|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-268 |
6.89e-102 |
|
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: 307.22 E-value: 6.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGffsREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRS 85
Cdd:COG1123 260 LLEVRNLSKRYPVRG---KGGVRAVDDVSLTL--RRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK-LS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQLQ 165
Cdd:COG1123 334 RRSLRELRRRVQMVFQDPYSSLNPRMTVGD-IIAEPLRLHGLLSRAERRERVAELLERVGLP-PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 245
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250 260
....*....|....*....|...
gi 1817161977 246 VLEHPKHAYSIALKNAVLPPNPR 268
Cdd:COG1123 492 VFANPQHPYTRALLAAVPSLDPA 514
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-268 |
7.21e-93 |
|
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: 277.70 E-value: 7.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKA---DRGSIHFDGTDVKA 82
Cdd:COG0444 1 LLEVRNLKVYFPTR----RGVVKAVDGVSFDV--RRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAkSRAEKEAIADVALQRVGLSMAE-IKGRFSHELSG 161
Cdd:COG0444 75 LSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGL-SKAEARERAIELLERVGLPDPErRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|....*..
gi 1817161977 242 DARDVLEHPKHAYSIALKNAVLPPNPR 268
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPD 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-279 |
3.38e-90 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 271.22 E-value: 3.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkA 82
Cdd:COG4608 7 LLEVRDLKKHFPVrGGLFGRTVgvVKAVDGVSFDI--RRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGG 162
Cdd:COG4608 84 GLSGRELRPLRRRMQMVFQDPYASLNPRMTVGD-IIAEPLRIHGLASKAERRERVAELLELVGLR-PEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 163 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 242
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 1817161977 243 ARDVLEHPKHAYSIALKNAVLPPNPReasailRLRQR 279
Cdd:COG4608 242 RDELYARPLHPYTQALLSAVPVPDPE------RRRER 272
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-264 |
1.31e-84 |
|
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: 254.34 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrs 85
Cdd:COG1124 1 MLEVRNLSVSYGQG----GRRVPVLKDVSLEV--APGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLL--ATAHRFKGAKSRAEKeaiadvALQRVGLSmAEIKGRFSHELSGGQ 163
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAepLRIHGLPDREERIAE------LLEQVGLP-PSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250 260
....*....|....*....|.
gi 1817161977 244 RDVLEHPKHAYSIALKNAVLP 264
Cdd:COG1124 224 ADLLAGPKHPYTRELLAASLA 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-241 |
1.19e-82 |
|
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: 248.57 E-value: 1.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGFfsreKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGG----SVKALDDVSFSIK--KGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQLQ 165
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-263 |
1.82e-81 |
|
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: 255.38 E-value: 1.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKAdRGSIHFDGTDVKA 82
Cdd:COG4172 275 LLEARDLKVWFPIkRGLFRRTVghVKAVDGVSLTLRRG--ETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 vRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLA---TAHRfkGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHEL 159
Cdd:COG4172 352 -LSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQ-IIAeglRVHG--PGLSAAERRARVAEALEEVGLD-PAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 239
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....
gi 1817161977 240 SGDARDVLEHPKHAYSIALKNAVL 263
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-254 |
9.00e-67 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 209.31 E-value: 9.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIG-GFFSREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK--- 81
Cdd:COG4167 4 LLEVRNLSKTFKYRtGLFRRQQFEAVKPVSFTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 -AVRSRRDReafMakvqpVFQNPFEAFNPLTRIDEYL-----LATAHRfkgAKSRAEKeaIADVaLQRVGLsMAEIKGRF 155
Cdd:COG4167 82 yKYRCKHIR---M-----IFQDPNTSLNPRLNIGQILeeplrLNTDLT---AEEREER--IFAT-LRLVGL-LPEHANFY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
250
....*....|....*....
gi 1817161977 236 VVVESGDARDVLEHPKHAY 254
Cdd:COG4167 227 EVVEYGKTAEVFANPQHEV 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-268 |
1.82e-66 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 210.59 E-value: 1.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSREKM-KAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkAV 83
Cdd:PRK11308 5 LLQAIDLKKHYPVkRGLFKPERLvKALDGVSFTLERGK--TLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 RSRRDREAFMAKVQPVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQ 163
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKV-GQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260
....*....|....*....|....*..
gi 1817161977 244 RDVLEHPKHAYSIALKNAV--LPPNPR 268
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATprLNPDDR 266
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-268 |
2.25e-63 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 202.63 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGG----FFSREK-MKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwFWQPPKtLKAVDGVTLRLYEG--ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVrSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRFSHELS 160
Cdd:PRK15079 86 LGM-KDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGL-LPNLINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 240
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 243
|
250 260
....*....|....*....|....*...
gi 1817161977 241 GDARDVLEHPKHAYSIALKNAVLPPNPR 268
Cdd:PRK15079 244 GTYDEVYHNPLHPYTKALMSAVPIPDPD 271
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-278 |
2.24e-58 |
|
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: 194.74 E-value: 2.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGFFsrekmkAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGTDVKA 82
Cdd:COG1123 4 LLEVRDLSVRYPGGDVP------AVDGVSLTIAPG--ETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VRSR-RDREAFMakvqpVFQNPFEAFNPLTRIDEylLATAHRFKGAkSRAEKEAIADVALQRVGLsmAEIKGRFSHELSG 161
Cdd:COG1123 76 LSEAlRGRRIGM-----VFQDPMTQLNPVTVGDQ--IAEALENLGL-SRAEARARVLELLEAVGL--ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1817161977 242 DARDVLEHPKH---AYSIALKNAVLPPNPREASAILRLRQ 278
Cdd:COG1123 226 PPEEILAAPQAlaaVPRLGAARGRAAPAAAAAEPLLEVRN 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-254 |
9.31e-58 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 188.77 E-value: 9.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLlELDHVTKLFpiGGFFsrekmkAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:COG3842 1 MAMPAL-ELENVSKRY--GDVT------ALDDVS--LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRSRRdREAFMakvqpVFQNP--------FE--AFnPLtrideyllatahRFKGAkSRAEKEAIADVALQRVGLS-MA 149
Cdd:COG3842 70 TGLPPEK-RNVGM-----VFQDYalfphltvAEnvAF-GL------------RMRGV-PKAEIRARVAELLELVGLEgLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 150 EikgRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRV 229
Cdd:COG3842 130 D---RYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRI 206
|
250 260
....*....|....*....|....*
gi 1817161977 230 VIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-271 |
1.73e-56 |
|
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: 183.08 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGFFSREKMKAV-DDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR 84
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRAPVlTNVS--LSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 sRRDREAFMAKVQPVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQL 164
Cdd:TIGR02769 80 -RKQRRAFRRDVQLVFQDSPSAVNPRMTV-RQIIGEPLRHLTSLDESEQKARIAELLDMVGLR-SEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
250 260
....*....|....*....|....*..
gi 1817161977 245 DVLEHpKHAYSIALKNAVLPPNPREAS 271
Cdd:TIGR02769 237 QLLSF-KHPAGRNLQSAVLPEHPVRRS 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-278 |
4.86e-56 |
|
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: 189.13 E-value: 4.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLLELDHVTKLFPIGGFFSRekmkAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILG----SEKADRGSIHFD 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVE----AVKGVSFDI--AAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 77 GTDV-----KAVRSRRDREAFMakvqpVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSMAEI 151
Cdd:COG4172 75 GQDLlglseRELRRIRGNRIAM-----IFQEPMTSLNPLHTI-GKQIAEVLRLHRGLSGAAARARALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 152 K-GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 230
Cdd:COG4172 149 RlDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 231 IMRKGVVVESGDARDVLEHPKHAYSIALKNA----VLPPNPREASAILRLRQ 278
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQHPYTRKLLAAeprgDPRPVPPDAPPLLEARD 280
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-272 |
1.46e-55 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 180.65 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGFFSREKMKAV-DDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVr 84
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHQHQTVlNNVSLSLKSG--ETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQL 164
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVRE-IIREPLRHLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVG 237
|
250 260
....*....|....*....|....*...
gi 1817161977 245 DVLeHPKHAYSIALKNAVLPPNPREASA 272
Cdd:PRK10419 238 DKL-TFSSPAGRVLQNAVLPAFPVRRRT 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-250 |
6.48e-53 |
|
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: 172.86 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGFfsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:COG1127 5 MIEVRNLTKSF--GDR------VVLDGVSLDV--PRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNP--------FE--AFnPLtrideyllatahRFKGAKSRAEKEAIADVALQRVGLSmaEIKGRF 155
Cdd:COG1127 74 EKELYELRRRIGMLFQGGalfdsltvFEnvAF-PL------------REHTDLSEAEIRELVLEKLELVGLP--GAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|....*
gi 1817161977 236 VVVESGDARDVLEHP 250
Cdd:COG1127 219 KIIAEGTPEELLASD 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-241 |
2.05e-52 |
|
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: 170.78 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03259 1 LELKGLSKTY--------GSVRALDDLS--LTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFmakvqpVFQNpFEAFNPLTRIDEylLATAHRFKGaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQR 166
Cdd:cd03259 71 RRNIGM------VFQD-YALFPHLTVAEN--IAFGLKLRG-VPKAEIRARVRELLELVGLE--GLLNRYPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-254 |
8.88e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.41 E-value: 8.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSshflLELDHVTKLFpiGGFfsrekmKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:COG1118 1 MS----IEVRNISKRF--GSF------TLLDDVSLEIASG--ELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRSRRDReafmaKVQPVFQNpfeafnpltrideYLLatahrFK----------GAK----SRAEKEAIADVALQRVGL 146
Cdd:COG1118 67 FTNLPPRER-----RVGFVFQH-------------YAL-----FPhmtvaeniafGLRvrppSKAEIRARVEELLELVQL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 147 SmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYIS 226
Cdd:COG1118 124 E--GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELA 201
|
250 260
....*....|....*....|....*...
gi 1817161977 227 DRVVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:COG1118 202 DRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-251 |
5.00e-51 |
|
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: 167.76 E-value: 5.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:cd03258 1 MIELKNVSKVFGDTG----GKVTALKDVS--LSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNpFEAFNPLTRID--EYLLATAHrfkgaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQ 163
Cdd:cd03258 74 GKELRKARRRIGMIFQH-FNLLSSRTVFEnvALPLEIAG-----VPKAEIEERVLELLELVGLE--DKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*...
gi 1817161977 244 RDVLEHPK 251
Cdd:cd03258 226 EEVFANPQ 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-253 |
7.62e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.64 E-value: 7.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:COG1135 2 IELENLSKTFPTKG----GPVTALDDVS--LTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAfMAKVQPVFQNpfeaFNpltrideyLLAT-------AHRFKGAK-SRAEKEAIADVALQRVGLSmaEIKGRFSHE 158
Cdd:COG1135 76 ELRAA-RRKIGMIFQH----FN--------LLSSrtvaenvALPLEIAGvPKAEIRKRVAELLELVGLS--DKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 159 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250
....*....|....*
gi 1817161977 239 ESGDARDVLEHPKHA 253
Cdd:COG1135 221 EQGPVLDVFANPQSE 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-239 |
1.30e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.37 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSShfLLELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:COG1136 1 MSP--LLELRNLTKSYGTGE----GEVTALRGVS--LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRS------RRDREAFmakvqpVFQNpfeaFNpltrideyLLAT---------AHRFKGaKSRAEKEAIADVALQRVG 145
Cdd:COG1136 73 SSLSErelarlRRRHIGF------VFQF----FN--------LLPEltalenvalPLLLAG-VSRKERRERARELLERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 146 LsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYi 225
Cdd:COG1136 134 L--GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR- 210
|
250
....*....|....
gi 1817161977 226 SDRVVIMRKGVVVE 239
Cdd:COG1136 211 ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-237 |
8.03e-50 |
|
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: 164.20 E-value: 8.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrEKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSR 86
Cdd:cd03255 1 IELKNLSKTYGGGG----EKVQALKGVSL--SIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAK-VQPVFQNpfeaFN--P-LTRIDEYLLATahRFKGaKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGG 162
Cdd:cd03255 74 KELAAFRRRhIGFVFQS----FNllPdLTALENVELPL--LLAG-VPKKERRERAEELLERVGL--GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 163 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVV 237
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-251 |
3.47e-49 |
|
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: 162.89 E-value: 3.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTklfpiggFFSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsR 86
Cdd:COG1122 1 IELENLS-------FSYPGGTPALDDVSLSIEKG--EFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT----K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNP----FE-------AFNPLTRideyllatahrfkgAKSRAEKEAIADVALQRVGLSmaEIKGRF 155
Cdd:COG1122 68 KNLRELRRKVGLVFQNPddqlFAptveedvAFGPENL--------------GLPREEIRERVEEALELVGLE--HLADRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|....*.
gi 1817161977 236 VVVESGDARDVLEHPK 251
Cdd:COG1122 211 RIVADGTPREVFSDYE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-268 |
2.69e-48 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 163.74 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKAD---RGSIHFDGTDV-----KAVRSRRDREAFMakvqpVF 100
Cdd:PRK09473 31 AVNDLNFSLRAG--ETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNKLRAEQISM-----IF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFEAFNPLTRIDEYLLATAHRFKG-AKSRAEKEAIAdvALQRVglSMAEIKGR---FSHELSGGQLQRIAVARALIPE 176
Cdd:PRK09473 104 QDPMTSLNPYMRVGEQLMEVLMLHKGmSKAEAFEESVR--MLDAV--KMPEARKRmkmYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 177 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSI 256
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSI 259
|
250
....*....|..
gi 1817161977 257 ALKNAVlppnPR 268
Cdd:PRK09473 260 GLLNAV----PR 267
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-239 |
4.07e-48 |
|
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: 159.94 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03293 1 LEVRNVSKTYGGGG----GAVTALEDISLSVEEG--EFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RdreAFMakvqpvFQNPfeAFNP-LTRIDEYLLATahRFKGAkSRAEKEAIADVALQRVGLSMAEikGRFSHELSGGQLQ 165
Cdd:cd03293 75 R---GYV------FQQD--ALLPwLTVLDNVALGL--ELQGV-PKAEARERAEELLELVGLSGFE--NAYPHQLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM--RKGVVVE 239
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-254 |
7.44e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 163.32 E-value: 7.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSShflLELDHVTKLFpiGGFfsrekmKAVDDVSFALsADKpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:COG3839 1 MAS---LELENVSKSY--GGV------EALKDIDLDI-EDG-EFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRSRrDREAFMakvqpVFQNP--------FE--AFnPLtrideyllatahRFKGAkSRAEKEAIADVALQRVGLSmaE 150
Cdd:COG3839 68 TDLPPK-DRNIAM-----VFQSYalyphmtvYEniAF-PL------------KLRKV-PKAEIDRRVREAAELLGLE--D 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 151 IKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 230
Cdd:COG3839 126 LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIA 205
|
250 260
....*....|....*....|....
gi 1817161977 231 IMRKGVVVESGDARDVLEHPKHAY 254
Cdd:COG3839 206 VMNDGRIQQVGTPEELYDRPANLF 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-235 |
1.01e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:COG1116 7 ALELRGVSKRFPTGG----GGVTALDDVSLTVAAG--EFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRdreAFmakvqpVFQNPfeafnpltrideYLL---------ATAHRFKGaKSRAEKEAIADVALQRVGLSMAEikGRFS 156
Cdd:COG1116 81 DR---GV------VFQEP------------ALLpwltvldnvALGLELRG-VPKAERRERARELLELVGLAGFE--DAYP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 157 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-248 |
1.79e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.69 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 86
Cdd:COG1131 1 IEVRGLTKRY--GDK------TALDGVSL--TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-----A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNPfeAFNPLTRIDEYLLATAhRFKGAKSRAEKEAIADVaLQRVGLsmAEIKGRFSHELSGGQLQR 166
Cdd:COG1131 66 RDPAEVRRRIGYVPQEP--ALYPDLTVRENLRFFA-RLYGLPRKEARERIDEL-LELFGL--TDAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 246
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
..
gi 1817161977 247 LE 248
Cdd:COG1131 219 KA 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-252 |
6.51e-47 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 158.41 E-value: 6.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSREKMKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK--- 81
Cdd:PRK15112 4 LLEVRNLSKTFRYrTGWFRRQTVEAVKPLSFTLREGQ--TLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 -AVRSRRDREafmakvqpVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRFSHELS 160
Cdd:PRK15112 82 ySYRSQRIRM--------IFQDPSTSLNPRQRISQ-ILDFPLRLNTDLEPEQREKQIIETLRQVGL-LPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 240
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|..
gi 1817161977 241 GDARDVLEHPKH 252
Cdd:PRK15112 232 GSTADVLASPLH 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-251 |
1.35e-46 |
|
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: 156.24 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 86
Cdd:cd03300 1 IELENVSKFY--GGF------VALDGVSLDI--KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rdrEAFMAKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQR 166
Cdd:cd03300 68 ---PPHKRPVNTVFQN-YALFPHLTVFEN--IAFGLRLKK-LPKAEIKERVAEALDLVQLE--GYANRKPSQLSGGQQQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 246
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
....*
gi 1817161977 247 LEHPK 251
Cdd:cd03300 219 YEEPA 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-253 |
4.71e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.46 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGFfsrekmKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrS 85
Cdd:COG1126 1 MIEIENLHKSF--GDL------EVLKGIS--LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD--S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLA--TAHRfkgaKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQ 163
Cdd:COG1126 69 KKDINKLRRKVGMVFQQ-FNLFPHLTVLENVTLApiKVKK----MSKAEAEERAMELLERVGL--ADKADAYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
250
....*....|
gi 1817161977 244 RDVLEHPKHA 253
Cdd:COG1126 221 EEFFENPQHE 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-247 |
1.57e-44 |
|
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: 151.73 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTklfpiggfFSREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:COG1120 1 MLEAENLS--------VGYGGRPVLDDVSLSL--PPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVqpvFQNPFEAFnPLTRIDEYLLA-TAHRFKGAKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQL 164
Cdd:COG1120 70 RRELARRIAYV---PQEPPAPF-GLTVRELVALGrYPHLGLFGRPSAEDREAVEEALERTGL--EHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
...
gi 1817161977 245 DVL 247
Cdd:COG1120 224 EVL 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
29-263 |
1.73e-44 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 150.98 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILG----SEKADRGSIHFDGTDVKAVrSRRDREAFMakvqpVFQNPF 104
Cdd:TIGR02770 1 LVQDLNL--SLKRGEVLALVGESGSGKSLTCLAILGllppGLTQTSGEILLDGRPLLPL-SIRGRHIAT-----IMQNPR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 EAFNPLTRIDEYLLATAhRFKGAKSRAEKEAIADvALQRVGL-SMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:TIGR02770 73 TAFNPLFTMGNHAIETL-RSLGKLSKQARALILE-ALEAVGLpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 184 EPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKNAVL 263
Cdd:TIGR02770 151 EPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAHL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-254 |
1.74e-44 |
|
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: 151.34 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSR 86
Cdd:cd03296 3 IEVRNVSKRF--GDF------VALDDVSLDIPSG--ELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREafmakVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADVA---LQRVGLSMAEikGRFSHELSGGQ 163
Cdd:cd03296 72 QERN-----VGFVFQH-YALFRHMTVFDN--VAFGLRVKPRSERPPEAEIRAKVhelLKLVQLDWLA--DRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
250
....*....|.
gi 1817161977 244 RDVLEHPKHAY 254
Cdd:cd03296 222 DEVYDHPASPF 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-235 |
6.19e-44 |
|
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: 147.72 E-value: 6.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsreKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSR 86
Cdd:cd03229 1 LELKNVSKRYG--------QKTVLNDVSLNIEAG--EIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLAtahrfkgaksraekeaiadvalqrvglsmaeikgrfsheLSGGQLQR 166
Cdd:cd03229 69 DELPPLRRRIGMVFQD-FALFPHLTVLENIALG---------------------------------------LSGGQQQR 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:cd03229 109 VALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-254 |
1.53e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 150.63 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 8 ELDHVTKLFPiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK---AVR 84
Cdd:COG1125 3 EFENVTKRYP-------DGTVAVDDLS--LTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRdldPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDreafMAKV-Q-----P---VFQNpfeafnpltrideylLATAHRFKGaKSRAEKEAIADVALQRVGLSMAEIKGRF 155
Cdd:COG1125 74 LRRR----IGYViQqiglfPhmtVAEN---------------IATVPRLLG-WDKERIRARVDELLELVGLDPEEYRDRY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:COG1125 134 PHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
250
....*....|....*....
gi 1817161977 236 VVVESGDARDVLEHPKHAY 254
Cdd:COG1125 214 RIVQYDTPEEILANPANDF 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-250 |
1.80e-43 |
|
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: 148.60 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiGGFfsrekmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA---V 83
Cdd:cd03295 1 IEFENVTKRYG-GGK------KAVNNLNL--EIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 RSRRdreafmaKVQPVFQNPfeAFNPLTRIDEYLlATAHRFKGAkSRAEKEAIADVALQRVGLSMAEIKGRFSHELSGGQ 163
Cdd:cd03295 72 ELRR-------KIGYVIQQI--GLFPHMTVEENI-ALVPKLLKW-PKEKIRERADELLALVGLDPAEFADRYPHELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
....*..
gi 1817161977 244 RDVLEHP 250
Cdd:cd03295 221 DEILRSP 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-254 |
2.12e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.31 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLLELDHVTklfpiggfFSREKMKAVDDVSFALSAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:COG1121 1 MMMMPAIELENLT--------VSYGGRPVLEDVSLTIPP--GEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRSRrdreafMAKVqPvfQNpfEAFN---PLTRIDeyLLAT----AHRFKGAKSRAEKEAIADvALQRVGlsMAEIKG 153
Cdd:COG1121 71 RRARRR------IGYV-P--QR--AEVDwdfPITVRD--VVLMgrygRRGLFRRPSRADREAVDE-ALERVG--LEDLAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 154 RFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMR 233
Cdd:COG1121 135 RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN 213
|
250 260
....*....|....*....|...
gi 1817161977 234 KGVVVeSGDARDVL--EHPKHAY 254
Cdd:COG1121 214 RGLVA-HGPPEEVLtpENLSRAY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-235 |
2.81e-43 |
|
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: 147.23 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNP---F 104
Cdd:cd03225 15 PALDDISLTI--KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR----KVGLVFQNPddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 eaFNPLTRiDEylLATAHRFKGaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADE 184
Cdd:cd03225 89 --FGPTVE-EE--VAFGLENLG-LPEEEIEERVEEALELVGLE--GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 185 PVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-258 |
7.44e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 153.71 E-value: 7.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSR--EKMKAVDDVSFALSADkpEIFTIVGESGSGKST----LAKMIlgsekADRGSIHFDGT 78
Cdd:PRK15134 275 LLDVEQLQVAFPIrKGILKRtvDHNVVVKNISFTLRPG--ETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 79 DVKAvRSRRDREAFMAKVQPVFQNPFEAFNP---LTRIDEYLLATAHRFKGAKSRaEKEAIAdvALQRVGLSmAEIKGRF 155
Cdd:PRK15134 348 PLHN-LNRRQLLPVRHRIQVVFQDPNSSLNPrlnVLQIIEEGLRVHQPTLSAAQR-EQQVIA--VMEEVGLD-PETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250 260
....*....|....*....|...
gi 1817161977 236 VVVESGDARDVLEHPKHAYSIAL 258
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEYTRQL 525
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-254 |
1.40e-41 |
|
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: 144.71 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLF----------PIGGFFSREKMK------AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADR 70
Cdd:cd03294 1 IKIKGLYKIFgknpqkafklLAKGKSKEEILKktgqtvGVNDVSLDVREG--EIFVIMGLSGSGKSTLLRCINRLIEPTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 71 GSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNpFEAFNPLTRID--EYLLATAHRfkgakSRAEKEAIADVALQRVGLsm 148
Cdd:cd03294 79 GKVLIDGQDIAAMSRKELRELRRKKISMVFQS-FALLPHRTVLEnvAFGLEVQGV-----PRAEREERAAEALELVGL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 149 AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDR 228
Cdd:cd03294 151 EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDR 230
|
250 260
....*....|....*....|....*.
gi 1817161977 229 VVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:cd03294 231 IAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-251 |
2.35e-41 |
|
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: 142.96 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03219 1 LEVRGLTKRF--GGL------VALDDVSF--SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKvqpVFQNPfEAFNPLTRIDEYLLA----TAHRFKGAKSRAEKEAI---ADVALQRVGLsmAEIKGRFSHEL 159
Cdd:cd03219 71 EIARLGIGR---TFQIP-RLFPELTVLENVMVAaqarTGSGLLLARARREEREArerAEELLERVGL--ADLADRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVE 239
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 1817161977 240 SGDARDVLEHPK 251
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-278 |
2.63e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 149.47 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 2 SSHFLLELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKAD-----RGSIHFD 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQ----TVRTVVNDVS--LQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 77 GTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAIADvALQRVGLSMAeiKGR-- 154
Cdd:PRK15134 75 GESLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILN-CLDRVGIRQA--AKRlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 -FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMR 233
Cdd:PRK15134 152 dYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1817161977 234 KGVVVESGDARDVLEHPKHAYSIALKNA----VLPPNPREASAILRLRQ 278
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHPYTQKLLNSepsgDPVPLPEPASPLLDVEQ 280
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-249 |
3.52e-41 |
|
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: 143.34 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:TIGR04520 1 IEVENVSFSYP------ESEKPALKNVSL--SIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RD-REafmaKVQPVFQNP---F-----E---AFNPltridEYLlatahrfkgAKSRAEKEAIADVALQRVGlsMAEIKGR 154
Cdd:TIGR04520 73 WEiRK----KVGMVFQNPdnqFvgatvEddvAFGL-----ENL---------GVPREEMRKRVDEALKLVG--MEDFRDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRK 234
Cdd:TIGR04520 133 EPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNK 211
|
250
....*....|....*
gi 1817161977 235 GVVVESGDARDVLEH 249
Cdd:TIGR04520 212 GKIVAEGTPREIFSQ 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-267 |
3.83e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 150.39 E-value: 3.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 82
Cdd:PRK10261 313 ILQVRNLVTRFPLrSGLLNRVTreVHAVEKVSFDLWPG--ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VrSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLAT--AHRFKGAKSRAEKEAIAdvaLQRVGLsMAEIKGRFSHELS 160
Cdd:PRK10261 391 L-SPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPlrVHGLLPGKAAAARVAWL---LERVGL-LPEHAWRYPHEFS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 240
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
250 260
....*....|....*....|....*..
gi 1817161977 241 GDARDVLEHPKHAYSIALKNAVLPPNP 267
Cdd:PRK10261 546 GPRRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-246 |
8.59e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.73 E-value: 8.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiGGFfsrekmKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:COG3638 2 MLELRNLSKRYP-GGT------PALDDVS--LEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDReAFMAKVQPVFQNpfeaFN---PLTRIDEYLLATAHRFKGAKS------RAEKEAIADvALQRVGLS-MAEIKgrf 155
Cdd:COG3638 73 RALR-RLRRRIGMIFQQ----FNlvpRLSVLTNVLAGRLGRTSTWRSllglfpPEDRERALE-ALERVGLAdKAYQR--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVIMR 233
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHqvDLARRY--ADRIIGLR 221
|
250
....*....|...
gi 1817161977 234 KGVVVESGDARDV 246
Cdd:COG3638 222 DGRVVFDGPPAEL 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-241 |
2.56e-40 |
|
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: 139.70 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsreKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03301 1 VELENVTKRFG--------NVTALDDLN--LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDREAFMakvqpVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADVALQrvgLSMAEIKGRFSHELSGGQLQR 166
Cdd:cd03301 71 -DRDIAM-----VFQN-YALYPHMTVYDN--IAFGLKLRKVPKDEIDERVREVAEL---LQIEHLLDRKPKQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-246 |
2.86e-40 |
|
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: 140.40 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrekmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-----K 81
Cdd:cd03256 1 IEVENLSKTYPNGK-------KALKDVSL--SINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 AVRSRRDREAFmakvqpVFQNpFEAFNPLTRIDEYL---LATAHRFKGAK---SRAEKEaIADVALQRVGLS-MAEIKgr 154
Cdd:cd03256 72 ALRQLRRQIGM------IFQQ-FNLIERLSVLENVLsgrLGRRSTWRSLFglfPKEEKQ-RALAALERVGLLdKAYQR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 fSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVIM 232
Cdd:cd03256 142 -ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHqvDLAREY--ADRIVGL 218
|
250
....*....|....
gi 1817161977 233 RKGVVVESGDARDV 246
Cdd:cd03256 219 KDGRIVFDGPPAEL 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-263 |
6.14e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 141.97 E-value: 6.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEK------ADRgsIHFDGTDVKAVrSRRDREAFMAK-VQP 98
Cdd:COG4170 19 RVKAVDRVSLTLNEG--EIRGLVGESGSGKSLIAKAICGITKdnwhvtADR--FRWNGIDLLKL-SPRERRKIIGReIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQNPFEAFNPLTRIDEYLLAT--AHRFKG-----AKSRAeKEAIAdvALQRVGLSMAE-IKGRFSHELSGGQLQRIAVA 170
Cdd:COG4170 94 IFQEPSSCLDPSAKIGDQLIEAipSWTFKGkwwqrFKWRK-KRAIE--LLHRVGIKDHKdIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 171 RALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
250
....*....|...
gi 1817161977 251 KHAYSIALKNAVL 263
Cdd:COG4170 251 HHPYTKALLRSMP 263
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-254 |
1.37e-39 |
|
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: 139.02 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGFfsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:COG0411 4 LLEVRGLTKRF--GGL------VAVDDVSLEV--ERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVqpvFQNPfEAFNPLT-----------RIDEYLLATAHRFKGAKsRAEKEAIADV--ALQRVGLsmAEIK 152
Cdd:COG0411 74 HRIARLGIART---FQNP-RLFPELTvlenvlvaahaRLGRGLLAALLRLPRAR-REEREARERAeeLLERVGL--ADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 153 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM 232
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
250 260
....*....|....*....|....
gi 1817161977 233 RKGVVVESGDARDVLEHPKH--AY 254
Cdd:COG0411 227 DFGRVIAEGTPAEVRADPRVieAY 250
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-250 |
1.48e-39 |
|
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: 138.40 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGffsrekmKAV-DDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:cd03261 1 IELRGLTKSF--GG-------RTVlKGVD--LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNPfeA-FNPLTRID--EYLLatahRFKGAKSRAEKEAIADVALQRVGLSMAEIKgrFSHELSGG 162
Cdd:cd03261 69 EAELYRLRRRMGMLFQSG--AlFDSLTVFEnvAFPL----REHTRLSEEEIREIVLEKLEAVGLRGAEDL--YPAELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 163 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 242
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....*...
gi 1817161977 243 ARDVLEHP 250
Cdd:cd03261 221 PEELRASD 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-241 |
1.97e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsR 86
Cdd:COG2884 2 IRFENVSKRYPGGR-------EALSDVSLEI--EKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQ--------NPFE--AFnPLtrideyllatahRFKGAKSRAEKEAIADVaLQRVGLSmaEIKGRFS 156
Cdd:COG2884 72 REIPYLRRRIGVVFQdfrllpdrTVYEnvAL-PL------------RVTGKSRKEIRRRVREV-LDLVGLS--DKAKALP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 157 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGV 236
Cdd:COG2884 136 HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
....*
gi 1817161977 237 VVESG 241
Cdd:COG2884 215 LVRDE 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-251 |
3.86e-39 |
|
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: 137.08 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFmakvqpVFQNpFEAFNP 109
Cdd:cd03299 15 LKNVSL--EVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISY------VPQN-YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRID--EYLLATAHRFKGAKSRAEKEaIADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:cd03299 86 MTVYKniAYGLKKRKVDKKEIERKVLE-IAEM------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-264 |
1.66e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 137.95 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFalSADKPEIFTIVGESGSGKS--TLAKMIL----GSEKADRgsIHFDGTDVKAVRSRRDREAFMAKVQPVFQ 101
Cdd:PRK11022 21 RAVDRISY--SVKQGEVVGIVGESGSGKSvsSLAIMGLidypGRVMAEK--LEFNGQDLQRISEKERRNLVGAEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NPFEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAIADVaLQRVGLSMAEIK-GRFSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK11022 97 DPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDL-LNQVGIPDPASRlDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKN 260
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
....
gi 1817161977 261 AvLP 264
Cdd:PRK11022 256 A-LP 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-265 |
1.80e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 136.21 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLLELDHVTKLFpiGGFfsrekmKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY--GPR------KGCRDVSFDLYPG--EVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 K----AVRSRRDREAFM----AKVQpvfQNPFEAFNPLT----RIDEYLLATAHRFKGaKSRAEkeaiADVALQRVGLSM 148
Cdd:PRK11701 71 QlrdlYALSEAERRRLLrtewGFVH---QHPRDGLRMQVsaggNIGERLMAVGARHYG-DIRAT----AGDWLERVEIDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 149 AEIKGRFShELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDR 228
Cdd:PRK11701 143 ARIDDLPT-TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHR 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 1817161977 229 VVIMRKGVVVESGDARDVLEHPKHAYSIALKNAVLPP 265
Cdd:PRK11701 222 LLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-251 |
1.91e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 138.70 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLlELDHVTKLFpiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:PRK11432 2 TQKNFV-VLKNITKRF--------GSNTVIDNLN--LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAvRSRRDREAFMakvqpVFQNpfEAFNPLTRIDE---YLLATAHRFKGAKSRAEKEAIADVALqrvglsmAEIKGRFSH 157
Cdd:PRK11432 71 TH-RSIQQRDICM-----VFQS--YALFPHMSLGEnvgYGLKMLGVPKEERKQRVKEALELVDL-------AGFEDRYVD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 158 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
250
....*....|....
gi 1817161977 238 VESGDARDVLEHPK 251
Cdd:PRK11432 216 MQIGSPQELYRQPA 229
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-254 |
5.63e-38 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 134.16 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:TIGR00968 1 IEIANISKRF--GSF------QALDDVNLEVPTGS--LVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFmakvqpVFQNpFEAFNPLTRIDEYLLATAHRfkgAKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQR 166
Cdd:TIGR00968 71 DRKIGF------VFQH-YALFKHLTVRDNIAFGLEIR---KHPKAKIKARVEELLELVQLE--GLGDRYPNQLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 246
Cdd:TIGR00968 139 VALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
....*...
gi 1817161977 247 LEHPKHAY 254
Cdd:TIGR00968 219 YDHPANPF 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-246 |
5.84e-38 |
|
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: 133.85 E-value: 5.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKAVRSrrDREAFMAKV 96
Cdd:cd03260 8 VYYGDKHALKDISLDIPKG--EITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDV--DVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QPVFQ--NPFeafnPLTRIDEylLATAHRFKGAKSRAEKEAIADVALQRVGLSmAEIKGRFS-HELSGGQLQRIAVARAL 173
Cdd:cd03260 84 GMVFQkpNPF----PGSIYDN--VAYGLRLHGIKLKEELDERVEEALRKAALW-DEVKDRLHaLGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 174 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 246
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-254 |
1.56e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 136.32 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpigGFFSrekmkAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS- 85
Cdd:TIGR03265 5 LSIDNIRKRF---GAFT-----ALKDISLSVK--KGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAfmakvqpVFQNpFEAFNPLTRID--EYLLATahrfKGAKsRAEKEAIADVALQRVGLSMAEIKgrFSHELSGGQ 163
Cdd:TIGR03265 75 KRDYGI-------VFQS-YALFPNLTVADniAYGLKN----RGMG-RAEVAERVAELLDLVGLPGSERK--YPGQLSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:TIGR03265 140 QQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
250
....*....|.
gi 1817161977 244 RDVLEHPKHAY 254
Cdd:TIGR03265 220 QEIYRHPATPF 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-250 |
2.14e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.91 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--- 82
Cdd:PRK09493 1 MIEFKNVSKHF--------GPTQVLHNID--LNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 -VRSRRdREAFMakvqpVFQNpFEAFNPLTRIDEYLLATAHrFKGAkSRAEKEAIADVALQRVGLsmAEIKGRFSHELSG 161
Cdd:PRK09493 71 dERLIR-QEAGM-----VFQQ-FYLFPHLTALENVMFGPLR-VRGA-SKEEAEKQARELLAKVGL--AERAHHYPSELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
....*....
gi 1817161977 242 DARDVLEHP 250
Cdd:PRK09493 219 DPQVLIKNP 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-237 |
2.21e-37 |
|
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: 131.88 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrSR 86
Cdd:cd03262 1 IEIKNLHKSF--GDF------HVLKGID--LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLATAHRFKgaKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQR 166
Cdd:cd03262 69 KNINELRQKVGMVFQQ-FNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGL--ADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDL-RDALNVSIVyiTHDLATAYYISDRVVIMRKGVV 237
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVV--THEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-237 |
2.36e-37 |
|
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: 130.60 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsreKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsr 86
Cdd:cd03230 1 IEVRNLSKRYG--------KKTALDDISLTV--EKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNP--FEAFNPLtridEYLlatahrfkgaksraekeaiadvalqrvglsmaeikgrfshELSGGQL 164
Cdd:cd03230 66 KEPEEVKRRIGYLPEEPslYENLTVR----ENL----------------------------------------KLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-241 |
2.42e-37 |
|
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: 130.63 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrdreafmakvqpvfq 101
Cdd:cd03214 7 VGYGGRTVLDDLSL--SIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 npfeafnpltrideyllatahrfkGAKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:cd03214 67 ------------------------SPKELARKIAYVPQALELLGL--AHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
29-237 |
3.87e-37 |
|
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: 131.12 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKvqpvfqnpFEAFN 108
Cdd:cd03235 14 VLEDVSFEV--KPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---KPLEKERKRIGYVPQ--------RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 ---PLTRIDEYLLA-TAHRFKGAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADE 184
Cdd:cd03235 81 rdfPISVRDVVLMGlYGHKGLFRRLSKADKAKVDEALERVG--LSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 185 PVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-253 |
5.60e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.54 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 8 ELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSRR 87
Cdd:PRK11153 3 ELKNISKVFPQGG----RTIHALNNVS--LHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAL-SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 88 DREAFMAKVQPVFQNpfeaFNPL---TRIDEylLATAHRFKGaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQL 164
Cdd:PRK11153 76 ELRKARRQIGMIFQH----FNLLssrTVFDN--VALPLELAG-TPKAEIKARVTELLELVGLS--DKADRYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
....*....
gi 1817161977 245 DVLEHPKHA 253
Cdd:PRK11153 227 EVFSHPKHP 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-248 |
5.78e-37 |
|
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: 131.90 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiggffsrEKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrs 85
Cdd:COG4555 1 MIEVENLSKKY--------GKVPALKDVSF--TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNpFEAFNPLTrIDEYLLATAhRFKGAKSRAEKEAIADVaLQRVGLSmaEIKGRFSHELSGGQLQ 165
Cdd:COG4555 66 RKEPREARRQIGVLPDE-RGLYDRLT-VRENIRYFA-ELYGLFDEELKKRIEEL-IELLGLE--EFLDRRVGELSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 245
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
...
gi 1817161977 246 VLE 248
Cdd:COG4555 219 LRE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-241 |
7.50e-37 |
|
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: 130.49 E-value: 7.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADKPEIFT-IVGESGSGKSTLAKMILGSEKADRGSIHFDGT-----DVKAVRSRRDReafmaKVQPVFQ 101
Cdd:cd03297 8 KRLPDFTLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQR-----KIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NpfEAFNPLTRIDEYLLATAHRfkgaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:cd03297 83 Q--YALFPHLNVRENLAFGLKR----KRNREDRISVDELLDLLGLD--HLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-251 |
1.72e-36 |
|
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: 131.42 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFFSRekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSR 86
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEK---KALDDVSLTI--EDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA-KKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNP----FE-------AFNPltrideyllataHRFKGAKSRAEKEAIAdvALQRVGLSmAEIKGRF 155
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQFPehqlFEetvykdiAFGP------------KNLGLSEEEAEERVKE--ALELVGLD-EEYLERS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:TIGR04521 140 PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
250
....*....|....*.
gi 1817161977 236 VVVESGDARDVLEHPK 251
Cdd:TIGR04521 220 KIVLDGTPREVFSDVD 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-249 |
5.21e-36 |
|
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: 129.34 E-value: 5.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsrekMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:TIGR02315 1 MLEVENLSKVYPNG-------KQALKNINLNIN--PGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAfMAKVQPVFQNpFEAFNPLTRIDEYLlataHRFKGAK----------SRAEKEaIADVALQRVGLS-MAEIKgr 154
Cdd:TIGR02315 72 KKLRKL-RRRIGMIFQH-YNLIERLTVLENVL----HGRLGYKptwrsllgrfSEEDKE-RALSALERVGLAdKAYQR-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 fSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVIM 232
Cdd:TIGR02315 143 -ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHqvDLAKKY--ADRIVGL 219
|
250
....*....|....*..
gi 1817161977 233 RKGVVVESGDARDVLEH 249
Cdd:TIGR02315 220 KAGEIVFDGAPSELDDE 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-254 |
5.91e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 132.38 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:PRK09452 14 LVELRGISKSF--------DGKEVISNLD--LTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 -RRDreafmakVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADvALQRVGLS-MAEikgRFSHELSGGQ 163
Cdd:PRK09452 84 eNRH-------VNTVFQS-YALFPHMTVFEN--VAFGLRMQKTPAAEITPRVME-ALRMVQLEeFAQ---RKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
250
....*....|.
gi 1817161977 244 RDVLEHPKHAY 254
Cdd:PRK09452 230 REIYEEPKNLF 240
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-255 |
3.19e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 129.54 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrdrEAFMAKVQPVFQNpfEAFNPLTRIDEYLlATAHRFKG 126
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV------PPHLRHINMVFQS--YALFPHMTVEENV-AFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 127 AkSRAEKEAIADVALQRVglSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRD 206
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLV--QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1817161977 207 ALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYS 255
Cdd:TIGR01187 149 QLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFV 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-250 |
5.61e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.43 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKlfpiggFFSREKMkaVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:PRK10851 3 IEIANIKK------SFGRTQV--LNDIS--LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDReafmaKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADVALQRvgLSM---AEIKGRFSHELSGGQ 163
Cdd:PRK10851 73 -DR-----KVGFVFQH-YALFRHMTVFDN--IAFGLTVLPRRERPNAAAIKAKVTQL--LEMvqlAHLADRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
....*..
gi 1817161977 244 RDVLEHP 250
Cdd:PRK10851 222 DQVWREP 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
28-263 |
7.99e-35 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 126.48 E-value: 7.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREA---FMAKVQ--PVFQN 102
Cdd:TIGR02323 17 KGCRDVSFDLYPG--EVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAerrRLMRTEwgFVHQN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 PFEAF----NPLTRIDEYLLATAHRFKGaKSRAEkeaiADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARALIPEPK 178
Cdd:TIGR02323 95 PRDGLrmrvSAGANIGERLMAIGARHYG-NIRAT----AQDWLEEVEIDPTRIDDLPR-AFSGGMQQRLQIARNLVTRPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 179 LIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIAL 258
Cdd:TIGR02323 169 LVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLL 248
|
....*
gi 1817161977 259 KNAVL 263
Cdd:TIGR02323 249 VSSIL 253
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-185 |
8.10e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 123.14 E-value: 8.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPFeaFNP 109
Cdd:pfam00005 1 LKNVSLTLNPG--EILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL----TDDERKSLRKEIGYVFQDPQ--LFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 110 LTRIDEYLLATAHRFkgAKSRAEKEAIADVALQRVGLS--MAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEP 185
Cdd:pfam00005 73 RLTVRENLRLGLLLK--GLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-255 |
8.18e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.57 E-value: 8.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiggffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrs 85
Cdd:PRK11607 19 LLEIRNLTKSF--------DGQHAVDDVS--LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 rrdreafmakvqPVFQNPFE------AFNPLTRIDEYLlatahRFKGAKSRAEKEAIADVALQRVGL-SMAEIKGRFSHE 158
Cdd:PRK11607 87 ------------PPYQRPINmmfqsyALFPHMTVEQNI-----AFGLKQDKLPKAEIASRVNEMLGLvHMQEFAKRKPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 159 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
250
....*....|....*..
gi 1817161977 239 ESGDARDVLEHPKHAYS 255
Cdd:PRK11607 230 QIGEPEEIYEHPTTRYS 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-238 |
2.08e-34 |
|
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: 122.54 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsr 86
Cdd:cd03216 1 LELRGITKRF--GGV------KALDGVSLSV--RRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rdreafmakvqpvFQNPFEAfnpltrideyllatahrfkgaksraekeaiadvalQRVGLSMAeikgrfsHELSGGQLQR 166
Cdd:cd03216 66 -------------FASPRDA-----------------------------------RRAGIAMV-------YQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-249 |
2.54e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiggffsREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDG-----TDV 80
Cdd:PRK13635 5 IIRVEHISFRYP------DAATYALKDVSF--SVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRsrrdreafmAKVQPVFQNPFEAFNPLTRIDEYLLATAHRfkgAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELS 160
Cdd:PRK13635 77 WDVR---------RQVGMVFQNPDNQFVGATVQDDVAFGLENI---GVPREEMVERVDQALRQVG--MEDFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVES 240
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
....*....
gi 1817161977 241 GDARDVLEH 249
Cdd:PRK13635 222 GTPEEIFKS 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-277 |
3.52e-34 |
|
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: 127.14 E-value: 3.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFALSAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDreafmakVQP-------VFQnpf 104
Cdd:COG4148 17 DVDFTLPG--RGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIF-------LPPhrrrigyVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 EA--FNPLTrIDEYLLATAHRFKGAKSRAEKEAIADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVA 182
Cdd:COG4148 85 EArlFPHLS-VRGNLLYGRKRAPRAERRISFDEVVEL------LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 183 DEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPkhaysialknAV 262
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP----------DL 227
|
250
....*....|....*.
gi 1817161977 263 LPPNP-REASAILRLR 277
Cdd:COG4148 228 LPLAGgEEAGSVLEAT 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
27-268 |
6.79e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 126.07 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 27 MKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEK------ADRgsIHFDGTDVKAVRSRRDREAFMAKVQPVF 100
Cdd:PRK15093 20 VKAVDRVSMTLT--EGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtADR--MRFDDIDLLRLSPRERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFEAFNPLTRIDEYLLATA----------HRFKGAKSRAEKeaiadvALQRVGL-SMAEIKGRFSHELSGGQLQRIAV 169
Cdd:PRK15093 96 QEPQSCLDPSERVGRQLMQNIpgwtykgrwwQRFGWRKRRAIE------LLHRVGIkDHKDAMRSFPYELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 170 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
250 260
....*....|....*....|....*
gi 1817161977 250 PKHAYSIALKNAV------LPPNPR 268
Cdd:PRK15093 250 PHHPYTQALIRAIpdfgsaMPHKSR 274
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-241 |
4.41e-33 |
|
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: 121.07 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFfsrekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 86
Cdd:cd03263 1 LQIRNLTKTYKKGTK------PAVDDLSLNV--YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQnpfeaFNPLtriDEYLLATAH-----RFKGaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSG 161
Cdd:cd03263 68 TDRKAARQSLGYCPQ-----FDAL---FDELTVREHlrfyaRLKG-LPKSEIKEEVELLLRVLGLT--DKANKRARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-246 |
5.65e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 5.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPigGFfsrekmKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRS 85
Cdd:COG1129 4 LLEMRGISKSFG--GV------KALDGVSLELRPG--EVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQ--NPFEAfnpLTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSM---AEIKgrfshELS 160
Cdd:COG1129 71 RSPRDAQAAGIAIIHQelNLVPN---LSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIdpdTPVG-----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASlrmSIVNLF---RDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTER---EVERLFriiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 1817161977 238 VESGDARDV 246
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-235 |
6.63e-33 |
|
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: 118.50 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmakvqpvfq 101
Cdd:cd00267 7 FRYGGRTALDNVSLTL--KAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 npfeafnpltrideyllatahrfkgaksraekeaiadvalQRVGlsmaeikgrFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:cd00267 73 ----------------------------------------RRIG---------YVPQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-258 |
9.96e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsREKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGTDVKAV 83
Cdd:PRK13640 6 VEFKHVSFTYP------DSKKPALNDISFSIP--RGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 RSRRDREafmaKVQPVFQNPFEAFNPLTRIDEYLLATAHRfkgAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQ 163
Cdd:PRK13640 78 TVWDIRE----KVGIVFQNPDNQFVGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVG--MLDYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVVESGDA 243
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSP 227
|
250
....*....|....*
gi 1817161977 244 RDVLEHPKHAYSIAL 258
Cdd:PRK13640 228 VEIFSKVEMLKEIGL 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-262 |
2.07e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 125.74 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDG-------------TDVKAVRSRRDRE 90
Cdd:PRK10261 26 QQKIAAVRNLSFSLQ--RGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 91 AFMAKVqpvFQNPFEAFNPLTRIDEYLlATAHRFKGAKSRAEKEAIADVALQRVGLSMAE-IKGRFSHELSGGQLQRIAV 169
Cdd:PRK10261 104 ADMAMI---FQEPMTSLNPVFTVGEQI-AESIRLHQGASREEAMVEAKRMLDQVRIPEAQtILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 170 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
250
....*....|...
gi 1817161977 250 PKHAYSIALKNAV 262
Cdd:PRK10261 260 PQHPYTRALLAAV 272
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-258 |
2.09e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADKPEifTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNPFEAFn 108
Cdd:PRK13648 24 TLKDVSFNIPKGQWT--SIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK----HIGIVFQNPDNQF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 pLTRIDEYLLATAHRfKGAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK13648 97 -VGSIVKYDVAFGLE-NHAVPYDEMHRRVSEALKQVD--MLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 189 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYSIAL 258
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGL 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-248 |
4.17e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQ 101
Cdd:PRK13632 17 YPNSENNALKNVSFEI--NEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK----KIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NPFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADVAlQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:PRK13632 91 NPDNQFIGATVEDD--IAFGLENKKVPPKKMKDIIDDLA-KKVG--MEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-249 |
1.77e-31 |
|
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: 122.94 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFfsrekmkAVDDVSFALSAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 86
Cdd:COG4988 337 IELEDVSFSYPGGRP-------ALDGLSLTIPP--GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDREAFMAKVQPVFQNPfeafnpltrideYLlatahrFKG--------AKSRAEKEAIADvALQRVGLS---------MA 149
Cdd:COG4988 405 -DPASWRRQIAWVPQNP------------YL------FAGtirenlrlGRPDASDEELEA-ALEAAGLDefvaalpdgLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 150 EIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAyYISDRV 229
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALL-AQADRI 541
|
250 260
....*....|....*....|
gi 1817161977 230 VIMRKGVVVESGDARDVLEH 249
Cdd:COG4988 542 LVLDDGRIVEQGTHEELLAK 561
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-253 |
2.58e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmkavdDVSFALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR-S 85
Cdd:COG3840 2 LRLDDLTYRY--GDF----------PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRdreafmaKVQPVFQ--NPFE----------AFNPLTRIdeyllatahrfkgakSRAEKEAIADvALQRVGLsmAEIKG 153
Cdd:COG3840 70 ER-------PVSMLFQenNLFPhltvaqniglGLRPGLKL---------------TAEQRAQVEQ-ALERVGL--AGLLD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 154 RFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMR 233
Cdd:COG3840 125 RLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVA 204
|
250 260
....*....|....*....|
gi 1817161977 234 KGVVVESGDARDVLEHPKHA 253
Cdd:COG3840 205 DGRIAADGPTAALLDGEPPP 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-251 |
2.95e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 117.21 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDdvsfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR------DR---EA 91
Cdd:COG4598 18 FGDLEVLKGVS-----LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpaDRrqlQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 92 FMAKVQPVFQNpfeaFN---PLTRIDEYLLATAHRFKgaKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQRIA 168
Cdd:COG4598 93 IRTRLGMVFQS----FNlwsHMTVLENVIEAPVHVLG--RPKAEAIERAEALLAKVGL--ADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 169 VARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
...
gi 1817161977 249 HPK 251
Cdd:COG4598 244 NPK 246
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-243 |
3.40e-31 |
|
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: 116.38 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 2 SSHFLLELDHVTKLFPIGgffsREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTG----AGELTILKGISLEVEAG--ESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 AV------RSRRDREAFmakvqpVFQNpFEAFNPLTRIDEYL----LATAhrfKGAKSRAEKEaiadvaLQRVGLSmaei 151
Cdd:COG4181 78 ALdedaraRLRARHVGF------VFQS-FQLLPTLTALENVMlpleLAGR---RDARARARAL------LERVGLG---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 152 kGRFSH---ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDR 228
Cdd:COG4181 138 -HRLDHypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDR 215
|
250
....*....|....*
gi 1817161977 229 VVIMRKGVVVESGDA 243
Cdd:COG4181 216 VLRLRAGRLVEDTAA 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-238 |
7.40e-31 |
|
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: 114.66 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMakvqpVFQNP 103
Cdd:cd03226 10 KKGTEILDDLSLDLYAG--EIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGY-----VMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEAFNPLTRIDEYLLatahrfkGAKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:cd03226 81 DYQLFTDSVREELLL-------GLKELDAGNEQAETVLKDLDLY--ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 184 EPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYISDRVVIMRKGVVV 238
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
6-251 |
1.34e-30 |
|
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: 117.29 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGffsrEKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:TIGR02314 1 MIKLSNITKVFHQGT----KTIQALNNVS--LHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQPVFQNpfeaFNPLT-RIDEYLLATAHRFKGAKSRAEKEAIADVaLQRVGLSmaEIKGRFSHELSGGQL 164
Cdd:TIGR02314 74 NSELTKARRQIGMIFQH----FNLLSsRTVFGNVALPLELDNTPKDEIKRKVTEL-LALVGLG--DKHDSYPSNLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:TIGR02314 147 QRVAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVS 226
|
....*..
gi 1817161977 245 DVLEHPK 251
Cdd:TIGR02314 227 EIFSHPK 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-239 |
1.52e-30 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 114.37 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGGFfsreKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKL----DTRVLKGVSL--SIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAK-----VQpvFQNPFEAFNPLTRIDEYLLAtahrfkGAKSRAEKEAIADVALQRVGLsmaeiKGRFSH--- 157
Cdd:TIGR02211 74 SNERAKLRNKklgfiYQ--FHHLLPDFTALENVAMPLLI------GKKSVKEAKERAYEMLEKVGL-----EHRINHrps 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 158 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYIsDRVVIMRKGVV 237
Cdd:TIGR02211 141 ELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
..
gi 1817161977 238 VE 239
Cdd:TIGR02211 220 FN 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-237 |
1.92e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTklfpiggfFSREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDvkavRSR 86
Cdd:COG4619 1 LELEGLS--------FRVGGKPILSPVSLTL--EAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP----LSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNP--FEAfnpltRIDEYLLATAHrfkgAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQL 164
Cdd:COG4619 67 MPPPEWRRQVAYVPQEPalWGG-----TVRDNLPFPFQ----LRERKFDRERALELLERLGLP-PDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-252 |
4.54e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 4.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSfaLSADKPEIFTIVGESGSGKSTLAK-------MILGSeKADrGSIHFDGTDVKAvrSRRDREAFMAKVQPVF 100
Cdd:COG1117 25 QALKDIN--LDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA-RVE-GEILLDGEDIYD--PDVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 Q--NPFeafnPLTrIDE---YLLatahRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRFSH---ELSGGQLQRIAVARA 172
Cdd:COG1117 99 QkpNPF----PKS-IYDnvaYGL----RLHGIKSKSELDEIVEESLRKAAL-WDEVKDRLKKsalGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 173 LIPEPKLIVADEPVSMVD--ASLRmsIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpiSTAK--IEELILELKK--DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
..
gi 1817161977 251 KH 252
Cdd:COG1117 245 KD 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-246 |
4.64e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 4.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGFfsrekmKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVR 84
Cdd:COG3845 5 ALELRGITKRF--GGV------VANDDVSLTV---RPgEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLATAHRFKGAKSRAE-KEAIADVAlQRVGLSM---AEIkgrfsHELS 160
Cdd:COG3845 71 IRSPRDAIALGIGMVHQH-FMLVPNLTVAENIVLGLEPTKGGRLDRKAaRARIRELS-ERYGLDVdpdAKV-----EDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSM-----VDAslrmsivnLFRDLRD--ALNVSIVYITHDLATAYYISDRVVIMR 233
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVltpqeADE--------LFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLR 215
|
250
....*....|...
gi 1817161977 234 KGVVVESGDARDV 246
Cdd:COG3845 216 RGKVVGTVDTAET 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-261 |
5.94e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 113.64 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKAD----RGSIHFDGTDV--KAVRSRrdreafmaKVQPVFQNP 103
Cdd:PRK10418 19 VHGVSLTLQ--RGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVapCALRGR--------KIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEAFNPLTRIDEYLLATAHrfkgAKSRAEKEAIADVALQRVGLSMAE-IKGRFSHELSGGQLQRIAVARALIPEPKLIVA 182
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCL----ALGKPADDATLTAALEAVGLENAArVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 183 DEPVSMVDASLRMSIVNLFRDL--RDALNVSIVyiTHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKN 260
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvqKRALGMLLV--THDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
.
gi 1817161977 261 A 261
Cdd:PRK10418 243 A 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-246 |
9.82e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 9.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV--KAVRSRRDreafmaKVQPVFQNPFEAF 107
Cdd:PRK13650 23 LNDVSFHVK--QGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRH------KIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 NPLTRIDEylLATAHRFKGAKSRAEKEAIaDVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:PRK13650 95 VGATVEDD--VAFGLENKGIPHEEMKERV-NEALELVG--MQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVVESGDARDV 246
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
37-252 |
1.00e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFM----AKVQPVFQNpFEAFnPLTR 112
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrqlrQHVGFVFQN-FNLF-PHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 113 IDEYLLATAHRFKGaKSRAEKEAIADVALQRVGLSMAEikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDAS 192
Cdd:PRK11264 102 VLENIIEGPVIVKG-EPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 193 LRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 252
Cdd:PRK11264 179 LVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-254 |
1.71e-29 |
|
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: 117.63 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTklfpiggF-FSREKMKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV- 83
Cdd:COG2274 474 IELENVS-------FrYPGDSPPVLDNISLTI---KPgERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQId 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 -RSRRDREAFmakvqpVFQNPFeafnpltrideylLatahrFKG--------AKSRAEKEAIADvALQRVGLsMAEIK-- 152
Cdd:COG2274 544 pASLRRQIGV------VLQDVF-------------L-----FSGtirenitlGDPDATDEEIIE-AARLAGL-HDFIEal 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 153 --------GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyY 224
Cdd:COG2274 598 pmgydtvvGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-R 674
|
250 260 270
....*....|....*....|....*....|
gi 1817161977 225 ISDRVVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-258 |
2.67e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK------AVRSRrdreAFMakvqpVFQN 102
Cdd:PRK13633 25 ALDDVN--LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwDIRNK----AGM-----VFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 PfeafnpltriDEYLLATAHR----FKGAKSRAEKEAI---ADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIP 175
Cdd:PRK13633 94 P----------DNQIVATIVEedvaFGPENLGIPPEEIrerVDESLKKVG--MYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 176 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYS 255
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
...
gi 1817161977 256 IAL 258
Cdd:PRK13633 241 IGL 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-235 |
4.15e-29 |
|
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: 109.01 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffSREKmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 86
Cdd:cd03228 1 IEFKNVSFSYP-----GRPK-PVLKDVSL--TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDREAFMAKVQPVFQNPFeafnpltrideyllatahRFKGaksraekeaiadvalqrvglSMAE-IkgrfsheLSGGQLQ 165
Cdd:cd03228 70 -DLESLRKNIAYVPQDPF------------------LFSG--------------------TIREnI-------LSGGQRQ 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyYISDRVVIMRKG 235
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-262 |
5.20e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.12 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSR 86
Cdd:COG4152 2 LELKGLTKRF--GDK------TAVDDVSF--TVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMakvqpvfqnPFE-AFNPLTRIDEYLLATAhRFKGAKSRAEKEAIADVaLQRVGLsmAEIKGRFSHELSGGQLQ 165
Cdd:COG4152 70 RRRIGYL---------PEErGLYPKMKVGEQLVYLA-RLKGLSKAEAKRRADEW-LERLGL--GDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVD---ASLrmsIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 242
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
250 260
....*....|....*....|.
gi 1817161977 243 ARDVLE-HPKHAYSIALKNAV 262
Cdd:COG4152 213 VDEIRRqFGRNTLRLEADGDA 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
26-248 |
5.27e-29 |
|
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: 110.22 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKV---QPVFQN 102
Cdd:cd03224 12 KSQILFGVSL--TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVpegRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 pfeafnpLTrIDEYLLATAHRFKGAKSRAEKEAIADV--ALqrvglsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:cd03224 90 -------LT-VEENLLLGAYARRRAKRKARLERVYELfpRL-------KERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-239 |
8.96e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.72 E-value: 8.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:COG4525 4 LTVRHVSVRYPGGG----QPQPALQDVSLTIESG--EFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RdreafmaKVqpVFQNpfEAFNP-LTRIDEylLATAHRFKGAkSRAEKEAIADVALQRVGLSMAEikGRFSHELSGGQLQ 165
Cdd:COG4525 78 R-------GV--VFQK--DALLPwLNVLDN--VAFGLRLRGV-PKAERRARAEELLALVGLADFA--RRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM--RKGVVVE 239
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
37-251 |
1.61e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSI-----HFD---GTDVKAVRSRRDreafmaKVQPVFQNpfeaFN 108
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfskTPSDKAIRELRR------NVGMVFQQ----YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 --PLTRIDEYLLATAHRFKG-AKSRAEKEAiaDVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEP 185
Cdd:PRK11124 93 lwPHLTVQQNLIEAPCRVLGlSKDQALARA--EKLLER--LRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 186 VSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDArDVLEHPK 251
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-250 |
3.00e-28 |
|
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: 111.36 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQnpfEA--FNP 109
Cdd:TIGR02142 15 DADFTLPGQ--GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQ---EArlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTrIDEYLLATAHRFKGAKSRAEKEAIADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:TIGR02142 90 LS-VRGNLRYGMKRARPSERRISFERVIEL------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 190 DASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-237 |
5.46e-28 |
|
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: 107.49 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGgffsrekMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsR 86
Cdd:cd03292 1 IEFINVTKTYPNG-------TAALDGINI--SISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR-G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADvALQRVGLSMAEikGRFSHELSGGQLQR 166
Cdd:cd03292 71 RAIPYLRRKIGVVFQD-FRLLPDRNVYEN--VAFALEVTGVPPREIRKRVPA-ALELVGLSHKH--RALPAELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
29-251 |
8.69e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIH-----FD---GTDVKAVRSRRDreafmaKVQPVF 100
Cdd:COG4161 17 ALFDINLECPSG--ETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfsqKPSEKAIRLLRQ------KVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNpFEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAiaDVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:COG4161 89 QQ-YNLWPHLTVMENLIEAPCKVLGLSKEQAREKA--MKLLAR--LRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDArDVLEHPK 251
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-241 |
1.08e-27 |
|
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: 106.51 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsreKMKAVDDVSFALSadkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 86
Cdd:cd03264 1 LQLENLTKRYG--------KKRALDGVSLTLG---PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-----L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNPfeAFNPLTRIDEYLlATAHRFKGAKSRAEKEAIaDVALQRVGLsmAEIKGRFSHELSGGQLQR 166
Cdd:cd03264 65 KQPQKLRRRIGYLPQEF--GVYPNFTVREFL-DYIAWLKGIPSKEVKARV-DEVLELVNL--GDRAKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
36-253 |
1.40e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.36 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 36 ALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS---------RRDREAFMAKVQPVFQNpFEA 106
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadKNQLRLLRTRLTMVFQH-FNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 107 FNPLTRIDEYLLATAHRFKGAKSRAEKEAIAdvALQRVGLSMAEiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 186
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVLGLSKQEARERAVK--YLAKVGIDERA-QGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 187 SMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA 253
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-241 |
3.23e-27 |
|
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: 105.27 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 35 FALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR-SRRdreafmaKVQPVFQ--NPFEAFNPLT 111
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpADR-------PVSMLFQenNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 112 RIDeylLAtahRFKGAKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDA 191
Cdd:cd03298 90 NVG---LG---LSPGLKLTAEDRQAIEVALARVGL--AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1817161977 192 SLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
47-250 |
3.27e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP----FE-------AFNPLTride 115
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPehqlFEetvekdiCFGPMN---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 116 yllatahrFkGAkSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 195
Cdd:PRK13634 114 --------F-GV-SEEDAKQKAREMIELVGLP-EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 196 SIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-241 |
3.57e-27 |
|
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: 105.06 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiggffsREKmKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrSR 86
Cdd:cd03269 1 LEVENVTKRF-------GRV-TALDDISF--SVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--AA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpfeafnplTRIDEYLLATAhRFKGAKSRAEKEAIaDVALQRVGLSmaEIKGRFSHELSGGQLQR 166
Cdd:cd03269 69 RNRIGYLPEERGLYPK--------MKVIDQLVYLA-QLKGLKKEEARRRI-DEWLERLELS--EYANKRVEELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 167 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-252 |
3.89e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 44 IFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPfeafNPLTR--IDEY 116
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDI----FKMDVIELRRRVQMVFQIP----NPIPNlsIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLATAHRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRF---SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 193
Cdd:PRK14247 103 VALGLKLNRLVKSKKELQERVRWALEKAQL-WDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 194 RMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 252
Cdd:PRK14247 182 TAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-285 |
4.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV--KAVRSRRDREafmaKVQPVFQNPfe 105
Cdd:PRK13637 21 KALDNVNI--EIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK----KVGLVFQYP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 106 afnpltridEYLLATAHRFK----GAKSRA-EKEAIAD---VALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEP 177
Cdd:PRK13637 93 ---------EYQLFEETIEKdiafGPINLGlSEEEIENrvkRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 178 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIA 257
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIG 243
|
250 260
....*....|....*....|....*...
gi 1817161977 258 LknAVlppnPREASAILRLRQRNAETNE 285
Cdd:PRK13637 244 L--AV----PQVTYLVRKLRKKGFNIPD 265
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
30-247 |
8.27e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAKVQPVF-QNPFEAFn 108
Cdd:PRK13548 18 LDDVSLTLRPG--EVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-----LARRRAVLpQHSSLSF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTrideyllatAH------RFKGAKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALI------PE 176
Cdd:PRK13548 90 PFT---------VEevvamgRAPHGLSRAEDDALVAAALAQVDL--AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 177 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLA-TAYYiSDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARY-ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-253 |
1.25e-26 |
|
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: 104.08 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAkvqpVFQNpFEAFNP 109
Cdd:TIGR01184 1 LKGVN--LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MV----VFQN-YSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATaHRFKGAKSRAEKEAIADVALQRVGLSMAEIKgrFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:TIGR01184 69 LTVRENIALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAADK--RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 190 DASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG-----------DARDVLEHPKHA 253
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGqilevpfprprDRLEVVEDPSYY 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-241 |
1.30e-26 |
|
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: 103.99 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiGGFfsrekmKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 86
Cdd:cd03265 1 IEVENLVKKY--GDF------EAVRGVSFRVR--RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-----V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNPfeafnpltRIDEYLLATAH-----RFKGAKSRAEKEAIADVaLQRVGLsmAEIKGRFSHELSG 161
Cdd:cd03265 66 REPREVRRRIGIVFQDL--------SVDDELTGWENlyihaRLYGVPGAERRERIDEL-LDFVGL--LEAADRLVKTYSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-241 |
3.85e-26 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.45 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIggffSREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrs 85
Cdd:cd03266 1 MITADALTKRFRD----VKKTVQAVDGVSF--TVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 rrdreafmakvqpvfQNPFEA------FNPLTRIDEYLLATAH-----RFKGAKSRAEKEAIADVALQrvgLSMAEIKGR 154
Cdd:cd03266 71 ---------------KEPAEArrrlgfVSDSTGLYDRLTARENleyfaGLYGLKGDELTARLEELADR---LGMEELLDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRK 234
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHR 211
|
....*..
gi 1817161977 235 GVVVESG 241
Cdd:cd03266 212 GRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-254 |
7.09e-26 |
|
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: 106.77 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 2 SSHFLLELDHVTKLFPIGGFfsrekmKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 81
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGR------PVLDGLSLTLPPG--ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 AVR--SRRDREAFMAkvqpvfQNPfeafnpltrideYLLAT--AHRFKGAKSRAEKEAIADvALQRVGLS---------- 147
Cdd:COG4987 401 DLDedDLRRRIAVVP------QRP------------HLFDTtlRENLRLARPDATDEELWA-ALERVGLGdwlaalpdgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 148 ---MAEiKGRFsheLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIvnlFRDLRDAL-NVSIVYITHDLATAY 223
Cdd:COG4987 462 dtwLGE-GGRR---LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLAGLE 534
|
250 260 270
....*....|....*....|....*....|.
gi 1817161977 224 YIsDRVVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:COG4987 535 RM-DRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-254 |
1.19e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNpFEAFN 108
Cdd:PRK10070 43 GVKDASLAI--EEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS-FALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIDEYLLATAHRFKGAKSRAEKeaiADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREK---ALDALRQVGLE--NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 189 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-250 |
1.35e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.15 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiGGFFsrekmkAVDDVSFALsADKpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:PRK11650 4 LKLQAVRKSYD-GKTQ------VIKGIDLDV-ADG-EFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDREAFMakvqpVFQNpfEAFNPLTRIDEYLlatAHRFKGAK-SRAEKEA-IADVA--------LQRvglsmaeiKGRfs 156
Cdd:PRK11650 75 -DRDIAM-----VFQN--YALYPHMSVRENM---AYGLKIRGmPKAEIEErVAEAArileleplLDR--------KPR-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 157 hELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGV 236
Cdd:PRK11650 134 -ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
250
....*....|....
gi 1817161977 237 VVESGDARDVLEHP 250
Cdd:PRK11650 213 AEQIGTPVEVYEKP 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
26-254 |
2.30e-25 |
|
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: 100.83 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR-----------DREafma 94
Cdd:COG0410 15 GIHVLHGVS--LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgigyvpeGRR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 95 kvqpVFQNpfeafnpLTrIDEYLLAtahrfkGAKSRAEKEAIADvALQRVgLSM----AEIKGRFSHELSGGQLQRIAVA 170
Cdd:COG0410 89 ----IFPS-------LT-VEENLLL------GAYARRDRAEVRA-DLERV-YELfprlKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 171 RALIPEPKLIVADEPV-----SMVDAslrmsIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 245
Cdd:COG0410 149 RALMSRPKLLLLDEPSlglapLIVEE-----IFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
250
....*....|.
gi 1817161977 246 VLEHP--KHAY 254
Cdd:COG0410 223 LLADPevREAY 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-252 |
8.20e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKAVRSrrDREAFMAKVQPVF 100
Cdd:PRK14239 17 KKKALNSVS--LDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRT--DTVDLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 Q--NPFeafnPLTRIDEYLLATahRFKGAKSRAEKEAIADVALQrvGLSM-AEIKGRFsHE----LSGGQLQRIAVARAL 173
Cdd:PRK14239 93 QqpNPF----PMSIYENVVYGL--RLKGIKDKQVLDEAVEKSLK--GASIwDEVKDRL-HDsalgLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 174 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 252
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
29-246 |
9.20e-25 |
|
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: 99.14 E-value: 9.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVqPVFQnpfEAFN 108
Cdd:TIGR03410 15 ILRGVSL--EVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV-PQGR---EIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTrIDEYLLATAhrfkGAKSRAEKEAIADV-ALQRVGLSMaeiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:TIGR03410 89 RLT-VEENLLTGL----AALPRRSRKIPDEIyELFPVLKEM---LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 246
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-235 |
1.52e-24 |
|
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: 97.12 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKVqpvfqnpfeAF 107
Cdd:cd03215 14 GAVRDVSFEVRAG--EIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRAGI---------AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 NPLTRIDEYLLATahrfkgaksraekEAIADVALqrvglsmaeikgrFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:cd03215 80 VPEDRKREGLVLD-------------LSVAENIA-------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1817161977 188 MVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
30-247 |
2.75e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.23 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAKVQPVF-QNPfeAFN 108
Cdd:COG4604 17 LDDVSLTIPKGG--ITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-----LAKRLAILrQEN--HIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIDEylLATAHRF---KGAKSRAEKEAIADvALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEP 185
Cdd:COG4604 88 SRLTVRE--LVAFGRFpysKGRLTAEDREIIDE-AIAYLDLE--DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 186 VSMVDASLRMSIVNLFRDLRDALNVSIVYITHDL--ATAYyiSDRVVIMRKGVVVESGDARDVL 247
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInfASCY--ADHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-241 |
3.75e-24 |
|
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: 96.90 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiggffsrEKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03268 1 LKTNDLTKTY--------GKKRVLDDISL--HVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpfeafnpLT-RIDEYLLATAHRFkgaksraeKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQ 165
Cdd:cd03268 71 LRRIGALIEAPGFYPN-------LTaRENLRLLARLLGI--------RKKRIDEVLDVVGLK--DSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 166 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-258 |
5.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.24 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVS-FALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVF 100
Cdd:PRK13642 12 FKYEKESDVNQLNgVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR----KIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFEAFNPLTRIDEYLLATAHrfkgaKSRAEKEAIADVALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK13642 88 QNPDNQFVGATVEDDVAFGMEN-----QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYSIAL 258
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-235 |
1.24e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 2 SSHFLLELDHVTKLFPIGGFFSrekmKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 81
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQT----DVLHNVSFSIG--EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 82 AVRSR-----RDRE-AFMAKvqpvFQNPFEAFNPLTRIDEYLLAtahrfkGAKSRAEKEAIADVALQRVGLSmAEIKGRF 155
Cdd:PRK11629 75 KLSSAakaelRNQKlGFIYQ----FHHLLPDFTALENVAMPLLI------GKKKPAEINSRALEMLAAVGLE-HRANHRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 ShELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISdRVVIMRKG 235
Cdd:PRK11629 144 S-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-222 |
1.41e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKAD---RGSIHFDGTDVKAVRSRRDREAFMakvqpvFQNPFea 106
Cdd:COG4136 17 LAPLSLTVA--PGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL------FQDDL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 107 FNP-LTRIDEYLLATAHRFKgaksRAEKEAIADVALQRVGLS-MAEikgRFSHELSGGQLQRIAVARALIPEPKLIVADE 184
Cdd:COG4136 87 LFPhLSVGENLAFALPPTIG----RAQRRARVEQALEEAGLAgFAD---RDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1817161977 185 PVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATA 222
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-250 |
1.60e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdrEAFMAKVQpVFQNpFEAFN 108
Cdd:PRK11300 20 AVNNVNLEVREQ--EIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ--IARMGVVR-TFQH-VRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIdEYLLATAHR------FKG-----AKSRAEKEAI--ADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIP 175
Cdd:PRK11300 94 EMTVI-ENLLVAQHQqlktglFSGllktpAFRRAESEALdrAATWLERVGLL--EHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 176 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-247 |
2.05e-23 |
|
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: 100.20 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 3 SHFLLELDHVTKLFpigGFFSrekmKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 82
Cdd:TIGR01193 470 LNGDIVINDVSYSY---GYGS----NILSDIS--LTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VrsrrDREAFMAKVQPVFQNPFeAFNPlTRIDEYLLatahrfkGAKSRAEKEAIADValqrvgLSMAEIKG--------- 153
Cdd:TIGR01193 541 I----DRHTLRQFINYLPQEPY-IFSG-SILENLLL-------GAKENVSQDEIWAA------CEIAEIKDdienmplgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 154 --RFSHE---LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlnvSIVYITHDLATAYYiSDR 228
Cdd:TIGR01193 602 qtELSEEgssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDK 677
|
250
....*....|....*....
gi 1817161977 229 VVIMRKGVVVESGDARDVL 247
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELL 696
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-252 |
2.26e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 44 IFTIVGESGSGKSTLAKM------ILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNPfeafNPLTRIDEY- 116
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQP----NPFPHLSIYd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLATAHRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRF---SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 193
Cdd:PRK14246 110 NIAYPLKSHGIKEKREIKKIVEECLRKVGL-WKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 194 RMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 252
Cdd:PRK14246 189 SQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
37-235 |
2.46e-23 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 95.09 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSRRDREAFMAKVQPVFQnpfeAFNPLtridEY 116
Cdd:TIGR02982 26 LEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGA-SKKQLVQLRRRIGYIFQ----AHNLL----GF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLATAHRFKGAK-----SRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDA 191
Cdd:TIGR02982 97 LTARQNVQMALElqpnlSYQEARERARAMLEAVGLG--DHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1817161977 192 SLRMSIVNLFRDLRDALNVSIVYITHDlATAYYISDRVVIMRKG 235
Cdd:TIGR02982 175 KSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-248 |
2.87e-23 |
|
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: 99.11 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD--VKAVRSRRDREAFMAKVQPVFQ 101
Cdd:TIGR03269 294 RGVVKAVDNVSLEVK--EGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPDGRGRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NPFEAFNPLTRIDEylLATAHRFKGAKSRAEKEAIadVALQRVGLS---MAEIKGRFSHELSGGQLQRIAVARALIPEPK 178
Cdd:TIGR03269 372 QEYDLYPHRTVLDN--LTEAIGLELPDELARMKAV--ITLKMVGFDeekAEEILDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 179 LIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-252 |
5.27e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 44 IFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDG-----TDVKAVRSRRdreafmaKVQPVFQNPfeafNPLTRI 113
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGrniysPDVDPIEVRR-------EVGMVFQYP----NPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 114 DEYL-LATAHRFKG-AKSRAEKEAIADVALQRVGLsMAEIKGR---FSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK14267 101 TIYDnVAIGVKLNGlVKSKKELDERVEWALKKAAL-WDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 189 VDASLRMSIVNLFRDLRDALnvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 252
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-253 |
1.00e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADKpeIFTIVGESGSGKSTLAKMIlgSEKADRGSIHFDGTDV----KAVRSRRDREAFMAKVQPVFQ--NP 103
Cdd:PRK14271 37 LDQVSMGFPARA--VTSLMGPTGSGKTTFLRTL--NRMNDKVSGYRYSGDVllggRSIFNYRDVLEFRRRVGMLFQrpNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FeafnPLTRIDEYLLAT-AHRFKgakSRAEKEAIADVALQRVGLSMAeIKGRFSH---ELSGGQLQRIAVARALIPEPKL 179
Cdd:PRK14271 113 F----PMSIMDNVLAGVrAHKLV---PRKEFRGVAQARLTEVGLWDA-VKDRLSDspfRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 180 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyiTHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA 253
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIV--THNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-247 |
1.59e-22 |
|
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: 93.32 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPFeAFN 108
Cdd:cd03252 17 ILDNISLRIKPG--EVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----DPAWLRRQVGVVLQENV-LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 --------------PLTRIDEYL-LATAHRFkgaksraekeaiadvaLQRVGLSMAEIKGRFSHELSGGQLQRIAVARAL 173
Cdd:cd03252 90 rsirdnialadpgmSMERVIEAAkLAGAHDF----------------ISELPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 174 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVL 247
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-222 |
1.81e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHfdgtdvkavRSRRDREAFMakVQpvfqnpfeafn 108
Cdd:NF040873 7 VLHGVD--LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYV--PQ----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 pLTRIDEYLLAT----------AHRFKGAKSRAEKEAIADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPK 178
Cdd:NF040873 63 -RSEVPDSLPLTvrdlvamgrwARRGLWRRLTRDDRAAVDDALERVGL--ADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1817161977 179 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATA 222
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-249 |
1.89e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 97.03 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGgffsreKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsR 86
Cdd:TIGR01842 317 LSVENVTIVPPGG------KKPTLRGISFSLQAG--EALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpFEAFnpltriDEYLLATAHRF-KGAKSRAEKEA--IADVALQRVGLSM---AEIkGRFSHELS 160
Cdd:TIGR01842 385 WDRETFGKHIGYLPQD-VELF------PGTVAENIARFgENADPEKIIEAakLAGVHELILRLPDgydTVI-GPGGATLS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLAtAYYISDRVVIMRKGVVVES 240
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPS-LLGCVDKILVLQDGRIARF 534
|
....*....
gi 1817161977 241 GDARDVLEH 249
Cdd:TIGR01842 535 GERDEVLAK 543
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-235 |
2.09e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDreafmakvqPVFQNpfEAFN 108
Cdd:PRK11248 16 ALEDINLTL--ESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG---------VVFQN--EGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIDEYLlATAHRFKGAkSRAEKEAIADVALQRVGLSMAEikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK11248 83 PWRNVQDNV-AFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAE--KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1817161977 189 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
43-243 |
3.65e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEK--ADRGSIHFDGTDVKAV----RSRRDreAFMAkvqpvFQNPfeafnplTRID-- 114
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELspdeRARAG--IFLA-----FQYP-------VEIPgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 115 --EYLLATA--HRFKGAKSRAEKEAIADVALQRVGLSMAEIKgRFSHE-LSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:COG0396 93 svSNFLRTAlnARRGEELSAREFLKLLKEKMKELGLDEDFLD-RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 190 DA-SLRMsIVNLFRDLRDAlNVSIVYITHdlataY-----YIS-DRVVIMRKGVVVESGDA 243
Cdd:COG0396 172 DIdALRI-VAEGVNKLRSP-DRGILIITH-----YqrildYIKpDFVHVLVDGRIVKSGGK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
48-249 |
3.68e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 48 VGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP----FE-------AFNPltridey 116
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPesqlFEetvlkdvAFGP------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 llataHRFkgAKSRAEKEAIADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 196
Cdd:PRK13649 112 -----QNF--GVSQEEAEALAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 197 IVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13649 184 LMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
35-242 |
5.12e-22 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 91.46 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 35 FALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-KAVRSRRdreafmaKVQPVFQNPfEAFNPLTrI 113
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtGLAPYQR-------PVSMLFQEN-NLFAHLT-V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 114 DEYLLATAHrfKGAKSRA-EKEAIADVAlQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDAS 192
Cdd:TIGR01277 88 RQNIGLGLH--PGLKLNAeQQEKVVDAA-QQVGI--ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1817161977 193 LRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 242
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-218 |
6.05e-22 |
|
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: 91.00 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKlfpiggffSREKMKAVDDVSFALSAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:COG4133 2 MLEAENLSC--------RRGERLLFSGLSFTLAA--GEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMakvqpVFQNPfeAFNP-LTrIDEYlLATAHRFKGAksRAEKEAIADvALQRVGLsmAEIKGRFSHELSGGQL 164
Cdd:COG4133 72 DYRRRLAY-----LGHAD--GLKPeLT-VREN-LRFWAALYGL--RADREAIDE-ALEAVGL--AGLADLPVRQLSAGQK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHD 218
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-251 |
1.10e-21 |
|
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: 91.07 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsrrdreafmakvQPVFQN--- 102
Cdd:cd03218 12 KRKVVNGVSLSV--KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--------------LPMHKRarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 -----PFEA--FNPLTrIDEYLLATAHRFKgaKSRAEKEAIADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIP 175
Cdd:cd03218 76 gigylPQEAsiFRKLT-VEENILAVLEIRG--LSKKEREEKLEELLEE--FHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 176 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVyIT-HDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVL-ITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-241 |
2.54e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTklfpiggfFS-REKMKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVr 84
Cdd:COG1132 340 IEFENVS--------FSyPGDRPVLKDISLTI---PPgETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 srrDREAFMAKVQPVFQNPFeafnpltrideyllatahRFKG--------AKSRAEKEAIADvALQRVGL-----SMAE- 150
Cdd:COG1132 408 ---TLESLRRQIGVVPQDTF------------------LFSGtireniryGRPDATDEEVEE-AAKAAQAhefieALPDg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 151 ---IKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD----ASLRMSIVNLFRDlrdalnVSIVYITHDLATay 223
Cdd:COG1132 466 ydtVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEALERLMKG------RTTIVIAHRLST-- 537
|
250 260
....*....|....*....|
gi 1817161977 224 yI--SDRVVIMRKGVVVESG 241
Cdd:COG1132 538 -IrnADRILVLDDGRIVEQG 556
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
37-254 |
2.78e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 89.12 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSE--KADRGSIHFDGTDVKAV----RSRRDreAFMAkvqpvFQNPFEAfnPL 110
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLppeeRARLG--IFLA-----FQYPPEI--PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 111 TRIDEYLlatahrfkgaksraekeaiadvalqrvglsmaeikgRFSHE-LSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:cd03217 92 VKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 190 DA-SLRMsIVNLFRDLRDAlNVSIVYITH--DLAtAYYISDRVVIMRKGVVVESGDARDVLEHPKHAY 254
Cdd:cd03217 136 DIdALRL-VAEVINKLREE-GKSVLIITHyqRLL-DYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-250 |
4.66e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.21 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 19 GGFFSREKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKVQP 98
Cdd:PRK11831 12 GVSFTRGNRCIFDNIS--LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV-RKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQ--------NPFE--AFnPL---TRIDEYLLATAHRFKgaksraekeaiadvaLQRVGL-SMAEIKgrfSHELSGGQL 164
Cdd:PRK11831 89 LFQsgalftdmNVFDnvAY-PLrehTQLPAPLLHSTVMMK---------------LEAVGLrGAAKLM---PSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
....*.
gi 1817161977 245 DVLEHP 250
Cdd:PRK11831 230 ALQANP 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-249 |
4.72e-21 |
|
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: 92.89 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKV----QPVfqnpfE 105
Cdd:COG4618 348 LRGVSFSLEPG--EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL----SQWDREELGRHIgylpQDV-----E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 106 AFNpltrideyllAT-----AhRFKGAKSRAekeAIAdvALQRVG-----LSMAE----IKGRFSHELSGGQLQRIAVAR 171
Cdd:COG4618 417 LFD----------GTiaeniA-RFGDADPEK---VVA--AAKLAGvhemiLRLPDgydtRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLAtAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-242 |
6.21e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 35 FALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD-VKAVRSRRdreafmakvqPV---FQ-NPFeaFNP 109
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSRR----------PVsmlFQeNNL--FSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTrIDEYLLATAHrfKGAK-SRAEKEAIADVAlQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK10771 86 LT-VAQNIGLGLN--PGLKlNAAQREKLHAIA-RQMGIE--DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 189 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 242
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-251 |
6.24e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMAKVQPVFQNPFEA-F 107
Cdd:PRK13639 17 ALKGINF--KAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--YDKKSLLEVRKTVGIVFQNPDDQlF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 NPltRIDEYLLATAHRFKGAKSRAEKEAIAdvALQRVGLSMAEIKGrfSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:PRK13639 93 AP--TVEEDVAFGPLNLGLSKEEVEKRVKE--ALKAVGMEGFENKP--PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-241 |
6.48e-21 |
|
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: 88.42 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 86
Cdd:cd03245 3 IEFRNVSFSYP------NQEIPALDNVSLTIRAG--EKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 rDREAFMAKVQPVFQNPF----------EAFNPLTRiDEYLLATAhRFKGAKSRaekeaiadVALQRVGLSMaEI--KGR 154
Cdd:cd03245 72 -DPADLRRNIGYVPQDVTlfygtlrdniTLGAPLAD-DERILRAA-ELAGVTDF--------VNKHPNGLDL-QIgeRGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FsheLSGGQLQRIAVARALIPEPKLIVADEPVSMVD-ASLRMSIVNLFRDLRDAlnvSIVYITHDLAtAYYISDRVVIMR 233
Cdd:cd03245 140 G---LSGGQRQAVALARALLNDPPILLLDEPTSAMDmNSEERLKERLRQLLGDK---TLIIITHRPS-LLDLVDRIIVMD 212
|
....*...
gi 1817161977 234 KGVVVESG 241
Cdd:cd03245 213 SGRIVADG 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-248 |
7.27e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEY 116
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLAtAHRFKGAKSRAEKeaIADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 196
Cdd:PRK13643 107 AFG-PQNFGIPKEKAEK--IAAEKLEMVGLA-DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 197 IVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-232 |
9.77e-21 |
|
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: 91.96 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--VR 84
Cdd:TIGR02857 322 LEFSGVSVAYP-------GRRPALRPVSFTVPPG--ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFmakvqpVFQNPFeaFNPLTRIDEYLLATahrfKGAKSRAEKEAIADVALQRV----GLSMAEIKGRFSHELS 160
Cdd:TIGR02857 393 SWRDQIAW------VPQHPF--LFAGTIAENIRLAR----PDASDAEIREALERAGLDEFvaalPQGLDTPIGEGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyYISDRVVIM 232
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-248 |
1.03e-20 |
|
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: 88.44 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVF 100
Cdd:cd03254 10 FSYDEKKPVLKDINF--SIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFeAFNplTRIDEYLlatahRFKGAKSRAEKEAIADVALQRVGLSMAEIKGRFS------HELSGGQLQRIAVARALI 174
Cdd:cd03254 84 QDTF-LFS--GTIMENI-----RLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 175 PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVyITHDLATAYYiSDRVVIMRKGVVVESGDARDVLE 248
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKG-RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-244 |
1.11e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDdvsfaLSADKPEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGTDV-KAVRSRRDREAFMAKV 96
Cdd:PRK09984 14 FNQHQALHAVD-----LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVqREGRLARDIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QPVFQNpFEAFNPLTRIDEYLLA---------TAHRFKgakSRAEKEAiADVALQRVGLSmaeikgRFSHE----LSGGQ 163
Cdd:PRK09984 89 GYIFQQ-FNLVNRLSVLENVLIGalgstpfwrTCFSWF---TREQKQR-ALQALTRVGMV------HFAHQrvstLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 243
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
.
gi 1817161977 244 R 244
Cdd:PRK09984 238 Q 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-287 |
1.54e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSRRDReafmAKVQPVFQnpFEAFNP 109
Cdd:PRK13536 57 VNGLSFTVASG--ECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLAR----ARIGVVPQ--FDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATAhRFKGAKSRaEKEAIADVALQRVGLSmAEIKGRFShELSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:PRK13536 128 EFTVRENLLVFG-RYFGMSTR-EIEAVIPSLLEFARLE-SKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 190 DASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKNAvlppNPRE 269
Cdd:PRK13536 204 DPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGG----DPHE 278
|
250
....*....|....*...
gi 1817161977 270 ASAILRLRQRNAETNEAT 287
Cdd:PRK13536 279 LSSLVKPYARRIEVSGET 296
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-262 |
1.66e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP---- 103
Cdd:PRK13646 21 QAIHDVNTEFEQGK--YYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEafnplTRIDEYLLATAHRFK----GAKSRAEKeAIADVALQRVGLSMAEIkgrfshELSGGQLQRIAVARALIPEPKL 179
Cdd:PRK13646 99 FE-----DTVEREIIFGPKNFKmnldEVKNYAHR-LLMDLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 180 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA--YSIA 257
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLadWHIG 246
|
....*
gi 1817161977 258 LKNAV 262
Cdd:PRK13646 247 LPEIV 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-250 |
1.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.17 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 12 VTKLFP---IGGF-FSREKMKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKA 82
Cdd:PRK14258 1 MSKLIPaikVNNLsFYYDTQKILEGVSMEIYQSK--VTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 83 VRSRRDReaFMAKVQPVFQNPfeAFNPLTRIDEylLATAHRFKGAKSRAEKEAIADVALQRVGLsMAEIKGRFSH---EL 159
Cdd:PRK14258 79 RRVNLNR--LRRQVSMVHPKP--NLFPMSVYDN--VAYGVKIVGWRPKLEIDDIVESALKDADL-WDEIKHKIHKsalDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM-----RK 234
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRI 231
|
250
....*....|....*.
gi 1817161977 235 GVVVESGDARDVLEHP 250
Cdd:PRK14258 232 GQLVEFGLTKKIFNSP 247
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
30-237 |
2.80e-20 |
|
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: 85.73 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQnpfeafnp 109
Cdd:cd03246 18 LRNVSFSIEPG--ESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW----DPNELGDHVGYLPQ-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 ltriDEYLlatahrFKGaksraekeaiadvalqrvglSMAEIKgrfsheLSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:cd03246 84 ----DDEL------FSG--------------------SIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1817161977 190 DASLRMSIVNLFRDLRdALNVSIVYITHDLATAyYISDRVVIMRKGVV 237
Cdd:cd03246 128 DVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-251 |
6.34e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP---- 103
Cdd:PRK13641 21 KGLDNISFELEEGS--FVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FE-------AFNPLTrideyllatahrFKGAKSRAEKEAIAdvALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPE 176
Cdd:PRK13641 99 FEntvlkdvEFGPKN------------FGFSEDEAKEKALK--WLKKVGLS-EDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 177 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-248 |
6.36e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 3 SHFLLELDHVTKLFPiggffsreKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKmIL------GSEKadrGSIHFD 76
Cdd:PRK13549 2 MEYLLEMKNITKTFG--------GVKALDNVSLKV--RAGEIVSLCGENGAGKSTLMK-VLsgvyphGTYE---GEIIFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 77 GTDVKAvRSRRDREA----------FMAKVQPVFQNPF--EAFNPLTRIDeyllatahrFKGAKSRAEKeaiadvALQRV 144
Cdd:PRK13549 68 GEELQA-SNIRDTERagiaiihqelALVKELSVLENIFlgNEITPGGIMD---------YDAMYLRAQK------LLAQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 145 GLSMaEIKGRFSHeLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYY 224
Cdd:PRK13549 132 KLDI-NPATPVGN-LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKA 208
|
250 260
....*....|....*....|....
gi 1817161977 225 ISDRVVIMRKGVVVESGDARDVLE 248
Cdd:PRK13549 209 ISDTICVIRDGRHIGTRPAAGMTE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-247 |
7.01e-20 |
|
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: 86.29 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTklfpiggfFSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSE-KADRGSIH-----FDGTD 79
Cdd:COG1119 3 LLELRNVT--------VRRGGKTILDDISWTVKPG--EHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRlfgerRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 80 VKAVRSRrdreafMAKVQPVFQnpfEAFNPLTRIDEYLL----ATAHRFKgaKSRAEKEAIADVALQRVGlsMAEIKGRF 155
Cdd:COG1119 73 VWELRKR------IGLVSPALQ---LRFPRDETVLDVVLsgffDSIGLYR--EPTDEQRERARELLELLG--LAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHdlatayYISD------RV 229
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgitHV 213
|
250
....*....|....*...
gi 1817161977 230 VIMRKGVVVESGDARDVL 247
Cdd:COG1119 214 LLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-265 |
9.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 25 EKMKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSI---------HFDGTDVKAVRSRRDREAFMA- 94
Cdd:PRK13631 37 NELVALNNISYTFEKNK--IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKIKNFKEl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 95 --KVQPVFQNP-FEAFNplTRIDEYLLATAHRFKGAKSRAEKeaIADVALQRVGLSMAEIKgRFSHELSGGQLQRIAVAR 171
Cdd:PRK13631 115 rrRVSMVFQFPeYQLFK--DTIEKDIMFGPVALGVKKSEAKK--LAKFYLNKMGLDDSYLE-RSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
250
....*....|....
gi 1817161977 252 HaysIALKNAVLPP 265
Cdd:PRK13631 269 I---INSTSIQVPR 279
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-243 |
2.05e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffsreKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSR 86
Cdd:PRK11288 5 LSFDGIGKTFP--------GVKALDDISF--DCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQNpfeafnpLTRIDE-------YLLATAHRFkGAKSRAEKEAIADVALQRVGLSM---AEIKgrfs 156
Cdd:PRK11288 72 STTAALAAGVAIIYQE-------LHLVPEmtvaenlYLGQLPHKG-GIVNRRLLNYEAREQLEHLGVDIdpdTPLK---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 157 hELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASlrmSIVNLFR---DLRDALNVsIVYITHDLATAYYISDRVVIMR 233
Cdd:PRK11288 140 -YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR---EIEQLFRvirELRAEGRV-ILYVSHRMEEIFALCDAITVFK 214
|
250
....*....|
gi 1817161977 234 KGVVVESGDA 243
Cdd:PRK11288 215 DGRYVATFDD 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-248 |
2.86e-19 |
|
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: 87.57 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGffsrekMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDVKAv 83
Cdd:TIGR02633 1 LLEMKGIVKTF--GG------VKALDGIDLEVRPG--ECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 RSRRDREA----------FMAKVQPVFQNPF---EAFNPLTRIDEYLLATahrfkgaksRAEKeaiadvALQRVGLSMAE 150
Cdd:TIGR02633 70 SNIRDTERagiviihqelTLVPELSVAENIFlgnEITLPGGRMAYNAMYL---------RAKN------LLRELQLDADN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 151 IKgRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVV 230
Cdd:TIGR02633 135 VT-RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTIC 212
|
250
....*....|....*...
gi 1817161977 231 IMRKGVVVESGDARDVLE 248
Cdd:TIGR02633 213 VIRDGQHVATKDMSTMSE 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-251 |
3.65e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFA----LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrDREAFMakvqpVFQNp 103
Cdd:PRK11000 11 KAYGDVVISkdinLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGM-----VFQS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 fEAFNP-LTrideylLATAHRFkGAK-SRAEKEAIAdvalQRVG-----LSMAEIKGRFSHELSGGQLQRIAVARALIPE 176
Cdd:PRK11000 84 -YALYPhLS------VAENMSF-GLKlAGAKKEEIN----QRVNqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 177 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-241 |
4.43e-19 |
|
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: 83.82 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADKPEI----FT--------IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKV 96
Cdd:cd03253 2 EFENVTFAYDPGRPVLkdvsFTipagkkvaIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV----TLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QPVFQNPFeAFNplTRIdeyllatAHRFKGAKSRAEKEAIADVA----LQRVGLSMAE----IKGRFSHELSGGQLQRIA 168
Cdd:cd03253 78 GVVPQDTV-LFN--DTI-------GYNIRYGRPDATDEEVIEAAkaaqIHDKIMRFPDgydtIVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 169 VARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESG 241
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-250 |
4.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsrekMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD------ 79
Cdd:PRK13644 1 MIRLENVSYSYPDG-------TPALENIN--LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfsk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 80 VKAVRSRrdreafmakVQPVFQNPFEAFnpLTRIDEYLLATAhrfkgaksrAEKEAIADVAL-QRVGLSMAEIK-GRFSH 157
Cdd:PRK13644 72 LQGIRKL---------VGIVFQNPETQF--VGRTVEEDLAFG---------PENLCLPPIEIrKRVDRALAEIGlEKYRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 158 E----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLaTAYYISDRVVIMR 233
Cdd:PRK13644 132 RspktLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMD 209
|
250
....*....|....*..
gi 1817161977 234 KGVVVESGDARDVLEHP 250
Cdd:PRK13644 210 RGKIVLEGEPENVLSDV 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-235 |
7.51e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiggffsreKMKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:PRK10762 4 LLQLKGIDKAFP--------GVKALSGAALNVYPGR--VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQ---------PVFQNPF---EAFNPLTRIDeyllatahrfkGAKSRAEkeaiADVALQRVGLSMAeikg 153
Cdd:PRK10762 74 KSSQEAGIGIIHqelnlipqlTIAENIFlgrEFVNRFGRID-----------WKKMYAE----ADKLLARLNLRFS---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 154 rfSH----ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRV 229
Cdd:PRK10762 135 --SDklvgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDV 211
|
....*.
gi 1817161977 230 VIMRKG 235
Cdd:PRK10762 212 TVFRDG 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-251 |
8.15e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA----VRSRRD-----REAfmakvqP 98
Cdd:COG1137 17 TVVKDVS--LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKRARLGigylpQEA------S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQNpfeafnpLTrIDEYLLATAHRFKgaKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPK 178
Cdd:COG1137 89 IFRK-------LT-VEDNILAVLELRK--LSKKEREERLEELLEEFGIT--HLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 179 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVyIT-HD----LAtayyISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL-ITdHNvretLG----ICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-247 |
9.46e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrdreAFMAKVQPVFQNPFEAFNP 109
Cdd:PRK09536 19 LDGVD--LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR----AASRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 189
Cdd:PRK09536 93 DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTG--VAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 190 DASLRMSIVNLFRDLRDALNVSIVYItHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-246 |
9.63e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTklfpiggFFSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 85
Cdd:COG3845 257 VLEVENLS-------VRDDRGVPALKDVSLEVRAG--EILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKV------------QPVFQNPFeafnpLTRIDEYLLATAH--RFKGAKSRAEkEAIA--DVALQRVGLSMA 149
Cdd:COG3845 328 RERRRLGVAYIpedrlgrglvpdMSVAENLI-----LGRYRRPPFSRGGflDRKAIRAFAE-ELIEefDVRTPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 150 EikgrfsheLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRV 229
Cdd:COG3845 402 S--------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRI 472
|
250
....*....|....*..
gi 1817161977 230 VIMRKGVVVESGDARDV 246
Cdd:COG3845 473 AVMYEGRIVGEVPAAEA 489
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-238 |
1.19e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKmILGS-EKADRGSIHFDGTDVKAVr 84
Cdd:PRK10535 4 LLELKDIRRSYPSG----EEQVEVLKGISLDIYAG--EMVAIVGASGSGKSTLMN-ILGClDKPTSGTYRVAGQDVATL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 srrDREAFMAKVQPVFQNPFEAFNPLTRideylLATAHRFK-----GAKSRAEKEAIADVALQRVGLsmAEIKGRFSHEL 159
Cdd:PRK10535 76 ---DADALAQLRREHFGFIFQRYHLLSH-----LTAAQNVEvpavyAGLERKQRLLRAQELLQRLGL--EDRVEYQPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYiSDRVVIMRKGVVV 238
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-238 |
1.23e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK------AVRSR-------RDREAFMA 94
Cdd:COG1129 266 GVVRDVSFSVRAG--EILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAGiayvpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 95 KvQPVFQNpfeafnpLTrideylLATAHRFKGAK--SRAEKEAIADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARA 172
Cdd:COG1129 344 D-LSIREN-------IT------LASLDRLSRGGllDRRRERALAEEYIKRLRIKTPSPEQPVG-NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 173 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-264 |
1.58e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfmakVQPVFQNP 103
Cdd:PRK13652 14 SGSKEALNNINF--IAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FE-----------AFNPLTR-IDEYllATAHRfkgaksraekeaiADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVAR 171
Cdd:PRK13652 88 DDqifsptveqdiAFGPINLgLDEE--TVAHR-------------VSSALHMLGLE--ELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 251
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
250
....*....|...
gi 1817161977 252 HAYSIALKNAVLP 264
Cdd:PRK13652 231 LLARVHLDLPSLP 243
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
28-241 |
1.94e-18 |
|
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: 80.82 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsrrdrEAFMAKVQPVFQNPfeaf 107
Cdd:cd03247 16 QVLKNLSLELKQG--EKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-----KALSSLISVLNQRP---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 npltrideYLLATAHRfkgaksraekeaiadvalQRVGLsmaeikgRFShelsGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:cd03247 85 --------YLFDTTLR------------------NNLGR-------RFS----GGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 188 MVDASLRMSIVNL-FRDLRDAlnvSIVYITHDLATAYYIsDRVVIMRKGVVVESG 241
Cdd:cd03247 128 GLDPITERQLLSLiFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
3.34e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 5 FLLELDHVTKLFPIGgffsrekMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavR 84
Cdd:PRK13636 4 YILKVEELNYNYSDG-------THALKGIN--INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID--Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFMAKVQPVFQNPFeafNPLTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQL 164
Cdd:PRK13636 73 SRKGLMKLRESVGMVFQDPD---NQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE--HLKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 244
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 1817161977 245 DVL 247
Cdd:PRK13636 228 EVF 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-235 |
6.44e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpIGGffsREKMKAVDdvsFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR 84
Cdd:PRK10908 1 MIRFEHVSKAY-LGG---RQALQGVT---FHM---RPgEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRrDREAFMAKVQPVFQnpfeafnpltriDEYLL---------ATAHRFKGAKSRAEKEAIAdVALQRVGLsmAEIKGRF 155
Cdd:PRK10908 71 NR-EVPFLRRQIGMIFQ------------DHHLLmdrtvydnvAIPLIIAGASGDDIRRRVS-AALDKVGL--LDKAKNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrDALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:PRK10908 135 PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-275 |
8.20e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.32 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmAKVQPVF 100
Cdd:PRK13647 12 FRYKDGTKALKGLS--LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR----SKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFEAFNPLTRIDEylLATAHRFKGAkSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK13647 86 QDPDDQVFSSTVWDD--VAFGPVNMGL-DKDEVERRVEEALKAVR--MWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA-----RDVLEHPKHAYS 255
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLRLP 239
|
250 260
....*....|....*....|....*....
gi 1817161977 256 IA---------LKNAVLPPNPREASAILR 275
Cdd:PRK13647 240 LVaqifedlpeLGQSKLPLTVKEAVQIIR 268
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-218 |
9.30e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLLELDHVTklfpiggfFSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 80
Cdd:PRK10247 2 QENSPLLQLQNVG--------YLAGDAKILNNISFSLRAG--EFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 81 KAVRSrrdrEAFMAKVQPVFQNPfeAFNPLTRIDEYLLATAHRfkgaKSRAEKEAIADvALQRVGLSMAEIKGRFShELS 160
Cdd:PRK10247 72 STLKP----EIYRQQVSYCAQTP--TLFGDTVYDNLIFPWQIR----NQQPDPAIFLD-DLERFALPDTILTKNIA-ELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 161 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHD 218
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
47-237 |
9.69e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsrrDREAFMakvqpvFQN----PFEafnplTRIDEYLLatah 122
Cdd:PRK11247 43 VVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLM------FQDarllPWK-----KVIDNVGL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 123 rfkGAKSRAEKEAIAdvALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFR 202
Cdd:PRK11247 105 ---GLKGQWRDAALQ--ALAAVGL--ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1817161977 203 DLRDALNVSIVYITHDLATAYYISDRVVIMRKGVV 237
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-263 |
1.43e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsRRDREAFMAKVqPVFQNP 103
Cdd:PRK15056 17 RNGHTALRDASFTVPGG--SIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYV-PQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEAFNPLTRIDEYLLATAHRFKGAKSRAEKEAIADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:PRK15056 90 DWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVD--MVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 184 EPVSMVDASLRMSIVNLFRDLRDALNVSIVYiTHDLATAYYISDRVViMRKGVVVESGDARDVL--EHPKHAYSIALKNA 261
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYTV-MVKGTVLASGPTETTFtaENLELAFSGVLRHV 245
|
..
gi 1817161977 262 VL 263
Cdd:PRK15056 246 AL 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-266 |
1.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 27 MKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAK--VQPVFQNPF 104
Cdd:PRK13651 20 LKALDNVSVEIN--QGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKlvIQKTRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 EAFNPLTR-------IDEYLLATAHRFK----GAKS----RAEKEAIADVALQRVGLSMAEIKgRFSHELSGGQLQRIAV 169
Cdd:PRK13651 98 KKIKEIRRrvgvvfqFAEYQLFEQTIEKdiifGPVSmgvsKEEAKKRAAKYIELVGLDESYLQ-RSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 170 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
250
....*....|....*..
gi 1817161977 250 PKhaysIALKNAVLPPN 266
Cdd:PRK13651 256 NK----FLIENNMEPPK 268
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-249 |
2.08e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHflLELDHVTKLFPIGGFFSR--------------EKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSE 66
Cdd:COG1134 1 MSSM--IEVENVSKSYRLYHEPSRslkelllrrrrtrrEEFWALKDVSFEVERG--ESVGIIGRNGAGKSTLLKLIAGIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 67 KADRGSIHFDGtdvkavrsrrdreafmaKVQPvfqnPFE---AFNP-LT-RidE--YLLATAHRFkgakSRAE-KEAIAD 138
Cdd:COG1134 77 EPTSGRVEVNG-----------------RVSA----LLElgaGFHPeLTgR--EniYLNGRLLGL----SRKEiDEKFDE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 139 VAlqrvglSMAEIkGRFSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVY 214
Cdd:COG1134 130 IV------EFAEL-GDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 1817161977 215 ITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:COG1134 202 VSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
25-248 |
4.56e-17 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 81.07 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 25 EKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPF 104
Cdd:TIGR03375 476 QETPALDNVSLTIRPG--EKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI----DPADLRRNIGYVPQDPR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 eAFNPLTRiDEYLLATAHrfkgaksrAEKEAIADvALQRVGLSM-------------AEiKGRFsheLSGGQLQRIAVAR 171
Cdd:TIGR03375 550 -LFYGTLR-DNIALGAPY--------ADDEEILR-AAELAGVTEfvrrhpdgldmqiGE-RGRS---LSGGQRQAVALAR 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMsivNLFRDLRDAL-NVSIVYITH-----DLAtayyisDRVVIMRKGVVVESGDARD 245
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEE---RFKDRLKRWLaGKTLVLVTHrtsllDLV------DRIIVMDNGRIVADGPKDQ 685
|
...
gi 1817161977 246 VLE 248
Cdd:TIGR03375 686 VLE 688
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-255 |
5.78e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.83 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffSREKMkAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:PRK11176 342 IEFRNVTFTYP-----GKEVP-ALRNINFKIPAGK--TVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREafmaKVQPVFQNpFEAFNpltriDEYLLATAHRFKGAKSRAEKEAIADVA-----LQRVGLSMAEIKGRFSHELSG 161
Cdd:PRK11176 414 SLRN----QVALVSQN-VHLFN-----DTIANNIAYARTEQYSREQIEEAARMAyamdfINKMDNGLDTVIGENGVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 162 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATayyI--SDRVVIMRKGVVVE 239
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLST---IekADEILVVEDGEIVE 558
|
250
....*....|....*.
gi 1817161977 240 SGDARDVLEHpKHAYS 255
Cdd:PRK11176 559 RGTHAELLAQ-NGVYA 573
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-248 |
1.11e-16 |
|
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: 77.58 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 23 SREKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK--AVRSRRDREAFmakvqpVF 100
Cdd:cd03249 12 SRPDVPILKGLSLTI--PPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGL------VS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPfeafnpltrideYLLATAHRFK---GAKSRAEKEAIAdVALQrvglsmAEIK--------------GRFSHELSGGQ 163
Cdd:cd03249 84 QEP------------VLFDGTIAENiryGKPDATDEEVEE-AAKK------ANIHdfimslpdgydtlvGERGSQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdaLNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDA 243
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTH 221
|
....*
gi 1817161977 244 RDVLE 248
Cdd:cd03249 222 DELMA 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
37-255 |
1.21e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.76 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDV--KAVRSRRDREAFMAkvqpvFQNPFEaFNPLTR 112
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIldLEPEERAHLGIFLA-----FQYPIE-IPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 113 IDEYLLA--TAHRFKGAKsraEKEAIADVALQRVGLSMAEIKGRFSHE-----LSGGQLQRIAVARALIPEPKLIVADEP 185
Cdd:CHL00131 102 ADFLRLAynSKRKFQGLP---ELDPLEFLEIINEKLKLVGMDPSFLSRnvnegFSGGEKKRNEILQMALLDSELAILDET 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 186 VSMVDASLRMSIVNLFRDLRDALNvSIVYITH-----DlataYYISDRVVIMRKGVVVESGDARDVLEHPKHAYS 255
Cdd:CHL00131 179 DSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrllD----YIKPDYVHVMQNGKIIKTGDAELAKELEKKGYD 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-251 |
2.93e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIhfdgtdvkaVRSRRDREAFMAKVqpvfqnpfeaf 107
Cdd:PRK09544 18 RVLSDVSLELKPGK--ILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQK----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 nplTRIDEYLLATAHRFKGAKSRAEKEAIADvALQRVglSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:PRK09544 76 ---LYLDTTLPLTVNRFLRLRPGTKKEDILP-ALKRV--QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVeSGDARDVLEHPK 251
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICC-SGTPEVVSLHPE 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-248 |
4.35e-16 |
|
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: 78.31 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiggffsrEKMKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSE--KADRGSI----------- 73
Cdd:TIGR03269 1 IEVKNLTKKF--------DGKEVLKNISFTI--EEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 74 -----HFDGTDVKAV-------------RSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLlatahrfkgaKSRAEKEA 135
Cdd:TIGR03269 71 yverpSKVGEPCPVCggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVL----------EALEEIGY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 136 IADVALQRVG--LSMAEIKGRFSH---ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNV 210
Cdd:TIGR03269 141 EGKEAVGRAVdlIEMVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 1817161977 211 SIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 248
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
43-241 |
5.99e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.00 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGtdvkavrSRRDREAFMAKVQPVFQnpFEAFNPLTRIDEYLLA 119
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNG-------QPRKPDQFQKCVAYVRQ--DDILLPGLTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 120 TAH---RFKGAKSRAEKEAiADVALQRVGLSMaeIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 196
Cdd:cd03234 105 TAIlrlPRKSSDAIRKKRV-EDVLLRDLALTR--IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1817161977 197 IVNLFRDLrdALNVSIVYIT-H----DLataYYISDRVVIMRKGVVVESG 241
Cdd:cd03234 182 LVSTLSQL--ARRNRIVILTiHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-248 |
7.38e-16 |
|
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: 74.96 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTklFPIGGffsrEKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:cd03251 1 VEFKNVT--FRYPG----DGPPVLRDISL--DIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREafmaKVQPVFQNPFeAFNplTRIDEYLLAtahrfkgAKSRAEKEAIADVA----LQRVGLSMAE----IKGRFSHE 158
Cdd:cd03251 73 SLRR----QIGLVSQDVF-LFN--DTVAENIAY-------GRPGATREEVEEAAraanAHEFIMELPEgydtVIGERGVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 159 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIvnlfrdlRDALN------VSIVyITHDLATayyI--SDRVV 230
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV-------QAALErlmknrTTFV-IAHRLST---IenADRIV 207
|
250
....*....|....*...
gi 1817161977 231 IMRKGVVVESGDARDVLE 248
Cdd:cd03251 208 VLEDGKIVERGTHEELLA 225
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
7-241 |
9.46e-16 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 77.05 E-value: 9.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPiggffSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 86
Cdd:TIGR02204 338 IEFEQVNFAYP-----ARPDQPALDGLNLTVRPG--ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 --RDREAFMAKVQPVFQNPFEAFNPLTRIDeyllATAHRFKgaksRAEKEAIADVALQRVGLSMAEIKGRFSHELSGGQL 164
Cdd:TIGR02204 411 elRARMALVPQDPVLFAASVMENIRYGRPD----ATDEEVE----AAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIvyITHDLATAYYiSDRVVIMRKGVVVESG 241
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLI--IAHRLATVLK-ADRIVVMDQGRIVAQG 556
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-249 |
9.69e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSRRDReafmAKVQPVFQnpFEAFNP 109
Cdd:PRK13537 23 VDGLSFHVQRG--ECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHAR----QRVGVVPQ--FDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATAHRFkgAKSRAEKEAIADVALQRVGL-SMAEIKGRfshELSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK13537 94 DFTVRENLLVFGRYF--GLSAAAARALVPPLLEFAKLeNKADAKVG---ELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 189 VDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13537 169 LDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-235 |
1.05e-15 |
|
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: 74.39 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPI---GGffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD--- 79
Cdd:COG4778 4 LLEVENLSKTFTLhlqGG----KRLPVLDGVSFSVAAG--ECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 80 --VKA-----VRSRRDREAFmakvqpVFQnpfeaF-NPLTRID------EYLLAtahrfKGAkSRAEKEAIADVALQRVG 145
Cdd:COG4778 78 dlAQAspreiLALRRRTIGY------VSQ-----FlRVIPRVSaldvvaEPLLE-----RGV-DREEARARARELLARLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 146 lsmaeIKGR--------FshelSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITH 217
Cdd:COG4778 141 -----LPERlwdlppatF----SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFH 210
|
250
....*....|....*...
gi 1817161977 218 DLATAYYISDRVVIMRKG 235
Cdd:COG4778 211 DEEVREAVADRVVDVTPF 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-231 |
1.54e-15 |
|
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: 74.37 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDvSFALSAD-----KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-------KAVRSRRDREAFM 93
Cdd:cd03237 5 TMKKTLG-EFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyiKADYEGTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 94 AKVQPVFQNPF---EAFNPLtrideyllatahrfkgaksraEKEAIADvalQRVglsmaeikgrfsHELSGGQLQRIAVA 170
Cdd:cd03237 84 SITKDFYTHPYfktEIAKPL---------------------QIEQILD---REV------------PELSGGELQRVAIA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 171 RALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 231
Cdd:cd03237 128 ACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-247 |
2.20e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR--DREAFMAKVQPVfqnpfeaf 107
Cdd:PRK11231 18 LNDLSLSLPTGK--ITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLT-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 nP----LTRIDEYLLATAHRFKGAKSRaEKEAIADVALQRVGLS-MAEikgRFSHELSGGQLQRIAVARALIPEPKLIVA 182
Cdd:PRK11231 88 -PegitVRELVAYGRSPWLSLWGRLSA-EDNARVNQAMEQTRINhLAD---RRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 183 DEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-247 |
2.22e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 33 VSFALSADkpEIFTIVGESGSGKSTL----AKMILGSekadrGSIHFDGTDVKAVRSR---RDReAFMAKVQ------PV 99
Cdd:PRK03695 15 LSAEVRAG--EILHLVGPNGAGKSTLlarmAGLLPGS-----GSIQFAGQPLEAWSAAelaRHR-AYLSQQQtppfamPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 100 FQnpfeafnpltrideYLlaTAHRFKGAKSRAEKEAIADVAlQRVGLSMaeiK-GRFSHELSGGQLQRIAVA-------R 171
Cdd:PRK03695 87 FQ--------------YL--TLHQPDKTRTEAVASALNEVA-EALGLDD---KlGRSVNQLSGGEWQRVRLAavvlqvwP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK03695 147 DINPAGQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-246 |
3.01e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIggffsrekMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrS 85
Cdd:PRK09700 5 YISMAGIGKSFGP--------VHALKSVNLTVY--PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY----N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRD-REAFMAKVQPVFQNpFEAFNPLTrIDEYLLATAH---RFKGAK--SRAEKEAIADVALQRVGL--SMAEIKGrfsh 157
Cdd:PRK09700 71 KLDhKLAAQLGIGIIYQE-LSVIDELT-VLENLYIGRHltkKVCGVNiiDWREMRVRAAMMLLRVGLkvDLDEKVA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 158 ELSGGQLQRIAVARALIPEPKLIVADEPVSmvdaSLRMSIVN-LF---RDLRDAlNVSIVYITHDLATAYYISDRVVIMR 233
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTS----SLTNKEVDyLFlimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMK 219
|
250
....*....|...
gi 1817161977 234 KGVVVESGDARDV 246
Cdd:PRK09700 220 DGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-249 |
5.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRG-SIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP- 103
Cdd:PRK13645 23 EFKALNNTSLTFKKNK--VTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEAFNPLTRIDeylLATAHRFKGAKSRAEKEAIADVaLQRVGLSMAEIKgRFSHELSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:PRK13645 101 YQLFQETIEKD---IAFGPVNLGENKQEAYKKVPEL-LKLVQLPEDYVK-RSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 184 EPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
43-241 |
5.37e-15 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 75.16 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPFeAFNPLTRiDEYLLAtah 122
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA----DPAWLRRQMGVVLQENV-LFSRSIR-DNIALC--- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 123 rfKGAKSRAEKEAIADVA-----LQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSI 197
Cdd:TIGR01846 555 --NPGAPFEHVIHAAKLAgahdfISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALI 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1817161977 198 VNLFRDLrdALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESG 241
Cdd:TIGR01846 633 MRNMREI--CRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-250 |
5.45e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiggffSREKMKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavr 84
Cdd:TIGR00958 478 LIEFQDVSFSYP-----NRPDVPVLKGLTFTL---HPgEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHrfKGAKSRAEKEAIADVALQRVGLSMAEIKGRFSHELSGGQL 164
Cdd:TIGR00958 546 VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 165 QRIAVARALIPEPKLIVADEPVSMVDAslrmSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDAR 244
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHK 698
|
....*.
gi 1817161977 245 DVLEHP 250
Cdd:TIGR00958 699 QLMEDQ 704
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-247 |
5.55e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMAKVQPVFQNPfeafnpltriDEYLLATahrfkg 126
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLALRQQVATVFQDP----------EQQIFYT------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 127 aksraekEAIADVA--LQRVGLSMAEIKGR------------FSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSM 188
Cdd:PRK13638 94 -------DIDSDIAfsLRNLGVPEAEITRRvdealtlvdaqhFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 189 VDASLRMSIVNLFRDLRDALNvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-271 |
6.08e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiggffsrEKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrs 85
Cdd:PRK13657 334 AVEFDDVSFSYD-------NSRQGVEDVSFEAKPG--QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 rrDREAFMAKVQPVFQNPFeAFNplTRIDEYLL-----ATAHRFKGAKSRAEkeAIADVALQRVGL-SMAEIKGRfshEL 159
Cdd:PRK13657 403 --TRASLRRNIAVVFQDAG-LFN--RSIEDNIRvgrpdATDEEMRAAAERAQ--AHDFIERKPDGYdTVVGERGR---QL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRmsivnlfRDLRDAL-----NVSIVYITHDLATAYYiSDRVVIMRK 234
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVKAALdelmkGRTTFIIAHRLSTVRN-ADRILVFDN 544
|
250 260 270
....*....|....*....|....*....|....*..
gi 1817161977 235 GVVVESGDARDVLEHPKHAYSIALKNAVLPPNPREAS 271
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQ 581
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-222 |
7.73e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSRRDREAFMAK-VQPVFQNpFEAFNPLTRIDEYLL 118
Cdd:PRK10584 34 KRgETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEEARAKLRAKhVGFVFQS-FMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 119 ATAHRfkGAKSRAEKEAIADVaLQRVGLSMaeikgRFSH---ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 195
Cdd:PRK10584 112 PALLR--GESSRQSRNGAKAL-LEQLGLGK-----RLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|....*..
gi 1817161977 196 SIVNLFRDLRDALNVSIVYITHDLATA 222
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
29-248 |
9.37e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADKPEIFTI------------VGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKV 96
Cdd:PRK10790 342 DIDNVSFAYRDDNLVLQNInlsvpsrgfvalVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG-VAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QpvfQNP------FEAFNPLTR-IDEyllatahrfkgaksraEK--EAIADVALQRVGLSMAE----IKGRFSHELSGGQ 163
Cdd:PRK10790 421 Q---QDPvvladtFLANVTLGRdISE----------------EQvwQALETVQLAELARSLPDglytPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDA 243
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*
gi 1817161977 244 RDVLE 248
Cdd:PRK10790 559 QQLLA 563
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-235 |
9.81e-15 |
|
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: 74.09 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPIGgffsrEKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGS-EKADRGSIHFDGtdvKAVR 84
Cdd:TIGR02633 257 ILEARNLTCWDVIN-----PHRKRVDDVSFSLR--RGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFING---KPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 SRRDREAFMAKVQPVFQN-PFEAFNPLTRIDEYL-LATAHRFKGaKSRAEKEAiadvALQRVGLSMAEIKGRFSH----- 157
Cdd:TIGR02633 327 IRNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCF-KMRIDAAA----ELQIIGSAIQRLKVKTASpflpi 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 158 -ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:TIGR02633 402 gRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-219 |
1.45e-14 |
|
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: 73.55 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR--RDREAFMAKVQPVFQnpfea 106
Cdd:TIGR02868 350 VLDGVSLDLPPG--ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLFD----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 107 fnplTRIDEYLLAtahrfkgAKSRAEKEAIADvALQRVGLS--MAEIKGRFSHE-------LSGGQLQRIAVARALIPEP 177
Cdd:TIGR02868 423 ----TTVRENLRL-------ARPDATDEELWA-ALERVGLAdwLRALPDGLDTVlgeggarLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1817161977 178 KLIVADEPVSMVDASLRMSIVnlfRDLRDALN-VSIVYITHDL 219
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELL---EDLLAALSgRTVVLITHHL 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-241 |
1.85e-14 |
|
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: 71.21 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLF-----------PIGGFFSREK--MKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSI 73
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligSLKSLFKRKYreVEALKGISFTIE--KGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 74 HfdgtdVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEY-LLATAHRFKGAKSRAEKEAIADValqrvgLSMAEIK 152
Cdd:cd03267 79 R-----VAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFyLLAAIYDLPPARFKKRLDELSEL------LDLEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 153 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM 232
Cdd:cd03267 148 DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
....*....
gi 1817161977 233 RKGVVVESG 241
Cdd:cd03267 228 DKGRLLYDG 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-241 |
2.34e-14 |
|
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: 70.52 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNP--FE 105
Cdd:cd03369 22 PVLKNVSFKVKAG--EKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDPtlFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 106 AF--NPLTRIDEYllatahrfkgaksrAEKEAIADVALQRVGLSmaeikgrfsheLSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:cd03369 96 GTirSNLDPFDEY--------------SDEEIYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 184 EPVSMV----DASLRMSIVNLFRdlrdalNVSIVYITHDLAT-AYYisDRVVIMRKGVVVESG 241
Cdd:cd03369 151 EATASIdyatDALIQKTIREEFT------NSTILTIAHRLRTiIDY--DKILVMDAGEVKEYD 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
47-277 |
2.71e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkaVRSRRDREAFMA----KVQPVFQnpfeafnpltridEYLLATAH 122
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGR----VLFDAEKGICLPpekrRIGYVFQ-------------DARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 123 RFKG-------AKSRAEKEAIadVALqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 195
Cdd:PRK11144 92 KVRGnlrygmaKSMVAQFDKI--VAL----LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 196 SIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPkhaysialknAVLPPNPR-EASAIL 274
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS----------AMRPWLPKeEQSSIL 235
|
...
gi 1817161977 275 RLR 277
Cdd:PRK11144 236 KVT 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-241 |
2.81e-14 |
|
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: 70.25 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFFSREKMK--------------AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGS 72
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKlgilgrkgevgefwALKDVSF--EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 73 IHFDGTdvkaVRSrrdreafmakvqpvfqnPFEA---FNP-LTRIDE-YLLATAHRFKGAKSRAEKEAIADvalqrvgls 147
Cdd:cd03220 79 VTVRGR----VSS-----------------LLGLgggFNPeLTGRENiYLNGRLLGLSRKEIDEKIDEIIE--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 148 MAEIkGRFSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAY 223
Cdd:cd03220 129 FSEL-GDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIK 206
|
250
....*....|....*...
gi 1817161977 224 YISDRVVIMRKGVVVESG 241
Cdd:cd03220 207 RLCDRALVLEKGKIRFDG 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-259 |
3.30e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 23 SREKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKAD--------RGSIHFDGTDVKAV---RSRRDREA 91
Cdd:PRK13547 10 ARRHRAILRDLS--LRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIdapRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 92 FMAKVQPVFqnPFEAfnpltriDEYLLATAH---RFKGAKSRAEKEaIADVALQRVGlsMAEIKGRFSHELSGGQLQRIA 168
Cdd:PRK13547 88 LPQAAQPAF--AFSA-------REIVLLGRYphaRRAGALTHRDGE-IAWQALALAG--ATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 169 VARAL---------IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 239
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250 260
....*....|....*....|..
gi 1817161977 240 SGDARDVL--EHPKHAYSIALK 259
Cdd:PRK13547 236 HGAPADVLtpAHIARCYGFAVR 257
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-237 |
3.37e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 70.19 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPFEAFNPL 110
Cdd:cd03248 32 DVSFTL---HPgEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 111 TRIDEYLLATAhRFKGAKSRAEKeAIADVALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:cd03248 105 QDNIAYGLQSC-SFECVKEAAQK-AHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1817161977 191 ASLRMSIVNLFRDlrDALNVSIVYITHDLATAYYiSDRVVIMRKGVV 237
Cdd:cd03248 183 AESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-245 |
3.61e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPiggffsreKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKAD--RGSIHFDGtDVKAV 83
Cdd:NF040905 1 ILEMRGITKTFP--------GVKALDDVN--LSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG-EVCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 RSRRDREAF--------MAKVqpvfqnpfeafnPLTRIDEYL-LATAHRFKGAKSRAEKEAIADVALQRVGLSmaEIKGR 154
Cdd:NF040905 70 KDIRDSEALgiviihqeLALI------------PYLSIAENIfLGNERAKRGVIDWNETNRRARELLAKVGLD--ESPDT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FSHELSGGQLQRIAVARALIPEPKLIVADEPVsmvdASLRMS----IVNLFRDLRDALNVSIVyITHDLATAYYISDRVV 230
Cdd:NF040905 136 LVTDIGVGKQQLVEIAKALSKDVKLLILDEPT----AALNEEdsaaLLDLLLELKAQGITSII-ISHKLNEIRRVADSIT 210
|
250
....*....|....*
gi 1817161977 231 IMRKGVVVESGDARD 245
Cdd:NF040905 211 VLRDGRTIETLDCRA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-254 |
4.85e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 28 KAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV----RSRRD-----REAFMAKVQP 98
Cdd:PRK10895 17 RVVEDVS--LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRARRGigylpQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQNpfeafnpltrideylLATAHRFKGAKSRAEKEAIADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPK 178
Cdd:PRK10895 95 VYDN---------------LMAVLQIRDDLSAEQREDRANELMEE--FHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 179 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL--EHPKHAY 254
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILqdEHVKRVY 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-249 |
5.50e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 8 ELDHVTKLFPI-----------GGFFSREK--MKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIH 74
Cdd:COG4586 3 EVENLSKTYRVyekepglkgalKGLFRREYreVEAVDDISF--TIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 75 FDGTDvkavrSRRDREAFMAKVQPVFQN---------PFEAFNpltrideyLLATAHRFKGAKSRAEKEAIADValqrvg 145
Cdd:COG4586 81 VLGYV-----PFKRRKEFARRIGVVFGQrsqlwwdlpAIDSFR--------LLKAIYRIPDAEYKKRLDELVEL------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 146 LSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYI 225
Cdd:COG4586 142 LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260
....*....|....*....|....
gi 1817161977 226 SDRVVIMRKGVVVESGDARDVLEH 249
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-227 |
5.73e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSfaLSADKPEIFTIVGESGSGKSTLAKM------ILGSEKADrGSIHFDG-----TDVKAVRSRRdreafmaKVQ 97
Cdd:PRK14243 25 AVKNVW--LDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGknlyaPDVDPVEVRR-------RIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 98 PVFQNPfeafNPLTRIDEYLLATAHRFKGAKsrAEKEAIADVALQRVGLsMAEIKGRFSHE---LSGGQLQRIAVARALI 174
Cdd:PRK14243 95 MVFQKP----NPFPKSIYDNIAYGARINGYK--GDMDELVERSLRQAAL-WDEVKDKLKQSglsLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 175 PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISD 227
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSD 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-247 |
7.38e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 27 MKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKV-QPVfqnpfe 105
Cdd:PRK11160 353 QPVLKGLSLQIKAG--EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA-ISVVsQRV------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 106 afnpltrideYLLATAHR--FKGAKSRAEKEAIADVaLQRVGLS------------MAEiKGRfshELSGGQLQRIAVAR 171
Cdd:PRK11160 424 ----------HLFSATLRdnLLLAAPNASDEALIEV-LQQVGLEklleddkglnawLGE-GGR---QLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLaTAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-241 |
8.43e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.35 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFFSREKMkaVDDVSFALsadKPEIFT-IVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDvkav 83
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL--LKNVSGKA---KPGELTaIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 84 rsrRDREAFMAKVQPVFQNpfEAFNP-LTrIDEYLLATAHrfkgaksraekeaiadvalqrvglsmaeIKGrfsheLSGG 162
Cdd:cd03213 75 ---LDKRSFRKIIGYVPQD--DILHPtLT-VRETLMFAAK----------------------------LRG-----LSGG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 163 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDL-ATAYYISDRVVIMRKGVVVESG 241
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-254 |
1.13e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 26 KMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV---KAVRSRRDREAFMAKVQPVFqn 102
Cdd:PRK11614 17 KIQALHEVS--LHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKIMREAVAIVPEGRRVF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 pfeafnplTRID-EYLLATAHRFkgAKSRAEKEAIADValQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:PRK11614 93 --------SRMTvEENLAMGGFF--AERDQFQERIKWV--YELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV--ESGDARDVLEHPKHAY 254
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDALLANEAVRSAY 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-231 |
1.66e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 34 SFALSAD-----KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIhfdGTDVKA------VRSRRDR--EAFMAKVQPVF 100
Cdd:PRK13409 352 DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKIsykpqyIKPDYDGtvEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPF---EAFNPLtRIDEYLlatahrfkgaksraEKEAiadvalqrvglsmaeikgrfsHELSGGQLQRIAVARALIPEP 177
Cdd:PRK13409 429 GSSYyksEIIKPL-QLERLL--------------DKNV---------------------KDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 178 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 231
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-235 |
2.14e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIggffsREKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEK-ADRGSIHFDGtdvKAVRS 85
Cdd:PRK13549 260 LEVRNLTAWDPV-----NPHIKRVDDVSFSLR--RGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG---KPVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVqpvfqnpfeAFNPLTR-----------IDEYLLATAHRFKGAkSRAEKEAIADVALQrvglSMAEIKGR 154
Cdd:PRK13549 330 RNPQQAIAQGI---------AMVPEDRkrdgivpvmgvGKNITLAALDRFTGG-SRIDDAAELKTILE----SIQRLKVK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FSH------ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDR 228
Cdd:PRK13549 396 TASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDR 474
|
....*..
gi 1817161977 229 VVIMRKG 235
Cdd:PRK13549 475 VLVMHEG 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-231 |
3.80e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 34 SFALSAD-----KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGT------DVKAVRSRRDREAFMAKVQPVFQN 102
Cdd:COG1245 353 GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqYISPDYDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 PF---EAFNPLtRIDEYLlatahrfkgaksraEKEaiadvalqrvglsmaeIKgrfshELSGGQLQRIAVARALIPEPKL 179
Cdd:COG1245 433 SYyktEIIKPL-GLEKLL--------------DKN----------------VK-----DLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 180 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 231
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
43-241 |
5.12e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMIL-----GSEKAdrGSIHFDGTDVKAVRSRRdREAFmakvqpVFQnpFEAFNPLTRIDEYL 117
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAfrspkGVKGS--GSVLLNGMPIDAKEMRA-ISAY------VQQ--DDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 118 LATAH-RFKGAKSRAEKEAIADVALQRVGLSMA---------EIKGrfsheLSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:TIGR00955 121 MFQAHlRMPRRVTKKEKRERVDEVLQALGLRKCantrigvpgRVKG-----LSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1817161977 188 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-185 |
6.10e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 31 DDVSFALSA-DKpeiFTIVGESGSGKSTLAKMILGSEKADRGSIHFDgtdvKAVR-SRRDREAFMAKVQPVFQNPFEAFN 108
Cdd:COG0488 15 DDVSLSINPgDR---IGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRiGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIDEYLLATAHRFKGAKSRAEK----------------EAIADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARA 172
Cdd:COG0488 88 ELRALEAELEELEAKLAEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVS-ELSGGWRRRVALARA 166
|
170
....*....|...
gi 1817161977 173 LIPEPKLIVADEP 185
Cdd:COG0488 167 LLSEPDLLLLDEP 179
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-242 |
6.43e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 33 VSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKAdRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNP--FEAfnpl 110
Cdd:PRK11174 369 LNFTLPAG--QRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELREL----DPESWRKHLSWVGQNPqlPHG---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 111 TRIDEYLLatahrfkgAKSRAEKEAIAD----------VALQRVGLSmAEIKGRfSHELSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK11174 438 TLRDNVLL--------GNPDASDEQLQQalenawvsefLPLLPQGLD-TPIGDQ-AAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 181 VADEPVSMVDAS---LRMSIVNlfrdlRDALNVSIVYITH---DLATAyyisDRVVIMRKGVVVESGD 242
Cdd:PRK11174 508 LLDEPTASLDAHseqLVMQALN-----AASRRQTTLMVTHqleDLAQW----DQIWVMQDGQIVQQGD 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-235 |
7.87e-13 |
|
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: 68.89 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFPigGFFSrekmKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvkavr 84
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSS----PAVDRLCVGV---RPgECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG------- 2000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 85 srrdrEAFMAKVQPVFQN-----PFEAFNPLTRIDEYLLATAhRFKGAKSRaEKEAIADVALQRVGLSMaeIKGRFSHEL 159
Cdd:TIGR01257 2001 -----KSILTNISDVHQNmgycpQFDAIDDLLTGREHLYLYA-RLRGVPAE-EIEKVANWSIQSLGLSL--YADRLAGTY 2071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 160 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM----SIVNLFRDLRdalnvSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
47-241 |
1.24e-12 |
|
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: 65.59 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFmaKVQPvfQNP--FEA---FN--PLTRI-DEYLL 118
Cdd:cd03244 35 IVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI--SIIP--QDPvlFSGtirSNldPFGEYsDEELW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 119 atahrfkgaksraekEAIADVALQRVGLSM-----AEIKGRFSHeLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 193
Cdd:cd03244 111 ---------------QALERVGLKEFVESLpggldTVVEEGGEN-LSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 194 RMSIVNLfrdLRDAL-NVSIVYITHDLATayyI--SDRVVIMRKGVVVESG 241
Cdd:cd03244 175 DALIQKT---IREAFkDCTVLTIAHRLDT---IidSDRILVLDKGRVVEFD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-235 |
1.59e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR-------------RDREAFMAKV 96
Cdd:PRK10762 268 VNDVSFTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisedRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QpVFQNpfeafNPLTRIDeYLLATAHRFKGAksrAEKEAIADValqrVGL------SMAEIKGrfshELSGGQLQRIAVA 170
Cdd:PRK10762 346 S-VKEN-----MSLTALR-YFSRAGGSLKHA---DEQQAVSDF----IRLfniktpSMEQAIG----LLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 171 RALIPEPKLIVADEPVSMVDASLRMSI---VNLFRdlrdALNVSIVYITHDLATAYYISDRVVIMRKG 235
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIyqlINQFK----AEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
47-217 |
2.66e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.75 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHF-DGTDVkavrsrrdreAFMAkvqpvfQNPFEafnPLTRIDEYLL--ATAHR 123
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------LFLP------QRPYL---PLGTLREALLypATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 124 FkgakSRAEKEAiadvALQRVGL----SMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSivn 199
Cdd:COG4178 455 F----SDAELRE----ALEAVGLghlaERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA--- 523
|
170
....*....|....*....
gi 1817161977 200 LFRDLRDAL-NVSIVYITH 217
Cdd:COG4178 524 LYQLLREELpGTTVISVGH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-245 |
3.46e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 23 SREKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsRRDREAFMAKVQPVFQN 102
Cdd:PRK09700 272 TSRDRKKVRDISFSVC--RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP---RSPLDAVKKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 103 PFE-AFNPLTRIDEYL-----LATAhRFKGAK---SRAEKEAIADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARAL 173
Cdd:PRK09700 347 RRDnGFFPNFSIAQNMaisrsLKDG-GYKGAMglfHEVDEQRTAENQRELLALKCHSVNQNIT-ELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 174 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVsIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 245
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-235 |
3.58e-12 |
|
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: 64.03 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvkavrsrrdREAFMAKvQP-----------VF 100
Cdd:cd03250 23 DINL--EVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQ-EPwiqngtireniLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 101 QNPFEAfnpltriDEYllatahrfkgaksraeKEAIADVALQR-----VGLSMAEI--KGRfshELSGGQLQRIAVARAL 173
Cdd:cd03250 89 GKPFDE-------ERY----------------EKVIKACALEPdleilPDGDLTEIgeKGI---NLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 174 IPEPKLIVADEPVSMVDASLRMSIVN--LFRDLRDalNVSIVYITHDLataYYIS--DRVVIMRKG 235
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQL---QLLPhaDQIVVLDNG 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-247 |
4.56e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 45 FT-IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreaFMAKVQPVFQNpfeAFNPLTRIDEYLLATA-- 121
Cdd:PRK10253 35 FTaIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE----VARRIGLLAQN---ATTPGDITVQELVARGry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 122 -HRFKGAKSRAEKEAIADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 200
Cdd:PRK10253 108 pHQPLFTRWRKEDEEAVTKAMQATGIT--HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1817161977 201 FRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-247 |
6.84e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDDVSFalSADKPEIFTIVGESGSGKSTLAKMIL----------------------------GSEK----- 67
Cdd:PTZ00265 1175 YISRPNVPIYKDLTF--SCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqGDEEqnvgm 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 68 ---------------------ADRGSIHFDGTDVKAVRSRRDREAFMAkvqpVFQNPFeAFNpLTRIDEYLLATAHRFKG 126
Cdd:PTZ00265 1253 knvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSI----VSQEPM-LFN-MSIYENIKFGKEDATRE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 127 AKSRAEKEAIADVALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRD 206
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1817161977 207 ALNVSIVYITHDLATAYYiSDRVVIM----RKGVVVESGDARDVL 247
Cdd:PTZ00265 1407 KADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAHGTHEEL 1450
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-264 |
7.96e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFA---------LSADKP--EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrdreAFMAKVQ 97
Cdd:PRK10575 13 ALRNVSFRvpgrtllhpLSLTFPagKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK----AFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 98 PVFQNPFEA----FNPLTRIDEYLLATA-HRFKGAKSRAEKEAIADVALQrvglsmaEIKGRFSHELSGGQLQRIAVARA 172
Cdd:PRK10575 89 YLPQQLPAAegmtVRELVAIGRYPWHGAlGRFGAADREKVEEAISLVGLK-------PLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 173 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP-- 250
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGEtl 241
|
250
....*....|....
gi 1817161977 251 KHAYSIALknAVLP 264
Cdd:PRK10575 242 EQIYGIPM--GILP 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-246 |
9.00e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSRRDREA----FMAKVQPVFQNPFEAf 107
Cdd:PRK15439 281 NISLEVRAG--EILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-LSTAQRLArglvYLPEDRQSSGLYLDA- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 108 nPLTRideYLLATAHRFKGAKSRAEKEAiadVALQRVGLSMAeIKgrFSHE------LSGGQLQRIAVARALIPEPKLIV 181
Cdd:PRK15439 357 -PLAW---NVCALTHNRRGFWIKPAREN---AVLERYRRALN-IK--FNHAeqaartLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 182 ADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVES--GDARDV 246
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGAltGAAINV 492
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-245 |
1.47e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFPIGGFfsrekmkAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsr 86
Cdd:PRK10522 323 LELRNVTFAYQDNGF-------SVGPINLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKVQPVFQnpfeafnpltriDEYLLataHRFKGAKSRAEKEAIADVALQRVGLS--MAEIKGRFSH-ELSGGQ 163
Cdd:PRK10522 390 EQPEDYRKLFSAVFT------------DFHLF---DQLLGPEGKPANPALVEKWLERLKMAhkLELEDGRISNlKLSKGQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 164 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDlaTAYYIS-DRVVIMRKGVVVE-SG 241
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD--DHYFIHaDRLLEMRNGQLSElTG 532
|
....
gi 1817161977 242 DARD 245
Cdd:PRK10522 533 EERD 536
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-245 |
1.84e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLFpiGGFfsrEKMKAVDdvsFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvkavrs 85
Cdd:PRK15439 11 LLCARSISKQY--SGV---EVLKGID---FTLHAG--EVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAFMAKVQP-----VFQNPFeAFNPLTrIDEYLLatahrFKGAKSRAEKEAIADValqrvglsMAEIKGRFSHELS 160
Cdd:PRK15439 73 NPCARLTPAKAHQlgiylVPQEPL-LFPNLS-VKENIL-----FGLPKRQASMQKMKQL--------LAALGCQLDLDSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 161 GGQL-----QRIAVARALIPEPKLIVADEPVsmvdASLR-MSIVNLFRDLRD--ALNVSIVYITHDLATAYYISDRVVIM 232
Cdd:PRK15439 138 AGSLevadrQIVEILRGLMRDSRILILDEPT----ASLTpAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVM 213
|
250
....*....|...
gi 1817161977 233 RKGVVVESGDARD 245
Cdd:PRK15439 214 RDGTIALSGKTAD 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-191 |
2.25e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 31 DDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsRRDREAFMAK---------VQPVFq 101
Cdd:PRK13538 18 SGLSFTLNAG--ELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDEYHQDllylghqpgIKTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NPFEafNpltrideylLATAHRFKGAKSRaekEAIADvALQRVGLSmaeikGR---FSHELSGGQLQRIAVARALIPEPK 178
Cdd:PRK13538 90 TALE--N---------LRFYQRLHGPGDD---EALWE-ALAQVGLA-----GFedvPVRQLSAGQQRRVALARLWLTRAP 149
|
170
....*....|...
gi 1817161977 179 LIVADEPVSMVDA 191
Cdd:PRK13538 150 LWILDEPFTAIDK 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-232 |
3.03e-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: 63.65 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSI-----------HFDGTDV----KAVRSRRDREAFmaKVQPVFQNPfEAFNP-- 109
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELqdyfKKLANGEIKVAH--KPQYVDLIP-KVFKGtv 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 ---LTRIDEyllatahrfkgaksRAEKEAIADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 186
Cdd:COG1245 181 relLEKVDE--------------RGKLDELAEK------LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1817161977 187 SMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIM 232
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
146-232 |
3.15e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 146 LSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAYYI 225
Cdd:PRK13409 200 LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYL 277
|
....*..
gi 1817161977 226 SDRVVIM 232
Cdd:PRK13409 278 ADNVHIA 284
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
43-241 |
3.46e-11 |
|
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: 63.88 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFqnpfeaFNPLTrIDEYLLATAh 122
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNIL------FHHLT-VAEHILFYA- 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 123 RFKGaKSRAEKEAIADVALQRVGLSMAeiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFR 202
Cdd:TIGR01257 1029 QLKG-RSWEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....*....
gi 1817161977 203 DLRDALnvSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:TIGR01257 1106 KYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-238 |
4.49e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKVqpvfqnpfeAFNPLTRIDEY 116
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAGI---------MLCPEDRKAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLATA-------------HRFKGAKSRAEKEA-IADVALQRVglsmaEIKGRfSHE-----LSGGQLQRIAVARALIPEP 177
Cdd:PRK11288 342 IIPVHsvadninisarrhHLRAGCLINNRWEAeNADRFIRSL-----NIKTP-SREqlimnLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 178 KLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-239 |
5.38e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 12 VTKLFPIGGffSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDgtdvkavrsrrdrea 91
Cdd:COG2401 30 VLEAFGVEL--RVVERYVLRDLNLEIEPG--EIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 92 fmakvqpVFQNPFEAFNPLtrIDEYllatahrfkgAKSRAEKEAIAdvALQRVGLSMAEIKGRFSHELSGGQLQRIAVAR 171
Cdd:COG2401 91 -------VPDNQFGREASL--IDAI----------GRKGDFKDAVE--LLNAVGLSDAVLWLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 172 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLAtAYYISDRVVIMRKGVVVE 239
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVI-DDLQPDLLIFVGYGGVPE 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
37-235 |
7.85e-11 |
|
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: 59.64 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 37 LSADKPEIFTIVGESGSGKSTLAKMILGSEKADRgsihfdgtdvkavrsrrdreafMAKVQPVFqnpfeAFNPLTRIDEY 116
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR----------------------LISFLPKF-----SRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 llatahrfkgaksraekEAIADVALQRVGLsmaeikGRFSHELSGGQLQRIAVARALI--PEPKLIVADEPVSMVDASLR 194
Cdd:cd03238 69 -----------------QFLIDVGLGYLTL------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1817161977 195 MSIVNLFRDLRDaLNVSIVYITHDLATAYYiSDRVVIMRKG 235
Cdd:cd03238 126 NQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-239 |
8.51e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKlfpigGFFSRekmKAVDDVSFALsaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFdGTDVKAvrs 85
Cdd:COG0488 315 VLELEGLSK-----SYGDK---TLLDDLSLRI--DRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 rrdreAFMAKVQpvfqnpfEAFNPLTRIDEYLLAtahrfkGAKSRAEKEAIAdvALQRVGLSMAEIKgRFSHELSGGQLQ 165
Cdd:COG0488 381 -----GYFDQHQ-------EELDPDKTVLDELRD------GAPGGTEQEVRG--YLGRFLFSGDDAF-KPVGVLSGGEKA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 166 RIAVARALIPEPKLIVADEP-----VSMVDAslrmsivnlfrdLRDALNV---SIVYITHD---LATayyISDRVVIMRK 234
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPtnhldIETLEA------------LEEALDDfpgTVLLVSHDryfLDR---VATRILEFED 504
|
....*
gi 1817161977 235 GVVVE 239
Cdd:COG0488 505 GGVRE 509
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-249 |
8.63e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 62.14 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 31 DDVSFALSADKPeI-----FT--------IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKV- 96
Cdd:COG5265 361 ENVSFGYDPERP-IlkgvsFEvpagktvaIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA-IGIVp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 Q-PVFQNPFEAFNpltrIdEYLLATAhrfkgakSRAEKEAIADvalqrvglsMAEIkgrfsHE----------------- 158
Cdd:COG5265 439 QdTVLFNDTIAYN----I-AYGRPDA-------SEEEVEAAAR---------AAQI-----HDfieslpdgydtrvgerg 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 159 --LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIvnlfrdlRDALNV------SIVyITHDLATayyI--SDR 228
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI-------QAALREvargrtTLV-IAHRLST---IvdADE 561
|
250 260
....*....|....*....|.
gi 1817161977 229 VVIMRKGVVVESGDARDVLEH 249
Cdd:COG5265 562 ILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-235 |
2.96e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 12 VTKLFPiggffsreKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREA 91
Cdd:PRK10982 4 ISKSFP--------GVKALDNVN--LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 92 FMAKVQPVFQNpFEAFNPLTRIDEYLLAtahRF--KG-----AKSRAEKEAIADV------ALQRVGlsmaeikgrfshE 158
Cdd:PRK10982 71 LENGISMVHQE-LNLVLQRSVMDNMWLG---RYptKGmfvdqDKMYRDTKAIFDEldididPRAKVA------------T 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 159 LSGGQLQRIAVARALIPEPKLIVADEPVSmvdaSLRMSIVN-LF---RDLRDAlNVSIVYITHDLATAYYISDRVVIMRK 234
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTS----SLTEKEVNhLFtiiRKLKER-GCGIVYISHKMEEIFQLCDEITILRD 209
|
.
gi 1817161977 235 G 235
Cdd:PRK10982 210 G 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-247 |
4.49e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEKADrgsiHFDGTDVkaVRSRRDREAFMAKVQPVFQNPFeAFNPLTRIDEYLLATAH 122
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTIL--ANNRKPTKQILKRTGFVTQDDI-LYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 123 RFKGAKSRAEKEAIADVALQRVGLSMAE---IKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 199
Cdd:PLN03211 168 RLPKSLTKQEKILVAESVISELGLTKCEntiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1817161977 200 LFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 247
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-232 |
5.05e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEKADRGSI-----------HFDGT------------DVKAVRsrrdreafmaKVQPV 99
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSelqnyftkllegDVKVIV----------KPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 100 FQNPfEAFNP-----LTRIDEyllatahrfkgaksRAEKEAIADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALI 174
Cdd:cd03236 97 DLIP-KAVKGkvgelLKKKDE--------------RGKLDELVDQ------LELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1817161977 175 PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHDLATAYYISDRVVIM 232
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
47-238 |
8.52e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDgTDVKAVRSRRDR-----------------------EAFMAKVQPVFQNP 103
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQDPprnvegtvydfvaegieeqaeylKRYHDISHLVETDP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 104 FEA-FNPLTRIDEYL-LATAHRFKgakSRaekeaIADVaLQRVGLSmAEIKgrfSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:PRK11147 113 SEKnLNELAKLQEQLdHHNLWQLE---NR-----INEV-LAQLGLD-PDAA---LSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 182 ADEPVSMVDASlrmSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVV 238
Cdd:PRK11147 180 LDEPTNHLDIE---TIEWLEGFLKT-FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-250 |
8.97e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR--SRRDREAFmakvqpVFQNPFe 105
Cdd:PRK10789 330 ALENVNFTL---KPgQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAV------VSQTPF- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 106 AFNPltrideyllATAHRFKGAKSRAEKEAIADVA-LQRVGLSMAEIKGRFSHE-------LSGGQLQRIAVARALIPEP 177
Cdd:PRK10789 400 LFSD---------TVANNIALGRPDATQQEIEHVArLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 178 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyiTHDLaTAYYISDRVVIMRKGVVVESGDARDVLEHP 250
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS--AHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-192 |
1.69e-09 |
|
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: 56.35 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 33 VSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTR 112
Cdd:cd03231 19 LSFTLAAG--EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 113 IdeyllataHRFKGaksraeKEAIADvALQRVGLSMAEikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDAS 192
Cdd:cd03231 97 W--------HADHS------DEQVEE-ALARVGLNGFE--DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-204 |
2.31e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 32 DVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAfMAKVQPvfQNpfeAFNPLT 111
Cdd:PRK13539 20 GLSFTLAAG--EALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEA-CHYLGH--RN---AMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 112 RIDEYLLATAhRFKGAKSRAEKEAIADVALQRVglsmAEIKGRfshELSGGQLQRIAVARalipepkLIVADEPVSMVD- 190
Cdd:PRK13539 89 TVAENLEFWA-AFLGGEELDIAAALEAVGLAPL----AHLPFG---YLSAGQKRRVALAR-------LLVSNRPIWILDe 153
|
170
....*....|....*.
gi 1817161977 191 --ASLRMSIVNLFRDL 204
Cdd:PRK13539 154 ptAALDAAAVALFAEL 169
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-235 |
2.81e-09 |
|
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: 56.19 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 18 IGGFFS-REKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKV 96
Cdd:cd03290 4 TNGYFSwGSGLATLSNINIRIPTG--QLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 QPVFQNPFEafnpLTRIDEYLLATAHRFKGAKSRAEKEAIA---DVALQRVGlSMAEIkGRFSHELSGGQLQRIAVARAL 173
Cdd:cd03290 82 AYAAQKPWL----LNATVEENITFGSPFNKQRYKAVTDACSlqpDIDLLPFG-DQTEI-GERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 174 IPEPKLIVADEPVSMVDASL-----RMSIVNLFRDLRDalnvSIVYITHDLATAYYiSDRVVIMRKG 235
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
41-231 |
2.85e-09 |
|
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: 55.27 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsrrdreafmakvqpvfqnpfeAFNPltrideyllat 120
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------VYKP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 121 ahrfkgaksraekeaiadvalQRVglsmaeikgrfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 200
Cdd:cd03222 68 ---------------------QYI-------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|.
gi 1817161977 201 FRDLRDALNVSIVYITHDLATAYYISDRVVI 231
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-241 |
4.17e-09 |
|
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: 55.35 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 24 REKMKAVDDVSFALsadKP-EIFTIVGESGSGKSTLAKMI---LGSEKADRGSIHFDGTDVKAVRSRRDREAfmakvqpV 99
Cdd:cd03233 17 RSKIPILKDFSGVV---KPgEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEI-------I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 100 FQNPFEAFNPLTRIDEyLLATAHRFKGaksraekeaiadvalqrvglsmaeikGRFSHELSGGQLQRIAVARALIPEPKL 179
Cdd:cd03233 87 YVSEEDVHFPTLTVRE-TLDFALRCKG--------------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 180 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLA-TAYYISDRVVIMRKGVVVESG 241
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-218 |
6.54e-09 |
|
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: 56.48 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 7 LELDHVTKLFpiggffsREKMkAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFdGTDVKAVRSR 86
Cdd:TIGR03719 323 IEAENLTKAF-------GDKL-LIDDLSFKLP--PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 87 RDREAFMAKvqpvfQNPFEAF---NPLTRIDEYLLAT-----AHRFKGAKSRaekeaiadvalQRVGlsmaeikgrfshE 158
Cdd:TIGR03719 392 QSRDALDPN-----KTVWEEIsggLDIIKLGKREIPSrayvgRFNFKGSDQQ-----------KKVG------------Q 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 159 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDaslrmsiVNLFRDLRDALNV---SIVYITHD 218
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEEALLNfagCAVVISHD 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-281 |
2.83e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 33 VSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQ-PVFQNPFEAFNplt 111
Cdd:PLN03232 1255 LSFFVSPS--EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQsPVLFSGTVRFN--- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 112 rIDEYllaTAHRFKGAKSRAEKEAIADVALQR-VGLSMAEIKGrfSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:PLN03232 1330 -IDPF---SEHNDADLWEALERAHIKDVIDRNpFGLDAEVSEG--GENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 191 ASLRMSIVNLFRDlrDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYSiALKNAVLPPNPREA 270
Cdd:PLN03232 1404 VRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF-RMVHSTGPANAQYL 1479
|
250
....*....|.
gi 1817161977 271 SAILRLRQRNA 281
Cdd:PLN03232 1480 SNLVFERRENG 1490
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
156-217 |
3.45e-08 |
|
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: 52.16 E-value: 3.45e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 156 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdalnVSIVYITH 217
Cdd:cd03223 89 DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
43-245 |
4.18e-08 |
|
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: 54.03 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 43 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAkvqpVFQ---------NPFEAFNPlTRI 113
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSA----VFSdfhlfdrllGLDGEADP-ARA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 114 DEYLlataHRFKgaksRAEKEAIADvalqrvglsmaeikGRFSH-ELSGGQLQRIAVARALIPEPKLIVADE------PV 186
Cdd:COG4615 434 RELL----ERLE----LDHKVSVED--------------GRFSTtDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 187 smvdaslrmsivnlFR---------DLRdALNVSIVYITHDlaTAYY-ISDRVVIMRKGVVVE-SGDARD 245
Cdd:COG4615 492 --------------FRrvfytellpELK-ARGKTVIAISHD--DRYFdLADRVLKMDYGKLVElTGPAAL 544
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
47-255 |
4.55e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAF-MAKVQPVFqnpfeaFNPLTR--IDEYLLAtahr 123
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFsMIPQDPVL------FDGTVRqnVDPFLEA---- 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 124 fkgakSRAEKEAiadvALQRVGLS---MAEIKGRFSHELSG------GQLQRIAVARALIPE-PKLIVADEPVSMVDASL 193
Cdd:PTZ00243 1411 -----SSAEVWA----ALELVGLRervASESEGIDSRVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEATANIDPAL 1481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 194 RMSIVNLFRDLRDALNVsiVYITHDLAT-AYYisDRVVIMRKGVVVESGDARDVLEHPKHAYS 255
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTV--ITIAHRLHTvAQY--DKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-246 |
4.83e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 23 SREKMKAVDDVSFALSADKPEIFtiVGESGSGKSTLAKMILGSEKADRGSIHF-DGTDVKAVRSRRDReafmAKVQPVFQ 101
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAF--VGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWR----SKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 NPFEAFNPLTRIDEYLLAT--------------------------AHRFKGA----------------KSRAEKEAIADV 139
Cdd:PTZ00265 468 DPLLFSNSIKNNIKYSLYSlkdlealsnyynedgndsqenknkrnSCRAKCAgdlndmsnttdsneliEMRKNYQTIKDS 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 140 ALQRVGLSM-------------AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRD 206
Cdd:PTZ00265 548 EVVDVSKKVlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1817161977 207 ALNVSIVYITHDLATAYYISDRVVIMRKgvvvESGDARDV 246
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLSNR----ERGSTVDV 663
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-257 |
7.85e-08 |
|
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: 53.41 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmAKVQPVFQNPFeAFNPLTRIDeyllatahrFKG 126
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----FKITIIPQDPV-LFSGSLRMN---------LDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 127 AKSRAEKEAIADVALQRVGLSMAEIKGRFSHE-------LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 199
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 200 LFRDLRDalNVSIVYITHDLATayyISD--RVVIMRKGVVVESGDARDVLEHPKHAYSIA 257
Cdd:TIGR00957 1463 TIRTQFE--DCTVLTIAHRLNT---IMDytRVIVLDKGEVAEFGAPSNLLQQRGIFYSMA 1517
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-249 |
2.37e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMK---AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGT-DVKAVRSRRDreafmakv 96
Cdd:PRK13545 28 FFRSKDGEyhyALNNISF--EVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSGLN-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 97 qpvfqnpfeafNPLTRIDEYLLatahrfKGAKSRAEKEAIADVALQRVglSMAEIkGRFSHE----LSGGQLQRIAVARA 172
Cdd:PRK13545 98 -----------GQLTGIENIEL------KGLMMGLTKEKIKEIIPEII--EFADI-GKFIYQpvktYSSGMKSRLGFAIS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 173 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-190 |
2.99e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 22 FSREKMKAVDDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsRRDREAFMAKVQPVfq 101
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAG--EALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYLGHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 102 npfeafnPLTRIDEYLLATAHRFKGAKSRAEKEAIADvALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 181
Cdd:PRK13543 91 -------PGLKADLSTLENLHFLCGLHGRRAKQMPGS-ALAIVGL--AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 1817161977 182 ADEPVSMVD 190
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
41-242 |
4.54e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KP-EIFTIVGESGSGKSTLAKMILGSE--KADRGSIHFDGTDVKAV--RSRRDREAFMAKVQPV----FQNPFEAFNPLT 111
Cdd:PRK09580 25 RPgEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELspEDRAGEGIFMAFQYPVeipgVSNQFFLQTALN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 112 RIDEYL-LATAHRFKGAKSRAEKEAIADVALQRVGLSMAEikgrfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:PRK09580 105 AVRSYRgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNV-------GFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1817161977 191 ASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYIS-DRVVIMRKGVVVESGD 242
Cdd:PRK09580 178 IDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
129-241 |
9.32e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 129 SRAEKEAIADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDL-RDA 207
Cdd:NF000106 117 SRKDARARADELLER--FSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDG 194
|
90 100 110
....*....|....*....|....*....|....
gi 1817161977 208 lnVSIVYITHDLATAYYISDRVVIMRKGVVVESG 241
Cdd:NF000106 195 --ATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
31-218 |
1.19e-06 |
|
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: 47.06 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 31 DDVSFALSADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkavrsrrdreafmakvqpvfqnpfeafnpl 110
Cdd:cd03221 17 KDISLTINPG--DRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 111 TRIdeyllatahrfkgaksraekeaiadvalqrvglsmaeikGRFSHeLSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:cd03221 63 VKI---------------------------------------GYFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*...
gi 1817161977 191 ASLRMSIVNLFRDLRDALnvsiVYITHD 218
Cdd:cd03221 103 LESIEALEEALKEYPGTV----ILVSHD 126
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-190 |
1.62e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--VRSRRdREAFMAkvQP-------- 98
Cdd:NF033858 281 AVDHVSFRIR--RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdIATRR-RVGYMS--QAfslygelt 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQNpfeafnpltrideyLLATAHRFKGAKSRAEkEAIADVaLQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPK 178
Cdd:NF033858 356 VRQN--------------LELHARLFHLPAAEIA-ARVAEM-LERFDL--ADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170
....*....|..
gi 1817161977 179 LIVADEPVSMVD 190
Cdd:NF033858 418 LLILDEPTSGVD 429
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-253 |
1.70e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 21 FFSREKMKAVDDVSfaLSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSihfdgtdVKAVRSrrdreafMAKV--QP 98
Cdd:PTZ00243 667 FFELEPKVLLRDVS--VSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-------VWAERS-------IAYVpqQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 99 VFQNPFEAFNPL--TRIDEYLLATAHRFkgakSRAEkeaiADVALQRVGLSmAEIkGRFSHELSGGQLQRIAVARALIPE 176
Cdd:PTZ00243 731 WIMNATVRGNILffDEEDAARLADAVRV----SQLE----ADLAQLGGGLE-TEI-GEKGVNLSGGQKARVSLARAVYAN 800
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 177 PKLIVADEPVSMVDASLRMSIV-NLFRD-LRDALNVSIVYITHDLATAyyisDRVVIMRKGVVVESGDARDVLEHPKHA 253
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGERVVeECFLGaLAGKTRVLATHQVHVVPRA----DYVVALGDGRVEFSGSSADFMRTSLYA 875
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-249 |
3.31e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KP-EIFTIVGESGSGKSTLAKMIL----GSEKADRGSIHFDGTDVKAVRSR-RDREAFMAKVQPVFQNpfeafnpLTRID 114
Cdd:TIGR00956 85 KPgELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHyRGDVVYNAETDVHFPH-------LTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 115 EylLATAHRFKGAKSRAE-------KEAIADVALQRVGLSM---AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADE 184
Cdd:TIGR00956 158 T--LDFAARCKTPQNRPDgvsreeyAKHIADVYMATYGLSHtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817161977 185 PVSMVDASLRMSIVNLFRDLRDALN-VSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQY 301
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-190 |
3.97e-06 |
|
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: 48.37 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 1 MSSHFLLELDHVTKLFPIGGFFSREKMKA---------VDDVSFALSADKPeiFTIVGESGSGKSTLAKMILGSEKADrG 71
Cdd:TIGR01271 1197 LSTVLVIENPHAQKCWPSGGQMDVQGLTAkyteagravLQDLSFSVEGGQR--VGLLGRTGSGKSTLLSALLRLLSTE-G 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 72 SIHFDGTDVKAVRSRRDREAFMAKVQPVFqnpfeAFNPLTR--IDEYllatahrfkgakSRAEKEAIADVAlQRVGL-SM 148
Cdd:TIGR01271 1274 EIQIDGVSWNSVTLQTWRKAFGVIPQKVF-----IFSGTFRknLDPY------------EQWSDEEIWKVA-EEVGLkSV 1335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1817161977 149 AEI---KGRFSHE-----LSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:TIGR01271 1336 IEQfpdKLDFVLVdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-235 |
6.59e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmakvqpvfqnpfeafnpltrideyllat 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 121 ahrfkgaksraekeaiadvalqrvglsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 200
Cdd:smart00382 51 ----------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1817161977 201 FRDLRDAL-----NVSIVYITHDL-----ATAYYISDRVVIMRKG 235
Cdd:smart00382 103 EELRLLLLlksekNLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
47-241 |
8.60e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGS-EKADRGSIHFDGTdvkavrsrrdrEAFMAKVQPVFqnpfeafNPLTRiDEYLLatahrfk 125
Cdd:PLN03232 648 IVGGTGEGKTSLISAMLGElSHAETSSVVIRGS-----------VAYVPQVSWIF-------NATVR-ENILF------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 126 GAKSRAEK--EAIADVALQR-----VGLSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIV 198
Cdd:PLN03232 702 GSDFESERywRAIDVTALQHdldllPGRDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1817161977 199 N--LFRDLRDALNVSIVYITHDLAtayyISDRVVIMRKGVVVESG 241
Cdd:PLN03232 781 DscMKDELKGKTRVLVTNQLHFLP----LMDRIILVSEGMIKEEG 821
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-237 |
1.45e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 6 LLELDHVTKLfpiggffsreKMKAVDDVSFALSadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRS 85
Cdd:PRK10982 250 ILEVRNLTSL----------RQPSIRDVSFDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 86 RRDREAF---MAKVQP------VFQNPFEAFNPL-TRIDEYLLATAhRFKGAKSRAEKEAIADvalqrvglSM-AEIKGR 154
Cdd:PRK10982 315 HNANEAInhgFALVTEerrstgIYAYLDIGFNSLiSNIRNYKNKVG-LLDNSRMKSDTQWVID--------SMrVKTPGH 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 155 FSH--ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIM 232
Cdd:PRK10982 386 RTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
....*
gi 1817161977 233 RKGVV 237
Cdd:PRK10982 465 SNGLV 469
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-73 |
1.46e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 7 LELDHVTKlfpigGFFSRekmKAVDDVSFALsadkPE--IFTIVGESGSGKSTLAKMILGSEKADRGSI 73
Cdd:PRK11819 325 IEAENLSK-----SFGDR---LLIDDLSFSL----PPggIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-248 |
1.46e-05 |
|
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: 46.48 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 34 SFALSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkavrsrrdreafMAKVqpvfqnPFEAFNPLTRI 113
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYV------PQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 114 DEYLLaTAHRFKGAKSRAEKEA---IADVALQRVGlSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:TIGR00957 716 RENIL-FGKALNEKYYQQVLEAcalLPDLEILPSG-DRTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 191 ASLRMSIVNLFRDLRDAL-NVSIVYITHDLAtayYI--SDRVVIMRKGVVVESGDARDVLE 248
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGVLkNKTRILVTHGIS---YLpqVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-190 |
1.91e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 30 VDDVSFALSADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsrRDREAFmaKVQPVFQNPFEAFNP 109
Cdd:PRK13540 17 LQQISFHLPAGG--LLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTY--QKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATAHRFKGAksraekeaiadvalqrvgLSMAEIKGRFSHE---------LSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGA------------------VGITELCRLFSLEhlidypcglLSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|
gi 1817161977 181 VADEPVSMVD 190
Cdd:PRK13540 150 LLDEPLVALD 159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-241 |
1.45e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGsEKADRGsihfDGTDVKavrsrRDREAFMAKVQPVFqnpfeafNPLTRiDEYLLatahrfkG 126
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLG-ELPPRS----DASVVI-----RGTVAYVPQVSWIF-------NATVR-DNILF-------G 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 127 AKSRAEK--EAIADVALQR-----VGLSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 199
Cdd:PLN03130 703 SPFDPERyeRAIDVTALQHdldllPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1817161977 200 lfRDLRDAL-NVSIVYITHDLataYYIS--DRVVIMRKGVVVESG 241
Cdd:PLN03130 782 --KCIKDELrGKTRVLVTNQL---HFLSqvDRIILVHEGMIKEEG 821
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
47-218 |
2.22e-04 |
|
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: 42.61 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHF-DGTDV------------KAVRsrrdrEAFMAKVQPVfQNPFEAFNPLTri 113
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgylpqepqldptKTVR-----ENVEEGVAEI-KDALDRFNEIS-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 114 DEYLLATAHRFKGAKSRAEKEAIADVA----LQRvGLSMAEIKGRFS------HELSGGQLQRIAVARALIPEPKLIVAD 183
Cdd:TIGR03719 108 AKYAEPDADFDKLAAEQAELQEIIDAAdawdLDS-QLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1817161977 184 EPVSMVDASlrmSIVNLFRDLRDaLNVSIVYITHD 218
Cdd:TIGR03719 187 EPTNHLDAE---SVAWLERHLQE-YPGTVVAVTHD 217
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
31-227 |
2.96e-04 |
|
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: 41.45 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 31 DDVSFALSAdkpeiFTIV-GESGSGKSTLAKMILG---SEKADRGSIHFDGTDvkavrsRRDREAFMAKVQPVFQNPF-- 104
Cdd:cd03271 14 IDVDIPLGV-----LTCVtGVSGSGKSSLINDTLYpalARRLHLKKEQPGNHD------RIEGLEHIDKVIVIDQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 105 -EAFNPLT-------------------RIDEYLLATahRFKGaKSraekeaIADV-----------------------AL 141
Cdd:cd03271 83 tPRSNPATytgvfdeirelfcevckgkRYNRETLEV--RYKG-KS------IADVldmtveealeffenipkiarklqTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 142 QRVGLSMAEIkGRFSHELSGGQLQRIAVARALI---PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHD 218
Cdd:cd03271 154 CDVGLGYIKL-GQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHN 231
|
250
....*....|..
gi 1817161977 219 L---ATAYYISD 227
Cdd:cd03271 232 LdviKCADWIID 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-190 |
6.37e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 6.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 131 AEKEAIADVAlqrvGLSM-AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 190
Cdd:PLN03073 320 AEARAASILA----GLSFtPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-249 |
1.55e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 29 AVDDVSFalSADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtDVKAVrsrrdreAFMAKVQpvfqnpfeafN 108
Cdd:PRK13546 39 ALDDISL--KAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVI-------AISAGLS----------G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 109 PLTRIDEYllatahRFK----GAKSRAEKEAIADValqrvgLSMAEIkGRFSHE----LSGGQLQRIAVARALIPEPKLI 180
Cdd:PRK13546 99 QLTGIENI------EFKmlcmGFKRKEIKAMTPKI------IEFSEL-GEFIYQpvkkYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 181 VADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 249
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-255 |
1.98e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 47 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQ-PVFQNPFEAFNpLTRIDEY-------LL 118
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQaPVLFSGTVRFN-LDPFNEHndadlweSL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 119 ATAHrFKGAKSRAEKEAIADVAlqrvglsmaEIKGRFSHelsgGQLQRIAVARALIPEPKLIVADEPVSMVD----ASLR 194
Cdd:PLN03130 1349 ERAH-LKDVIRRNSLGLDAEVS---------EAGENFSV----GQRQLLSLARALLRRSKILVLDEATAAVDvrtdALIQ 1414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817161977 195 MSIVNLFRdlrdalNVSIVYITHDLATAyyI-SDRVVIMRKGVVVESGDARDVLEHPKHAYS 255
Cdd:PLN03130 1415 KTIREEFK------SCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-190 |
2.57e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 2.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1817161977 137 ADVALQRVGLSMAEIKGRFsHELSGGQlQRIA-VARALIPEPKLIVADEPVSMVD 190
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPF-HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
158-217 |
4.34e-03 |
|
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: 38.58 E-value: 4.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 158 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDlrdaLNVSIVYITH 217
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-251 |
4.70e-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: 38.46 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 124 FKGAKSRAEKEAIADVALQR----------VGLSMAEIkGRFSHELSGGQLQRIAVARALIPEPK--LIVADEPVSMVDA 191
Cdd:TIGR00630 445 FNQLTLTPEEKKIAEEVLKEirerlgflidVGLDYLSL-SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQ 523
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817161977 192 SLRMSIVNLFRDLRDALNVSIVyITHD---LATAyyisDRVVIMRKGV------VVESGDARDVLEHPK 251
Cdd:TIGR00630 524 RDNRRLINTLKRLRDLGNTLIV-VEHDedtIRAA----DYVIDIGPGAgehggeVVASGTPEEILANPD 587
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
38-81 |
5.78e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 36.96 E-value: 5.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1817161977 38 SADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 81
Cdd:pfam06414 7 SQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFR 50
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
41-242 |
7.08e-03 |
|
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: 37.24 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 41 KPEIFTIVGESGSGKSTLAKMILGSEK-----------ADRGSIHFDGTDVKAVRSRRdrEAFMAKVQPVFQNPFEAFNP 109
Cdd:cd03270 20 RNKLVVITGVSGSGKSSLAFDTIYAEGqrryveslsayARQFLGQMDKPDVDSIEGLS--PAIAIDQKTTSRNPRSTVGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 110 LTRIDEYLLATAHRFkGAKSRAEkeaiadvALQRVGLSMAEIkGRFSHELSGGQLQRIAVARALipEPKLI----VADEP 185
Cdd:cd03270 98 VTEIYDYLRLLFARV-GIRERLG-------FLVDVGLGYLTL-SRSAPTLSGGEAQRIRLATQI--GSGLTgvlyVLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1817161977 186 VSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATaYYISDRVVIMRKGVVVESGD 242
Cdd:cd03270 167 SIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHDEDT-IRAADHVIDIGPGAGVHGGE 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-241 |
8.17e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 38 SADKPEIFT-IVGESGSGKSTLAKMILGSEKAdrGSIhfDGtDVKAVRSRRDREAFMAKVQPVFQNpfEAFNPLTRIDEY 116
Cdd:PLN03140 901 GAFRPGVLTaLMGVSGAGKTTLMDVLAGRKTG--GYI--EG-DIRISGFPKKQETFARISGYCEQN--DIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817161977 117 LLATAH-RFKGAKSRAEKEAIADVALQRVGLS--------MAEIKGrfsheLSGGQLQRIAVARALIPEPKLIVADEPVS 187
Cdd:PLN03140 974 LIYSAFlRLPKEVSKEEKMMFVDEVMELVELDnlkdaivgLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817161977 188 MVDASlRMSIVnlFRDLRDALNV--SIVYITH----DLATAYyisDRVVIM-RKGVVVESG 241
Cdd:PLN03140 1049 GLDAR-AAAIV--MRTVRNTVDTgrTVVCTIHqpsiDIFEAF---DELLLMkRGGQVIYSG 1103
|
|
| |
