKISMVFQHfNLLWSRT 98
Cdd:cd03288 39 HVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTLRS---RLSIILQD-PILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAfsmqiagvPKAKIA-ARVAELVELVGLKGREHAYPSQL-----------SGGQKQRVGIARALANNPDVLLCDE 166
Cdd:cd03288 111 IRFNLD--------PECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 167 ATSALDpQTTDQILDLLLdINRRFNLTIVLITHEMHVVRKiCDRVAVMENGKVVEEGDVLSVFTHPQQPITqQFVR 242
Cdd:cd03288 183 ATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA-SLVR 254
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-219 |
5.14e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqdisaakgeaLRQARLKISMVFQHFNLLWSRTVREN 102
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQIAGVPKAKIAARVAELvelvGLKGREHAYPS-QLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILD 181
Cdd:PLN03073 593 LYMMRCFPGVPEQKLRAHLGSF----GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
170 180 190
....*....|....*....|....*....|....*...
gi 695703442 182 LLLdinrRFNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:PLN03073 669 GLV----LFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-229 |
5.19e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPS--TGSVTVNGQDISaakgealRQARLKISMVFQHFNLLWS 96
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT-------KQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 97 RTVRENIAFsMQIAGVPKA---KIAARVAELV--ELvGLKGREH-----AYPSQLSGGQKQRVGIARALANNPDVLLCDE 166
Cdd:PLN03211 155 LTVRETLVF-CSLLRLPKSltkQEKILVAESVisEL-GLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 167 ATSALDPQTTDQILDLLLDINRRfNLTIVLITHE-MHVVRKICDRVAVMENGKVVEEG---DVLSVF 229
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGkgsDAMAYF 298
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
5.51e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-EKPSTGSVTVNGQDIsaaKGEALRQA-RLKISMV---FQHFNLLW 95
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPV---KIRNPQQAiAQGIAMVpedRKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SRTVRENIAFSM--QIAGVPKAKIAARVAELVELVG-LKGREhAYP----SQLSGGQKQRVGIARALANNPDVLLCDEAT 168
Cdd:PRK13549 355 VMGVGKNITLAAldRFTGGSRIDDAAELKTILESIQrLKVKT-ASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695703442 169 SALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-221 |
7.03e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAkgeALRQARLKISMVFQHfNLLWSRTVRENI 103
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQA-PVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 104 -AFSMQiagvPKAKI--AARVAELVELV-----GLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQT 175
Cdd:PLN03130 1334 dPFNEH----NDADLweSLERAHLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695703442 176 tdqilDLLLD--INRRF-NLTIVLITHEMHVVRKiCDRVAVMENGKVVE 221
Cdd:PLN03130 1410 -----DALIQktIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-219 |
7.12e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 20 AVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAK-------GEAL----RQARLKISMVF 88
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhGFALvteeRRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 89 QHFNLLWSrtvreNI-AFSMQIAGVPKAKIAARVAELVELVGLKGREHAYP-SQLSGGQKQRVGIARALANNPDVLLCDE 166
Cdd:PRK10982 343 IGFNSLIS-----NIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695703442 167 ATSALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
7.48e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.88 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGqdisaakgealrqarlKISMVFQhFNLLWSRTVREN 102
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQ-FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IafsmqIAGVPKAKIaaRVAELVELVGLKGREHAYPSQ-----------LSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:cd03291 118 I-----IFGVSYDEY--RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695703442 172 DPQTTDQILDLLLdINRRFNLTIVLITHEMHVVRKiCDRVAVMENG 217
Cdd:cd03291 191 DVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-225 |
8.62e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 18 LTAVDNVNLTIAQGQIYGIIGYSGAG--KSTLIRLLNGlekPSTGSVTVNGQDISAAKgEALRQArlkismVFQHFNLLW 95
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANR-RALRRT------IG*HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SR----TVRENIAFSMQIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSAL 171
Cdd:NF000106 96 GRresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695703442 172 DPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKVVEEGDV 225
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-172 |
1.12e-11 |
|
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: 65.58 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 27 TIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVtvngqDISAAKGEALRqaRLKISMVFQHFNLLWSRTVRenIAFS 106
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLK--RFRGTELQDYFKKLANGEIK--VAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 107 MQ-IAGVPKA----------KIAAR--VAELVELVGLKG---REhayPSQLSGGQKQRVGIARALANNPDVLLCDEATSA 170
Cdd:COG1245 166 PQyVDLIPKVfkgtvrelleKVDERgkLDELAEKLGLENildRD---ISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
..
gi 695703442 171 LD 172
Cdd:COG1245 243 LD 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-219 |
1.28e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.23 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGL-EKPSTGSVTVNGQDISAAK-GEALRQarlKISMV---FQHFNLLW 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNpAQAIRA---GIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 96 SRTVRENIAFSM--QIAGVPKAKIAARVAELVELVGLKGREHAYP----SQLSGGQKQRVGIARALANNPDVLLCDEATS 169
Cdd:TIGR02633 353 ILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695703442 170 ALDPQTTDQILDLLLDINRRfNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-219 |
1.47e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGsvtvngqDISAAKGealrqarLKISMVFQHfNLLWSRT 98
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKG-------IKLGYFAQH-QLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAgvPKAkIAARVAELVELVGLKGREHAYPS-QLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD 177
Cdd:PRK10636 391 DESPLQHLARLA--PQE-LEQKLRDYLGGFGFQGDKVTEETrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695703442 178 QILDLLLDinrrFNLTIVLITHEMHVVRKICDRVAVMENGKV 219
Cdd:PRK10636 468 ALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-217 |
2.78e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 11 FDNGKVALTAV-DNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGqdisaakgealrqarlKISMVFQ 89
Cdd:TIGR01271 431 FSNFSLYVTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 90 hFNLLWSRTVRENIAFSM-----QIAGVPKAkiaarvAELVELVGLKGREHAYP-----SQLSGGQKQRVGIARALANNP 159
Cdd:TIGR01271 495 -TSWIMPGTIKDNIIFGLsydeyRYTSVIKA------CQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLdINRRFNLTIVLITHEMHVVRKiCDRVAVMENG 217
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFESCL-CKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-183 |
3.61e-11 |
|
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: 61.49 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 5 SNISKVFDNGKVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPS--TGSVTVNGQdisaAKGEALRQarl 82
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR----PLDKNFQR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 83 KISMVFQHFNLLWSRTVRENIAFSMQIAGvpkakiaarvaelvelvglkgrehaypsqLSGGQKQRVGIARALANNPDVL 162
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSIL 130
|
170 180
....*....|....*....|.
gi 695703442 163 LCDEATSALDPQTTDQILDLL 183
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-210 |
4.14e-11 |
|
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: 60.46 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 30 QGQIYGIIGYSGAGKSTLIRLL-NGLEKPSTGSVTVNGQDISAAKGEALRQARLKISmvfqhfnllwsrtvreniafsmq 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 109 iagvpkakiaarvaelvelvglkgrehayPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDL-----L 183
Cdd:smart00382 58 -----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180
....*....|....*....|....*..
gi 695703442 184 LDINRRFNLTIVLITHEMHVVRKICDR 210
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-204 |
6.60e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.61 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNG--QDI-SAAKG-------EALRQARLKISMVFQHFNLLwSRTVR 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwDEIlDEFRGselqnyfTKLLEGDVKVIVKPQYVDLI-PKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIafsmqIAGVPKAKIAARVAELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSaldpqttdqil 180
Cdd:cd03236 105 GKV-----GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS----------- 168
|
170 180
....*....|....*....|....*..
gi 695703442 181 dlLLDINRRFNLTIV---LITHEMHVV 204
Cdd:cd03236 169 --YLDIKQRLNAARLireLAEDDNYVL 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
9.48e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 21 VDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaaKGEALRQARLkiSMVFQHFNLLWSRTVR 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKQL--CFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIAFSMQIAGVpkakiAARVAELVELVGLkgrEHA--YP-SQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTD 177
Cdd:PRK13540 93 ENCLYDIHFSPG-----AVGITELCRLFSL---EHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 695703442 178 QILDlLLDINRRFNLTIVLITHE 200
Cdd:PRK13540 165 TIIT-KIQEHRAKGGAVLLTSHQ 186
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-215 |
1.06e-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: 62.49 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 26 LTIAQGQIY-----GIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaakgealrqarLKISMVFQHFNLLWSRTVR 100
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----------------LKISYKPQYISPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 101 ENIafsmqiagvpKAKIAARV------AELVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDP- 173
Cdd:COG1245 420 EFL----------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVe 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695703442 174 ---QTTDQIldllldinRRF----NLTIVLITHEMHVVRKICDRVAVME 215
Cdd:COG1245 490 qrlAVAKAI--------RRFaenrGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-172 |
1.07e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 27 TIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNG---QDISAAKG-------EALRQARLKISMVFQHFNLLWS 96
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFRGtelqnyfKKLYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703442 97 R---TVREniafsmQIAGVPKAKIAARVAELVELVGLKGREhayPSQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:PRK13409 175 VfkgKVRE------LLKKVDERGKLDEVVERLGLENILDRD---ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-199 |
1.43e-10 |
|
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: 62.46 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVAltaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaakgealrqA 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVL---IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------------A 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 81 RLKISMVFQ--HFNLlwsRTVRENI-----AFSMQIAGVPKAKIAArVAELVELVGLKGREHAYPS------QLSGGQKQ 147
Cdd:TIGR00954 514 KGKLFYVPQrpYMTL---GTLRDQIiypdsSEDMKRRGLSDKDLEQ-ILDNVQLTHILEREGGWSAvqdwmdVLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695703442 148 RVGIARALANNPDVLLCDEATSALDPQTTDQILDLLldinRRFNLTIVLITH 199
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-219 |
2.96e-10 |
|
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: 60.25 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTL----IRLLNglekpSTGSVTVNGQDISAAkgeA 76
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVL---ENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSV---P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRQARLKISMVFQHFnLLWSRTVRENIAFSMQIAGVPKAKIAarvaelvELVGLKGREHAYPSQL-----------SGGQ 145
Cdd:cd03289 72 LQKWRKAFGVIPQKV-FIFSGTFRKNLDPYGKWSDEEIWKVA-------EEVGLKSVIEQFPGQLdfvlvdggcvlSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPqTTDQILDLLLdiNRRF-NLTIVLITHEMHVVRKiCDRVAVMENGKV 219
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTL--KQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-221 |
3.89e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNIsKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNG--------QDISAA 72
Cdd:PRK10636 1 MIVFSSL-QIRRGVRVLL---DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 73 KGEAL-------RQARlKISMVFQHFNllwSRTVRENIA-FSMQIAGVPKAKIAARVAELVELVGLKGREHAYP-SQLSG 143
Cdd:PRK10636 77 PQPALeyvidgdREYR-QLEAQLHDAN---ERNDGHAIAtIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 144 GQKQRVGIARALANNPDVLLCDEATSALDpqttdqiLDLLLDINR---RFNLTIVLITHEMHVVRKICDRVAVMENGKVV 220
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlkSYQGTLILISHDRDFLDPIVDKIIHIEQQSLF 225
|
.
gi 695703442 221 E 221
Cdd:PRK10636 226 E 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-172 |
6.64e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 27 TIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaakgealrqarLKISMVFQHFNLLWSRTVRENIafs 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------------LKISYKPQYIKPDYDGTVEDLL--- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 107 mqiagvpkAKIAARVA------ELVELVGLkgrEHAYPSQ---LSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:PRK13409 422 --------RSITDDLGssyyksEIIKPLQL---ERLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-219 |
8.33e-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: 60.31 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 1 MIVLSNISKVFDNGKVALtavDNVNLTIAQGQIYGIIGYSGAGKSTLI----RLLNglekpSTGSVTVNGQDISAAkgeA 76
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVL---QDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS-----TEGEIQIDGVSWNSV---T 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 77 LRQARLKISMVFQHFnLLWSRTVRENIAFSMQIAGVPKAKIAarvaelvELVGLKGREHAYPSQL-----------SGGQ 145
Cdd:TIGR01271 1287 LQTWRKAFGVIPQKV-FIFSGTFRKNLDPYEQWSDEEIWKVA-------EEVGLKSVIEQFPDKLdfvlvdggyvlSNGH 1358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695703442 146 KQRVGIARALANNPDVLLCDEATSALDPqTTDQILDLLLdiNRRF-NLTIVLITHEMHVVRKiCDRVAVMENGKV 219
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTL--KQSFsNCTVILSEHRVEALLE-CQQFLVIEGSSV 1429
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-183 |
1.10e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 22 DNVNLTIAQGQIYGIIGYSGAGKSTlirLLNGL-EKPSTGSVTvngQDISAAKGEALRQARLKISMVFQHFNL-LWSRTV 99
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTT---LLNVLaERVTTGVIT---GGDRLVNGRPLDSSFQRSIGYVQQQDLhLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 100 RENIAFSM---QIAGVPKAKIAARVAELVELVGLKGREHAY----PSQLSGGQKQRVGIARALANNPDVLL-CDEATSAL 171
Cdd:TIGR00956 854 RESLRFSAylrQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170
....*....|..
gi 695703442 172 DPQTTDQILDLL 183
Cdd:TIGR00956 934 DSQTAWSICKLM 945
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
38-174 |
1.76e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 38 GYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISAAKgealrqaRLKISMVFQHF-NLLWSRTVRENIAFSMQIAGVPKAK 116
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLpGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 117 IAARVaelVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK13543 117 MPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-224 |
2.27e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 24 VNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLE--KPSTGSVTVNGQDISAAKGEalRQARLKISMVFQH-------FNLL 94
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE--DRAGEGIFMAFQYpveipgvSNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 95 WSRTVRENIAFSMQIAGVPKAKIAARVAELVELVGLkgrehayPSQL---------SGGQKQRVGIARALANNPDVLLCD 165
Cdd:PRK09580 98 FLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKM-------PEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695703442 166 EATSALDP---QTTDQILDLLLDINRRFnltiVLITHEMHVVRKI-CDRVAVMENGKVVEEGD 224
Cdd:PRK09580 171 ESDSGLDIdalKIVADGVNSLRDGKRSF----IIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-251 |
2.53e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLL----NGLEKPSTGSVTVNGQDISAAK----GEALRQARLKIsmvfqHFNLL 94
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKkhyrGDVVYNAETDV-----HFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 95 wsrTVRENIAFSM-------QIAGVPKAKIAARVAELVelVGLKGREHAYPSQ--------LSGGQKQRVGIARALANNP 159
Cdd:TIGR00956 154 ---TVGETLDFAArcktpqnRPDGVSREEYAKHIADVY--MATYGLSHTRNTKvgndfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 160 DVLLCDEATSALDPQTTDQILDLLLDINRRFNLT-IVLITHEMHVVRKICDRVAVMENGKVVEEGDVLSV--------FT 230
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFK 308
|
250 260
....*....|....*....|.
gi 695703442 231 HPQQPITQQFVRQVSQYAEEE 251
Cdd:TIGR00956 309 CPDRQTTADFLTSLTSPAERQ 329
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-172 |
1.13e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 31 GQIYGIIGYSGAGKSTLIRLLNGLEKPS--TGSVTVNG----QDISAAKGEALRQARLKISMVfqhfnllwsrTVRENIA 104
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkQETFARISGYCEQNDIHSPQV----------TVRESLI 975
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 105 FS------MQIAGVPKAKIAARVAELVELVGLKGREHAYP--SQLSGGQKQRVGIARALANNPDVLLCDEATSALD 172
Cdd:PLN03140 976 YSaflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-183 |
2.16e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNGQDISaakgealRQARLKISMVFQHFNLLWSRTVREN 102
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-------NIAKPYCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 103 IAFSMQI----AGVPKAKIAARVAELVElvglkgrEHAYpsQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQ 178
Cdd:PRK13541 91 LKFWSEIynsaETLYAAIHYFKLHDLLD-------EKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
....*
gi 695703442 179 ILDLL 183
Cdd:PRK13541 162 LNNLI 166
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-207 |
3.03e-06 |
|
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: 47.22 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 36 IIGYSGAGKSTLIRLLN-GL--EKPSTGSVTVNGQDIsAAKGEALRQARLkismvfqHFNLLWSR--TVRENIAFSMQIA 110
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyALtgELPPNSKGGAHDPKL-IREGEVRAQVKL-------AFENANGKkyTITRSLAILENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 111 GVPKAKIAARVAELVElvglkgrehaypsQLSGGQKQ------RVGIARALANNPDVLLCDEATSALDPQTTD-QILDLL 183
Cdd:cd03240 99 FCHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEII 165
|
170 180
....*....|....*....|....
gi 695703442 184 LDINRRFNLTIVLITHEMHVVRKI 207
Cdd:cd03240 166 EERKSQKNFQLIVITHDEELVDAA 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-172 |
4.13e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 26 LTIAQGQIYGIIGYSGAGKSTLIRLL-----NGL---------EKPSTGSVTVNGQDISAAKGEALRQARLKISMVFQHf 91
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRYMamhaiDGIpkncqilhvEQEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQQ- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 92 nllwsRTVRENIAF----SMQIAGVPKAKIAARVAELVE-----------------LVGLK---GREHAYPSQLSGGQKQ 147
Cdd:PLN03073 277 -----RELEFETETgkgkGANKDGVDKDAVSQRLEEIYKrlelidaytaearaasiLAGLSftpEMQVKATKTFSGGWRM 351
|
170 180
....*....|....*....|....*
gi 695703442 148 RVGIARALANNPDVLLCDEATSALD 172
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-223 |
6.22e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 139 SQLSGGQKQRVGIARALANNPD--VLLCDEATSALDPQTTDQILDLLLDInRRFNLTIVLITHEMHVVRKiCDRVAVM-- 214
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFgp 163
|
90
....*....|...
gi 695703442 215 ----ENGKVVEEG 223
Cdd:cd03238 164 gsgkSGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-233 |
7.38e-06 |
|
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: 45.64 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 28 IAQGQIYGIIGYSGAGKSTLIRLLNGLEKPstgsvtvNGQDISaakgealrqarlkismvfqhfnllWSRTvreNIAFSM 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP-------NGDNDE------------------------WDGI---TPVYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 108 QiagvpkaKIaarvaelvelvglkgrehaypsQLSGGQKQRVGIARALANNPDVLLCDEATSALDpqtTDQILDLLLDIn 187
Cdd:cd03222 68 Q-------YI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD---IEQRLNAARAI- 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695703442 188 RRFNL----TIVLITHEMHVVRKICDRVAVMENgkvveEGDVLSVFTHPQ 233
Cdd:cd03222 115 RRLSEegkkTALVVEHDLAVLDYLSDRIHVFEG-----EPGVYGIASQPK 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-62 |
1.13e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 2 IVLSNISKVFDNGKValtaVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSV 62
Cdd:PRK15064 320 LEVENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-223 |
1.82e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLI---------------------RLLNGLEKPSTGSVTVNGQDISAAKGEALRQAR 81
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRNPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 82 L---KISMVFQHFNLLWSRtvreniafsmqiagvpkAKIAARVAELVElVGLkgrEHAYPSQ----LSGGQKQRVGIARA 154
Cdd:cd03270 93 StvgTVTEIYDYLRLLFAR-----------------VGIRERLGFLVD-VGL---GYLTLSRsaptLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695703442 155 LANNPDVLL--CDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVRkICDRV------AVMENGKVVEEG 223
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIR-AADHVidigpgAGVHGGEIVAQG 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-209 |
2.05e-05 |
|
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: 45.30 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 23 NVNLTIAQGQIYGIIGYSGAGKSTLIR--LLNGLEKPSTGSVTV--NGQDISAAK-------------GEALRQARLKIS 85
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQpgNHDRIEGLEhidkvividqspiGRTPRSNPATYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 86 MVFQHFNLLW------SRTVRE---------NIA--FSMQI-------AGVPKakIAARVAELVElVGLKGREHAYPS-Q 140
Cdd:cd03271 93 GVFDEIRELFcevckgKRYNREtlevrykgkSIAdvLDMTVeealeffENIPK--IARKLQTLCD-VGLGYIKLGQPAtT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695703442 141 LSGGQKQRVGIARAL---ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVrKICD 209
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVI-KCAD 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-211 |
2.11e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 2.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695703442 139 SQLSGGQKQRVGIARALAN---NPDVLLCDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVrKICDRV 211
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVV-KVADYV 881
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-200 |
2.32e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 19 TAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPSTGSVTVNgqdisaakgealrqARLKISMVFQHFNLL-WSR 97
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------------TKLEVAYFDQHRAELdPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 98 TVRENIAFSMQ---IAGVPKAKIAArvaeLVELVGLKGREHAYPSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQ 174
Cdd:PRK11147 399 TVMDNLAEGKQevmVNGRPRHVLGY----LQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
170 180
....*....|....*....|....*.
gi 695703442 175 TtdqiLDLLLDINRRFNLTIVLITHE 200
Cdd:PRK11147 475 T----LELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-199 |
5.47e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 5.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695703442 140 QLSGGQKQRVGIARALAN---NPDVLLC-DEATSALDPQTTDQILDLLLDINRRFNLTIVlITH 199
Cdd:cd03227 77 QLSGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITH 139
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-253 |
7.64e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 15 KVALTAVDNVNLTIAQGQIYGIIGYSGAGKSTLIRLLNGLEKPS---TGSVTVNGQDISAAkgeALRQARLKISMVFQHF 91
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEF---VPRKTSAYISQNDVHV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 92 NLLwsrTVRENIAFSMQIAGV--------------------PKAKI----AARVAELVE----------LVGLK------ 131
Cdd:PLN03140 252 GVM---TVKETLDFSARCQGVgtrydllselarrekdagifPEAEVdlfmKATAMEGVKsslitdytlkILGLDickdti 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 132 -GREHAypSQLSGGQKQRVGIARALANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNLTIVL-ITHEMHVVRKICD 209
Cdd:PLN03140 329 vGDEMI--RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFD 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 695703442 210 RVAVMENGKVVEEG---DVLSVFTH-----PQQPITQQFVRQVSQYAEEETF 253
Cdd:PLN03140 407 DIILLSEGQIVYQGprdHILEFFEScgfkcPERKGTADFLQEVTSKKDQEQY 458
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-199 |
1.50e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 33 IYGIIGYSGAGKSTLIRLLN-GLekpsTGSVTVNGQDISAAKGEALRQARlkISMVFQH-------------FNLLWSRT 98
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRyAL----YGKARSRSKLRSDLINVGSEEAS--VELEFEHggkryrierrqgeFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 99 VRENIAFSMQIAGVP------------KAKIAARVAELVELVGLKGREHAY------PSQLSGGQKQRVGIARALAnnpd 160
Cdd:COG0419 99 PSERKEALKRLLGLEiyeelkerlkelEEALESALEELAELQKLKQEILAQlsgldpIETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 695703442 161 vLLCDeaTSALDPQTTDQILDLLLDinrrfnltIVLITH 199
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
4.37e-03 |
|
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: 38.84 E-value: 4.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 141 LSGGQKQRVGIARAL---ANNPDVLLCDEATSALDPQTTDQILDLLLDINRRFNlTIVLITHEMHVVR 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
31-126 |
6.30e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 37.75 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703442 31 GQIYGIIGYSGAGKSTL----------IRLLNGLEKPSTGSVTVngqdISAAKGEALRQARLKisMVFQHFNLLWSRTVR 100
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLaldlavavatGRDWLGERRVKQGRVVY----LAAEDPRDGLRRRLK--AIGAHLGDEDAALAE 74
|
90 100
....*....|....*....|....*.
gi 695703442 101 ENIAFSMQIAGVPKAKIAARVAELVE 126
Cdd:cd01125 75 NLVIENLRGKPVSIDAEAPELERIIE 100
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
35-84 |
8.75e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.67 E-value: 8.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695703442 35 GIIGYSGAGKSTLI-RLLNGLEK----------PSTGSVTVNGQDI----------SAAKGEALRQARLKI 84
Cdd:pfam01926 3 ALVGRPNVGKSTLInALTGAKAIvsdypgttrdPNEGRLELKGKQIilvdtpglieGASEGEGLGRAFLAI 73
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-183 |
9.92e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 9.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 695703442 139 SQLSGGQKQRVG---IARALA--------NNPDVLLC--DEATSALDPQTTDQILDLL 183
Cdd:pfam13558 31 GGLSGGEKQLLAylpLAAALAaqygsaegRPPAPRLVflDEAFAKLDEENIRTALELL 88
|
|
| |
