|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-257 |
5.72e-119 |
|
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: 349.59 E-value: 5.72e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLH-LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN--AIREL 81
Cdd:COG1123 261 LEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARA 161
Cdd:COG1123 341 RRRVQMVFQDPYSSLNPRMTVGDIIAEPLR--LHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 162 LVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQH 241
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
250
....*....|....*.
gi 488473195 242 VVTQELLRAIPRIRVD 257
Cdd:COG1123 499 PYTRALLAAVPSLDPA 514
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-254 |
8.70e-119 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 342.48 E-value: 8.70e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLH-------LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN- 76
Cdd:COG4608 8 LEVRDLKKHfpvrgglFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 77 -AIRELRRSAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQR 155
Cdd:COG4608 88 rELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLR--IHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250
....*....|....*....
gi 488473195 236 YRDPQHVVTQELLRAIPRI 254
Cdd:COG4608 246 YARPLHPYTQALLSAVPVP 264
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-257 |
3.12e-116 |
|
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: 335.48 E-value: 3.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQP---DSGTVRFRGTSLTDAN--AIR 79
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 80 ELR-RSAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGL-DPES-ASRFPHEFSGGQRQRI 156
Cdd:COG0444 82 KIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLR--IHGGLSKAEARERAIELLERVGLpDPERrLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260
....*....|....*....|.
gi 488473195 237 RDPQHVVTQELLRAIPRIRVD 257
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPD 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-255 |
6.59e-111 |
|
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: 329.34 E-value: 6.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLH-------LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPDSGTVRFRGTSLT--DA 75
Cdd:COG4172 276 LEARDLKVWfpikrglFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDglSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 76 NAIRELRRSAAMVFQDPRSSLDPRMSIGRAITEPLRSpVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQR 155
Cdd:COG4172 355 RALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRV-HGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250 260
....*....|....*....|
gi 488473195 236 YRDPQHVVTQELLRAIPRIR 255
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-255 |
6.95e-110 |
|
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: 316.74 E-value: 6.95e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRS 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR-RRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLDPRMSIGRAITEPLRSpvarrTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILAEPLRI-----HGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVT 244
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
250
....*....|.
gi 488473195 245 QELLRAIPRIR 255
Cdd:COG1124 236 RELLAASLAFE 246
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-230 |
7.18e-107 |
|
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: 308.67 E-value: 7.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA-IRELRR 83
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SA-AMVFQDPRSSLDPRMSIGRAITEPLRSpVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARAL 162
Cdd:cd03257 82 KEiQMVFQDPMSSLNPRMTIGEQIAEPLRI-HGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-258 |
1.62e-92 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 275.69 E-value: 1.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLH------LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTD 74
Cdd:PRK11308 2 QQPLLQAIDLKKHypvkrgLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 75 AN--AIRELRRSAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQ 152
Cdd:PRK11308 82 ADpeAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLL--INTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 153 RQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKL 232
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260
....*....|....*....|....*.
gi 488473195 233 ADVYRDPQHVVTQELLRAIPRIRVDD 258
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDD 265
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-252 |
1.49e-91 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 273.51 E-value: 1.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGT---------NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA 75
Cdd:PRK15079 9 LEVADLKVHFDIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 76 NAI--RELRRSAAMVFQDPRSSLDPRMSIGRAITEPLRS--PvarRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGG 151
Cdd:PRK15079 89 KDDewRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyhP---KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 245
|
250 260
....*....|....*....|.
gi 488473195 232 LADVYRDPQHVVTQELLRAIP 252
Cdd:PRK15079 246 YDEVYHNPLHPYTKALMSAVP 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-257 |
1.37e-87 |
|
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: 269.63 E-value: 1.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKS-TLLKAMMALRQPD---SGTVRFRGTSLTDAN--AI 78
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSerEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELR-RSAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGL-DPES-ASRFPHEFSGGQRQR 155
Cdd:COG4172 87 RRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLR--LHRGLSGAAARARALELLERVGIpDPERrLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250 260
....*....|....*....|..
gi 488473195 236 YRDPQHVVTQELLRAIPRIRVD 257
Cdd:COG4172 245 FAAPQHPYTRKLLAAEPRGDPR 266
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-248 |
1.15e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 238.20 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSSGG-----TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA 75
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 76 NA------IRelrrsaaMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFS 149
Cdd:COG4167 81 DYkyrckhIR-------MIFQDPNTSLNPRLNIGQILEEPLR--LNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 150 GGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVER 229
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250
....*....|....*....
gi 488473195 230 GKLADVYRDPQHVVTQELL 248
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLI 250
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-255 |
3.17e-73 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 232.10 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD---SGTVRFRGTSLTDANa 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 78 IRELRRSAAMVFQDPRSSLDPrMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALE---NLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYR 237
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250
....*....|....*...
gi 488473195 238 DPQhvvtqeLLRAIPRIR 255
Cdd:COG1123 233 APQ------ALAAVPRLG 244
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-260 |
2.48e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 221.88 E-value: 2.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELR 82
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDprSSLDPRMSIGRAITEPLRspVARrTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG1135 82 RKIGMIFQH--FNLLSSRTVAENVALPLE--IAG-VPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHV 242
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250
....*....|....*...
gi 488473195 243 VTQELLRAIPRIRVDDST 260
Cdd:COG1135 236 LTRRFLPTVLNDELPEEL 253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-240 |
1.53e-67 |
|
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: 208.97 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN--AIRELR 82
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDpRSSLDPRMSIGRaITEPLRSPVARRTTRQQRKDRLAKVmvdVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:cd03258 82 RRIGMIFQH-FNLLSSRTVFEN-VALPLEIAGVPKAEIEERVLELLEL---VGLE-DKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-258 |
3.48e-66 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 208.81 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD---SGTVRFRGTSLTDANAiREL 81
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE-KEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RR----SAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKvMVDVGLDPESASR---FPHEFSGGQRQ 154
Cdd:PRK09473 92 NKlraeQISMIFQDPMTSLNPYMRVGEQLMEVLM--LHKGMSKAEAFEESVR-MLDAVKMPEARKRmkmYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260
....*....|....*....|....
gi 488473195 235 VYRDPQHVVTQELLRAIPRIRVDD 258
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEG 272
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-251 |
4.42e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.53 E-value: 4.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA-IRELRR 83
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPrsSLDPRMSIGRAITEPLRspVARRTTRQQRKDR----LAKVmvdvGLdPESASRFPHEFSGGQRQRIAIA 159
Cdd:COG1126 78 KVGMVFQQF--NLFPHLTVLENVTLAPI--KVKKMSKAEAEERamelLERV----GL-ADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 160 RALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|..
gi 488473195 240 QHVVTQELLRAI 251
Cdd:COG1126 228 QHERTRAFLSKV 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-240 |
1.13e-64 |
|
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: 201.41 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:COG1122 1 IELENLSF---SYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN-LRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLdprmsIGRAITEPLR-SPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:COG1122 77 VGLVFQNPDDQL-----FAPTVEEDVAfGPENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-252 |
9.17e-63 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 207.40 E-value: 9.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 22 NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRRSAAMVFQDPRSSLDPR 99
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlSPGKLQALRRDIQFIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK10261 418 QTVGDSIMEPLR--VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 180 VSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLRAIP 252
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-251 |
9.21e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 197.72 E-value: 9.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELR 82
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQ--DPRSSldprmsigRAITE----PLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRI 156
Cdd:PRK11153 82 RQIGMIFQhfNLLSS--------RTVFDnvalPLE---LAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|....*
gi 488473195 237 RDPQHVVTQELLRAI 251
Cdd:PRK11153 230 SHPKHPLTREFIQST 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-249 |
2.26e-61 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 201.47 E-value: 2.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPDSGTVRFRGTSLTDAN--AIRELRRSAAMVFQDPRSSLDPRM 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLNrrQLLPVRHRIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEPLRspVARRT-TRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK15134 380 NVLQIIEEGLR--VHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 180 VSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLR 249
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-228 |
3.50e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.18 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAI 78
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELRRSA-AMVFQDPRssLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:COG1136 81 ARLRRRHiGFVFQFFN--LLPELTALENVALPLL---LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVE 228
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-229 |
3.01e-60 |
|
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: 189.61 E-value: 3.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSltdanaIRELRRS 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP------VTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:cd03293 75 RGYVFQQDA--LLPWLTVLDNVALGLE---LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSV--GRIVER 229
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-251 |
1.26e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 189.90 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 11 HLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRRSAAMV 88
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 89 FQDPRSSLDPRMSIGRAITEPLRSPVARRTTRQQRkdRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDV 168
Cdd:PRK10419 95 FQDSISAVNPRKTVREIIREPLRHLLSLDKAERLA--RASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 169 LVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRdPQHVVTQELL 248
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT-FSSPAGRVLQ 251
|
...
gi 488473195 249 RAI 251
Cdd:PRK10419 252 NAV 254
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-228 |
3.64e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 188.37 E-value: 3.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQ---IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA 77
Cdd:COG1116 1 MSAAapaLELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 78 IRelrrsaAMVFQDPRssLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:COG1116 81 DR------GVVFQEPA--LLPWLTVLDNVALGLE---LRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLG-VVRhLCDTVAVMSV--GRIVE 228
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-256 |
1.48e-58 |
|
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: 186.93 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRRSAAMVFQDPRSSLDPRMS 101
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IGRAITEPLRSPVARRTTRQQRkdRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKA--RIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 182 VRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV--YRDPQHVVTQE-LLRAIPRIRV 256
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHPAGRNLQSaVLPEHPVRRS 262
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-230 |
2.36e-58 |
|
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: 184.65 E-value: 2.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelrRS 84
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDPEsASRFPHEFSGGQRQRIAIARALVT 164
Cdd:cd03259 74 IGMVFQDY--ALFPHLTVAENIAFGLK---LRGVPKAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-240 |
2.45e-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: 189.15 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKaMMA-LRQPDSGTVRFRGTSLTD--ANa 77
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-MIAgFETPDSGRILLDGRDVTGlpPE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 78 irelRRSAAMVFQDPrsSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:COG3842 76 ----KRNVGMVFQDY--ALFPHLTVAENVAFGLR---MRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD----LGvvrhLCDTVAVMSVGRIVERGKLA 233
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPE 221
|
....*..
gi 488473195 234 DVYRDPQ 240
Cdd:COG3842 222 EIYERPA 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-235 |
7.78e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.42 E-value: 7.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaiRELRRS 84
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP--AEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLDPRMSIGRAITEplrspVAR--RTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG1131 75 IGYVPQEP--ALYPDLTVRENLRF-----FARlyGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-251 |
9.69e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 181.79 E-value: 9.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN--AIRELR 82
Cdd:COG3638 3 LELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRssLDPRMS------IGRAITEPLRSPVARRTTRQQRkDRLAKVMVDVGLDPESASRfPHEFSGGQRQRI 156
Cdd:COG3638 80 RRIGMIFQQFN--LVPRLSvltnvlAGRLGRTSTWRSLLGLFPPEDR-ERALEALERVGLADKAYQR-ADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIvergkladVY 236
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VF 227
|
250
....*....|....*
gi 488473195 237 RDPQHVVTQELLRAI 251
Cdd:COG3638 228 DGPPAELTDAVLREI 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-226 |
1.28e-56 |
|
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: 180.38 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA---IREL 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRssLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARA 161
Cdd:cd03255 81 RRHIGFVFQSFN--LLPDLTALENVELPLL---LAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 162 LVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRI 226
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-225 |
1.39e-56 |
|
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: 179.97 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGSssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSA 85
Cdd:cd03225 1 ELKNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS-LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSSLdprmsIGRAITEPLR-SPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:cd03225 78 GLVFQNPDDQF-----FGPTVEEEVAfGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGR 225
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-257 |
5.62e-56 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 179.85 E-value: 5.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRS 84
Cdd:COG1120 2 LEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR-RELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLDprMS------IGRAitePLRSPVARRTtrqqRKDRLA--KVMVDVGLDpESASRFPHEFSGGQRQRI 156
Cdd:COG1120 77 IAYVPQEPPAPFG--LTvrelvaLGRY---PHLGLFGRPS----AEDREAveEALERTGLE-HLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGkladvy 236
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG------ 220
|
250 260
....*....|....*....|.
gi 488473195 237 rDPQHVVTQELLRAIPRIRVD 257
Cdd:COG1120 221 -PPEEVLTPELLEEVYGVEAR 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-240 |
8.33e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 182.27 E-value: 8.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTsltDANAIRELR-R 83
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNLPPReR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPrsSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:COG1118 76 RVGFVFQHY--ALFPHMTVAENIAFGLR---VRPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
8.72e-56 |
|
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: 179.02 E-value: 8.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN--AI 78
Cdd:COG1127 2 SEPMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELRRSAAMVFQDPR--SSldprMSIGRAITEPLRspvaRRT--TRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQ 154
Cdd:COG1127 78 YELRRRIGMLFQGGAlfDS----LTVFENVAFPLR----EHTdlSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALD-VSVRAqVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLA 233
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
..
gi 488473195 234 DV 235
Cdd:COG1127 228 EL 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-226 |
2.54e-55 |
|
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: 176.95 E-value: 2.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA-NAIRELRR 83
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDprSSLDPRMSIGRAITEPLRSpvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:cd03262 77 KVGMVFQQ--FNLFPHLTVLENITLAPIK--VKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-259 |
4.11e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 177.63 E-value: 4.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMAL----RQPDSGTVRFRGTSLTDANAi 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELRR----SAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLdPESASR---FPHEFSGG 151
Cdd:PRK11022 81 KERRNlvgaEVAMIFQDPMTSLNPCYTVGFQIMEAIK--VHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
250 260
....*....|....*....|....*...
gi 488473195 232 LADVYRDPQHVVTQELLRAIPRIRVDDS 259
Cdd:PRK11022 238 AHDIFRAPRHPYTQALLRALPEFAQDKA 265
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-252 |
6.11e-53 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 174.71 E-value: 6.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 10 LHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPDSGTV-----RFRGTSLTD--ANAIREL- 81
Cdd:COG4170 9 LTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKlsPRERRKIi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRSSLDPRMSIGRAITEPLRSPVARRT---TRQQRKDRLAKVMVDVGL-DPESASR-FPHEFSGGQRQRI 156
Cdd:COG4170 88 GREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIkDHKDIMNsYPHELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
250
....*....|....*.
gi 488473195 237 RDPQHVVTQELLRAIP 252
Cdd:COG4170 248 KSPHHPYTKALLRSMP 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-240 |
7.06e-53 |
|
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: 171.27 E-value: 7.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDanaIRELRRSAAMVFQDprSSLDP 98
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN---LPPHKRPVNTVFQN--YALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:cd03300 86 HLTVFENIAFGLR---LKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-251 |
8.29e-53 |
|
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: 171.60 E-value: 8.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN--AIRELR 82
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRssLDPRMS------IGRAITEPLRSPVARRTTRQQRKDRLAkVMVDVGLDpESASRFPHEFSGGQRQRI 156
Cdd:cd03256 78 RQIGMIFQQFN--LIERLSvlenvlSGRLGRRSTWRSLFGLFPKEEKQRALA-ALERVGLL-DKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADvy 236
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-- 231
|
250
....*....|....*
gi 488473195 237 rdpqhvVTQELLRAI 251
Cdd:cd03256 232 ------LTDEVLDEI 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-225 |
1.91e-52 |
|
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: 168.52 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAI-RELRR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPrsSLDPRMSIGRAITEPLrspvarrttrqqrkdrlakvmvdvgldpesasrfphefSGGQRQRIAIARALV 163
Cdd:cd03229 77 RIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGR 225
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-261 |
5.91e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.50 E-value: 5.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnaire 80
Cdd:COG1121 3 MMPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 lRRSAAMVFQdpRSSLDPRMSI--------GRAitepLRSPVARRTTRQQRkDRLAKVMVDVGLDpESASRFPHEFSGGQ 152
Cdd:COG1121 74 -RRRIGYVPQ--RAEVDWDFPItvrdvvlmGRY----GRRGLFRRPSRADR-EAVDEALERVGLE-DLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 153 RQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIvergkl 232
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV------ 217
|
250 260
....*....|....*....|....*....
gi 488473195 233 adVYRDPQHVVTQELLRAIPRIRVDDSTH 261
Cdd:COG1121 218 --AHGPPEEVLTPENLSRAYGGPVALLAH 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-253 |
1.63e-51 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 175.66 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 11 HLHLGSSSGGT--NALDGVSLHVNEGQRLGLVGGSGAGKS-TLLKAMMALRQPD----SGTVRFRGTSLTDANAiRELRR 83
Cdd:PRK15134 10 NLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASE-QTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 ----SAAMVFQDPRSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDpESASR---FPHEFSGGQRQRI 156
Cdd:PRK15134 89 vrgnKIAMIFQEPMVSLNPLHTLEKQLYEVLS--LHRGMRREAARGEILNCLDRVGIR-QAAKRltdYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250
....*....|....*..
gi 488473195 237 RDPQHVVTQELLRAIPR 253
Cdd:PRK15134 246 SAPTHPYTQKLLNSEPS 262
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-248 |
1.68e-51 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 168.81 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 22 NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN-AIRELRrsAAMVFQDPRSSLDPRM 100
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDySYRSQR--IRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDV 180
Cdd:PRK15112 105 RISQILDFPLR--LNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 181 SVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELL 248
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-226 |
3.28e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.14 E-value: 3.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIrELRRSAAMVFQDP 92
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP-EWRRQVAYVPQEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RssLdPRMSIGRAITEPLRspvarRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:COG4619 84 A--L-WGGTVRDNLPFPFQ-----LRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-251 |
1.22e-50 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 166.25 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 14 LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTS--LTDANAIRELRRSAAM---- 87
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqLRDLYALSEAERRRLLrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 88 --VFQDPRSSLDPRMSIGRAITEPLRSPVAR--RTTRQQRKDRLAKVMvdvgLDPESASRFPHEFSGGQRQRIAIARALV 163
Cdd:PRK11701 92 gfVHQHPRDGLRMQVSAGGNIGERLMAVGARhyGDIRATAGDWLERVE----IDAARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVV 243
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPY 247
|
....*...
gi 488473195 244 TQELLRAI 251
Cdd:PRK11701 248 TQLLVSSV 255
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-242 |
3.82e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 167.94 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKaMMA-LRQPDSGTVRFRGTsltDANAIREL 81
Cdd:COG3839 2 ASLELENVSK----SYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAgLEDPTSGEILIGGR---DVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPrsSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKV--MVDVG--LDpesasRFPHEFSGGQRQRIA 157
Cdd:COG3839 74 DRNIAMVFQSY--ALYPHMTVYENIAFPLK---LRKVPKAEIDRRVREAaeLLGLEdlLD-----RKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD------LGvvrhlcDTVAVMSVGRIVERGK 231
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGT 217
|
250
....*....|.
gi 488473195 232 LADVYRDPQHV 242
Cdd:COG3839 218 PEELYDRPANL 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-245 |
5.97e-50 |
|
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: 163.83 E-value: 5.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAI--RELR 82
Cdd:cd03261 1 IELRGLTKSFG----GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDprSSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIARAL 162
Cdd:cd03261 77 RRMGMLFQS--GALFDSLTVFENVAFPLR--EHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHV 242
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
...
gi 488473195 243 VTQ 245
Cdd:cd03261 232 VRQ 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-251 |
1.79e-49 |
|
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: 164.16 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRRSAAMVFQDPRSSL-- 96
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakKKKKLKDLRKKVGLVFQFPEHQLfe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 -----D----PR---MSIGRAiteplrspvarrttrqqrKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:TIGR04521 98 etvykDiafgPKnlgLSEEEA------------------EERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPqhvvt 244
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV----- 234
|
....*..
gi 488473195 245 qELLRAI 251
Cdd:TIGR04521 235 -DELEKI 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-239 |
8.03e-49 |
|
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: 161.31 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIrELRRSAAMVFQdpRSSLDP 98
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGYVIQ--QIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITeplRSPVARRTTRQQRKDRLAKVMVDVGLDPES-ASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:cd03295 89 HMTVEENIA---LVPKLLKWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-250 |
1.38e-48 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 161.02 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 25 DGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPdsGTVRFRGTSLTDANAI--RELR-RSAAMVFQDPRSSLDPRMS 101
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVapCALRgRKIATIMQNPRSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IGRAITEPLRSpvarrTTRQQRKDRLAKVMVDVGL-DPES-ASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK10418 98 MHTHARETCLA-----LGKPADDATLTAALEAVGLeNAARvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 180 VSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLRA 250
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-240 |
3.86e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 159.41 E-value: 3.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTV-----RFRGTSLTDANAIRELRRSAAMVFQdpR 93
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDFSKTPSDKAIRELRRNVGMVFQ--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 SSLDPRMSIGRAITE-PLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK11124 91 YNLWPHLTVQQNLIEaPCR---VLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKlADVYRDPQ 240
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-228 |
4.93e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 158.68 E-value: 4.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTD--ANAIRELR 82
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRssLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG2884 79 RRIGVVFQDFR--LLPDRTVYENVALPLR---VTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-226 |
1.03e-47 |
|
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: 156.02 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaiRELRRS 84
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLDPRMSIGRAIteplrspvarrttrqqrkdrlakvmvdvgldpesasrfphEFSGGQRQRIAIARALVT 164
Cdd:cd03230 75 IGYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-240 |
2.68e-47 |
|
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: 157.11 E-value: 2.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSggtnaLDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelrRS 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDprSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVM-VDVGLDpesasRFPHEFSGGQRQRIAIARALV 163
Cdd:cd03299 73 ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLgIDHLLN-----RKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
14-251 |
5.04e-47 |
|
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: 156.91 E-value: 5.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 14 LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG--------TSLTDANAIRELRRSA 85
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelelYQLSEAERRRLMRTEW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSSLDPRMSIGRAITEPLRSPVARR--TTRQQRKDRLAKVMVDVG-LDPEsasrfPHEFSGGQRQRIAIARAL 162
Cdd:TIGR02323 89 GFVHQNPRDGLRMRVSAGANIGERLMAIGARHygNIRATAQDWLEEVEIDPTrIDDL-----PRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHV 242
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHP 243
|
....*....
gi 488473195 243 VTQELLRAI 251
Cdd:TIGR02323 244 YTQLLVSSI 252
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-240 |
5.18e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 5.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVR-----FRGTSLTDANAIRELRRSAAMVFQdpR 93
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDFSQKPSEKAIRLLRQKVGMVFQ--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 SSLDPRMSIGRAITE-PLRspVARrTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:COG4161 91 YNLWPHLTVMENLIEaPCK--VLG-LSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKlADVYRDPQ 240
Cdd:COG4161 167 EPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-230 |
3.73e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 163.85 E-value: 3.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:COG2274 474 IELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID-PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPR---SSL-------DPRMSIgraiteplrspvarrttrqqrkDRLAKVMVDVGLDPEsASRFPH-------- 146
Cdd:COG2274 551 IGVVLQDVFlfsGTIrenitlgDPDATD----------------------EEIIEAARLAGLHDF-IEALPMgydtvvge 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 147 ---EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSV 223
Cdd:COG2274 608 ggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDK 684
|
....*..
gi 488473195 224 GRIVERG 230
Cdd:COG2274 685 GRIVEDG 691
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-230 |
3.99e-46 |
|
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: 153.60 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVN---EGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIREL---RRSAAMVFQDprSSLD 97
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEplrspVARRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:cd03297 88 PHLNVRENLAF-----GLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-230 |
6.38e-46 |
|
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: 151.82 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSA 85
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP-KELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQdprssldprmsigraiteplrspvarrttrqqrkdrlakVMVDVGLDPEsASRFPHEFSGGQRQRIAIARALVTE 165
Cdd:cd03214 76 AYVPQ---------------------------------------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
5-239 |
7.92e-46 |
|
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: 156.80 E-value: 7.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVeDLHLHLGSSsggtnALDgVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIREL--- 81
Cdd:COG4148 3 LEV-DFRLRRGGF-----TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRssLDPRMSIGRAITEplrspVARRTTRQQRKDRLAKV--MVDVG--LDpesasRFPHEFSGGQRQRIA 157
Cdd:COG4148 76 RRRIGYVFQEAR--LFPHLSVRGNLLY-----GRKRAPRAERRISFDEVveLLGIGhlLD-----RRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYR 237
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
..
gi 488473195 238 DP 239
Cdd:COG4148 224 RP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-240 |
1.23e-45 |
|
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: 152.88 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSggtnALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRElrRS 84
Cdd:cd03296 3 IEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQdpRSSLDPRMSIGRAITEPLR-SPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:cd03296 76 VGFVFQ--HYALFRHMTVFDNVAFGLRvKPRSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-234 |
1.82e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.22 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelrRSAAMVFQDprSSLDPRMSIGRAIT 107
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSMLFQE--NNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 108 EPLRSpvARRTTRQQRKdRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVL 187
Cdd:COG3840 94 LGLRP--GLKLTAEQRA-QVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488473195 188 NLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-254 |
2.45e-45 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.79 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 7 VEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN---------A 77
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 78 IRELRR----SAAMVFQDPRSSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDPESA---SRFPHEFSG 150
Cdd:PRK10261 95 AAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIR---LHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 151 GQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....
gi 488473195 231 KLADVYRDPQHVVTQELLRAIPRI 254
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQL 275
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-231 |
3.48e-45 |
|
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: 151.56 E-value: 3.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALR-----QPDSGTVRFRGTSLTDANAIR 79
Cdd:cd03260 1 IELRDLNV----YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 80 -ELRRSAAMVFQDPrsslDP-RMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASR-FPHEFSGGQRQRI 156
Cdd:cd03260 77 lELRRRVGMVFQKP----NPfPGSIYDNVAYGLR--LHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-238 |
3.68e-45 |
|
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: 151.68 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLGsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA--IREL 81
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkkLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQD----PRSSLDPRMSIGRAITEPLRSPVARRTTRQQRkdRLAKVMVD-VGLDPESASRfPHEFSGGQRQRI 156
Cdd:TIGR02315 78 RRRIGMIFQHynliERLTVLENVLHGRLGYKPTWRSLLGRFSEEDK--ERALSALErVGLADKAYQR-ADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
..
gi 488473195 237 RD 238
Cdd:TIGR02315 235 DE 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-240 |
6.25e-45 |
|
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: 151.73 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRE 80
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDPRssLDPRMSI-------------GRAITEPLRSPVARRTTRQQRkDRLAKVMVDVGLDPEsASRFPHE 147
Cdd:COG0411 77 ARLGIARTFQNPR--LFPELTVlenvlvaaharlgRGLLAALLRLPRARREEREAR-ERAEELLERVGLADR-ADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 148 FSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|...
gi 488473195 228 ERGKLADVYRDPQ 240
Cdd:COG0411 233 AEGTPAEVRADPR 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-242 |
6.27e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.01 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA-IRELRRSAAMVFQdpRSSLD 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdERLIRQEAGMVFQ--QFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSigrAITEPLRSPVARRTTRQQRKDRLAKVMVD-VGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:PRK09493 90 PHLT---ALENVMFGPLRVRGASKEEAEKQARELLAkVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 177 ALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP---------QHV 242
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPpsqrlqeflQHV 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-256 |
1.82e-44 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 150.87 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRR-SAAMVFQDpr 93
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRkKISMVFQS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 SSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:cd03294 111 FALLPHRTVLENVAFGLE---VQGVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLRAIPR 253
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
...
gi 488473195 254 IRV 256
Cdd:cd03294 267 AKV 269
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-225 |
2.69e-44 |
|
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: 147.14 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPR--SsldprMSIGRAIteplrspvarrttrqqrkdrlakvmvdvgldpesasrfpheFSGGQRQRIAIARAL 162
Cdd:cd03228 78 IAYVPQDPFlfS-----GTIRENI-----------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGR 225
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-240 |
4.85e-44 |
|
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: 148.74 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRS 84
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssLDPRMSI-------GRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGLDPEsASRFPHEFSGGQRQRIA 157
Cdd:cd03219 77 IGRTFQIPR--LFPELTVlenvmvaAQARTGSGLLLARARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYR 237
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 488473195 238 DPQ 240
Cdd:cd03219 233 NPR 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-228 |
5.03e-44 |
|
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: 148.74 E-value: 5.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT----DANAiRE 80
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARA-RL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDprSSLDPRMSIGRAITEPLrsPVARRTTRQQRkdrlAKVMVD-VGLDpESASRFPHEFSGGQRQRIAIA 159
Cdd:COG4181 88 RARHVGFVFQS--FQLLPTLTALENVMLPL--ELAGRRDARAR----ARALLErVGLG-HRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 160 RALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVE 228
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-174 |
7.61e-44 |
|
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: 145.48 E-value: 7.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPRssLDPRMSIG 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQDPQ--LFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 104 RAITEPLRSpvaRRTTRQQRKDRLAKVMVDVGLDP---ESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:pfam00005 78 ENLRLGLLL---KGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-235 |
1.72e-43 |
|
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: 147.70 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSsggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaiRELRRS 84
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLDPRMSIgraiTEPLRS-PVARRTTRQQRKDRLAKVMVDVGLDPESASRFpHEFSGGQRQRIAIARALV 163
Cdd:COG4555 76 IGVLPDER--GLYDRLTV----RENIRYfAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-230 |
2.25e-43 |
|
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: 146.25 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAireLRRSAAMVFQDprSSLDP 98
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMVFQN--YALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMvdvGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVPKDEIDERVREVAELL---QIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-238 |
1.14e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.73 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDL-HLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA-IRELR 82
Cdd:PRK13637 3 IKIENLtHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRSSLDPRmSIGRAITeplRSPVARRTTRQQRKDRLAKVMVDVGLDPES-ASRFPHEFSGGQRQRIAIARA 161
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEE-TIEKDIA---FGPINLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 162 LVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-249 |
3.20e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.51 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFrGTSLTDA--------NAIRELRRSAAMVFQD 91
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTarslsqqkGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 92 prSSLDPRMSIGRAITE-PLrspVARRTTRQQRKDRLAKVMVDVGLDPESASrFPHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:PRK11264 94 --FNLFPHRTVLENIIEgPV---IVKGEPKEEATARARELLAKVGLAGKETS-YPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLVRERgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLR 249
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-225 |
3.56e-42 |
|
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: 141.23 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDaNAIRELRRSA 85
Cdd:cd00267 1 EIENLSF----RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK-LPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQdprssldprmsigraiteplrspvarrttrqqrkdrlakvmvdvgldpesasrfpheFSGGQRQRIAIARALVTE 165
Cdd:cd00267 76 GYVPQ---------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGR 225
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-238 |
4.36e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 4.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPrsSLDP 98
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQEL--NLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSI------GRaitEPLRSP-VARRTTRQQRKDRLAKvmVDVGLDPESASRfphEFSGGQRQRIAIARALVTEPDVLVA 171
Cdd:COG1129 93 NLSVaeniflGR---EPRRGGlIDWRAMRRRARELLAR--LGLDIDPDTPVG---DLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 172 DEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-239 |
6.44e-42 |
|
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: 145.71 E-value: 6.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 39 LVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAireLRRSAAMVFQDprSSLDPRMSIGRAITEPLRspvARRT 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP---HLRHINMVFQS--YALFPHMTVEENVAFGLK---MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 119 TRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERG 198
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488473195 199 LTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-240 |
2.50e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 142.25 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHlhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSL--------- 72
Cdd:COG4598 6 PPALEVRDLH----KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 73 ---TDANAIRELRRSAAMVFQDprSSLDPRMSIGRAITE-PLRspVARRTtRQQRKDRLAKVMVDVGLdPESASRFPHEF 148
Cdd:COG4598 82 lvpADRRQLQRIRTRLGMVFQS--FNLWSHMTVLENVIEaPVH--VLGRP-KAEAIERAEALLAKVGL-ADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
250
....*....|..
gi 488473195 229 RGKLADVYRDPQ 240
Cdd:COG4598 235 QGPPAEVFGNPK 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-235 |
6.36e-41 |
|
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: 140.26 E-value: 6.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSsggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRS 84
Cdd:cd03224 1 LEVENLNAGYGKS----QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssLDPRMSigraITEPLRSpVARRTTRQQRKDRLAKVMvdvgldpesaSRFP--HEF--------SGGQRQ 154
Cdd:cd03224 77 IGYVPEGRR--IFPELT----VEENLLL-GAYARRRAKRKARLERVY----------ELFPrlKERrkqlagtlSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
.
gi 488473195 235 V 235
Cdd:cd03224 219 L 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-249 |
6.63e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 6.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLGSSSggtnALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT---------- 73
Cdd:PRK10619 5 KLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 74 --DANAIRELRRSAAMVFQdpRSSLDPRMSIGRAITEplrSPV-ARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSG 150
Cdd:PRK10619 81 vaDKNQLRLLRTRLTMVFQ--HFNLWSHMTVLENVME---APIqVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 151 GQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
250
....*....|....*....
gi 488473195 231 KLADVYRDPQHVVTQELLR 249
Cdd:PRK10619 235 APEQLFGNPQSPRLQQFLK 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-237 |
7.10e-41 |
|
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: 147.60 E-value: 7.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRR 83
Cdd:COG4988 336 SIELEDVSF---SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-ASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPRssLdPRMSIGRAITepLRSPVArrtTRQQRKDRLAKVMVDV-------GLDP---ESASRFphefSGGQR 153
Cdd:COG4988 412 QIAWVPQNPY--L-FAGTIRENLR--LGRPDA---SDEELEAALEAAGLDEfvaalpdGLDTplgEGGRGL----SGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 154 QRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLA 233
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHE 556
|
....
gi 488473195 234 DVYR 237
Cdd:COG4988 557 ELLA 560
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-230 |
1.39e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:COG1132 340 IEFENVSF---SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDP-------RSSLdprmSIGRA-ITEplrspvarrttrqqrkDRLAKVMVDVGLDpESASRFPH---------- 146
Cdd:COG1132 416 IGVVPQDTflfsgtiRENI----RYGRPdATD----------------EEVEEAAKAAQAH-EFIEALPDgydtvvgerg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 147 -EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGR 225
Cdd:COG1132 475 vNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGR 551
|
....*
gi 488473195 226 IVERG 230
Cdd:COG1132 552 IVEQG 556
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-240 |
1.51e-40 |
|
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: 139.73 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGSSsggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSA 85
Cdd:COG0410 5 EVENLHAGYGGI----HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRssLDPRMSigraITEPLRSPVARRTTRQQRKDRLAKVMvdvgldpesaSRFP--HEF--------SGGQRQR 155
Cdd:COG0410 81 GYVPEGRR--IFPSLT----VEENLLLGAYARRDRAEVRADLERVY----------ELFPrlKERrrqragtlSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
....*
gi 488473195 236 YRDPQ 240
Cdd:COG0410 224 LADPE 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-227 |
3.12e-40 |
|
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: 136.40 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQdprssldp 98
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 rmsigraiteplrspvarrttrqqrkdrlakvmvdvgldpesasrfpheFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488473195 179 DVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:cd03216 114 TPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-252 |
3.42e-40 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 141.48 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD----SGTVRFRGTSLTDANAiRE 80
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSP-RE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRR----SAAMVFQDPRSSLDPRMSIGRAITEPLRSPVARRTTRQQ---RKDRLAKVMVDVGL-DPESASR-FPHEFSGG 151
Cdd:PRK15093 83 RRKlvghNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRfgwRKRRAIELLHRVGIkDHKDAMRsFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260
....*....|....*....|.
gi 488473195 232 LADVYRDPQHVVTQELLRAIP 252
Cdd:PRK15093 243 SKELVTTPHHPYTQALIRAIP 263
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-221 |
5.23e-40 |
|
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: 137.66 E-value: 5.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnairelRRSA 85
Cdd:cd03235 1 EVEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQdpRSSLDPRMSI--------GRaitepLRSPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:cd03235 71 GYVPQ--RRSIDRDFPIsvrdvvlmGL-----YGHKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVM 221
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-254 |
1.02e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.67 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT-DANAIRELRR 83
Cdd:PRK13639 2 LETRDLKY---SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPRSSL-DPRMSIGRAITePLRSPVARRTTRQQRKDRLAKVmvdvGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:PRK13639 79 TVGIVFQNPDDQLfAPTVEEDVAFG-PLNLGLSKEEVEKRVKEALKAV----GME-GFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQhV 242
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE-T 230
|
250
....*....|..
gi 488473195 243 VTQELLRaIPRI 254
Cdd:PRK13639 231 IRKANLR-LPRV 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-254 |
1.48e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 138.44 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLgssSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT-DANAIRELRR 83
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDP-----RSSLDPRMSIGraiteplrsPVARRTTRQQRKDRLAKVMVDVGLDPESaSRFPHEFSGGQRQRIAI 158
Cdd:PRK13636 83 SVGMVFQDPdnqlfSASVYQDVSFG---------AVNLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 159 ARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
250 260
....*....|....*....|
gi 488473195 239 pqhvvtQELLRAI----PRI 254
Cdd:PRK13636 233 ------KEMLRKVnlrlPRI 246
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-239 |
6.07e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 6.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAireLRRSAAMVFQDprSSL 96
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHVNTVFQS--YAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:PRK09452 98 FPHMTVFENVAFGLR---MQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 177 ALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-207 |
2.17e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.38 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD---SGTVRFRGTSLTDANAireLR 82
Cdd:COG4136 3 SLENLTITLG----GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA---EQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRssLDPRMSIGraitEPLRSPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG4136 76 RRIGILFQDDL--LFPHLSVG----ENLAFALPPTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD 207
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-230 |
4.09e-38 |
|
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: 132.88 E-value: 4.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEdlhlHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT-DAnaiRELRR 83
Cdd:cd03265 1 IEVE----NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEP---REVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDPrsSLDPRMS-------IGRAITEPlrspvarrttRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRI 156
Cdd:cd03265 74 RIGIVFQDL--SVDDELTgwenlyiHARLYGVP----------GAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-230 |
7.74e-38 |
|
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: 131.96 E-value: 7.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIreLRRSAAMVfqdP 92
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI---E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RSSLDPRMSiGRaitEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:cd03268 80 APGFYPNLT-AR---ENLR---LLARLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-228 |
1.04e-37 |
|
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: 132.09 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELR-RSAAMVFQdpRSSLD 97
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSklSSNERAKLRnKKLGFIYQ--FHHLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEPLrspVARRTTRQQRKDRLAKVMVDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:TIGR02211 96 PDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLcDTVAVMSVGRIVE 228
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-239 |
1.27e-37 |
|
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: 135.24 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDgVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIREL---RRSAAMVFQDPRssL 96
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEAR--L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEPLRspvarRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:TIGR02142 87 FPHLSVRGNLRYGMK-----RARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 177 ALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-261 |
1.48e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.59 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELR 82
Cdd:PRK13548 1 AMLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQdpRSSLD-P-------RMsiGRAiteplrspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQ 154
Cdd:PRK13548 76 RRRAVLPQ--HSSLSfPftveevvAM--GRA---------PHGLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALV------TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
250 260 270
....*....|....*....|....*....|...
gi 488473195 229 RGKladvyrdPQHVVTQELLRAIPRIRVDDSTH 261
Cdd:PRK13548 222 DGT-------PAEVLTPETLRRVYGADVLVQPH 247
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-239 |
2.30e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 134.44 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEdlhlHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRElrRS 84
Cdd:PRK10851 3 IEIA----NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA-RD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQdpRSSLDPRMSIGRAITEPLRS-PVARRTTRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIARALV 163
Cdd:PRK10851 76 VGFVFQ--HYALFRHMTVFDNIAFGLTVlPRRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
2.60e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.42 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHLHLGSSSggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIREL 81
Cdd:PRK13632 5 SVMIKVENVSFSYPNSE--NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRSSLdprmsIGRAITEPlrspVA-----RRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRI 156
Cdd:PRK13632 82 RKKIGIIFQNPDNQF-----IGATVEDD----IAfglenKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRhLCDTVAVMSVGRIVERGKLADVY 236
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
....
gi 488473195 237 RDPQ 240
Cdd:PRK13632 231 NNKE 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-234 |
3.33e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.86 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTsltDANAIRELRRSAAMVFQDPR--SSLDPRMSIGRA 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRRPVSMLFQENNlfSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 106 ITEPLRSPVARRTTRQQRKDRlakvmvdVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQ 185
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQ-------MGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488473195 186 VLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-254 |
3.57e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 132.23 E-value: 3.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:PRK13652 4 IETRDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSL-DPRMSIGRAIteplrSPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:PRK13652 80 VGLVFQNPDDQIfSPTVEQDIAF-----GPINLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVV 243
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
250
....*....|..
gi 488473195 244 TQEL-LRAIPRI 254
Cdd:PRK13652 234 RVHLdLPSLPKL 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-225 |
7.29e-37 |
|
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: 129.86 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLH----LHLgssSGGT--NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFR----GT 70
Cdd:COG4778 1 MTTLLEVENLSktftLHL---QGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 71 SLTDANA--IRELRRSA-AMVFQDPRSSldPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDPESASRFPHE 147
Cdd:COG4778 78 DLAQASPreILALRRRTiGYVSQFLRVI--PRVSALDVVAEPLL---ERGVDREEARARARELLARLNLPERLWDLPPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 148 FSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGR 225
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-240 |
1.10e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.30 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT---DANAIRELRRSAAMVFQDPRSSLDPR 99
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKPLRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 mSIGRAIT-EPLRSPVArrttrQQRKDRLAKVMVD-VGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13634 102 -TVEKDICfGPMNFGVS-----EEDAKQKAREMIElVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-261 |
1.18e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.24 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRS 84
Cdd:COG4559 2 LEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP-WELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDprSSLD-P-------RMsiGRAiteplrspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRI 156
Cdd:COG4559 77 RAVLPQH--SSLAfPftveevvAL--GRA---------PHGSSAAQDRQIVREALALVGLA-HLAGRSYQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARAL--VTEPD-----VLVADEPVSALDVSVRAQVLNLLNDLVReRGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVER 229
Cdd:COG4559 143 QLARVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
250 260 270
....*....|....*....|....*....|..
gi 488473195 230 GKladvyrdPQHVVTQELLRAIPRIRVDDSTH 261
Cdd:COG4559 222 GT-------PEEVLTDELLERVYGADLRVLAH 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-242 |
2.09e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 130.28 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG---TSLTDANAIRELRRSAAMVFQDPRSSL--D 97
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVFQFPESQLfeD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 prmSIGRAItepLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13646 102 ---TVEREI---IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHV 242
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-241 |
2.51e-36 |
|
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: 135.28 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELR 82
Cdd:COG4987 332 PSLELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDP-------RSSLdprmSIGR-AITEplrspvarrttrqqrkDRLAKVMVDVGLDP--------------ES 140
Cdd:COG4987 409 RRIAVVPQRPhlfdttlRENL----RLARpDATD----------------EELWAALERVGLGDwlaalpdgldtwlgEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 141 ASRFphefSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLgVVRHLCDTVAV 220
Cdd:COG4987 469 GRRL----SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRL-AGLERMDRILV 541
|
250 260
....*....|....*....|.
gi 488473195 221 MSVGRIVERGKLADVYRDPQH 241
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQNGR 562
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-229 |
3.30e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.21 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelr 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 rsaAMVFQDprSSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG4525 79 ---GVVFQK--DALLPWLNVLDNVAFGLR---LRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSV--GRIVER 229
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-246 |
3.57e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.00 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAM--MALRQPD---SGTVRFRGTSLTDA 75
Cdd:COG1117 8 LEPKIEVRNLNVYYG----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 76 NA-IRELRRSAAMVFQDPRssldP-RMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPE-------SASrfph 146
Cdd:COG1117 84 DVdVVELRRRVGMVFQKPN----PfPKSIYDNVAYGLR--LHGIKSKSELDEIVEESLRKAALWDEvkdrlkkSAL---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 147 EFSGGQRQRIAIARALVTEPDVLVADEPVSALD-VSVrAQVLNLLNDLvRERgLTMIFVSHDLGVVRHLCDTVAVMSVGR 225
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILEL-KKD-YTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
250 260
....*....|....*....|.
gi 488473195 226 IVERGKLADVYRDPQHVVTQE 246
Cdd:COG1117 231 LVEFGPTEQIFTNPKDKRTED 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-256 |
4.61e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIR-----ELRrsaamvfqdpr 93
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpEER----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 sSLDPRMSIGRAITEplrspVARRT--TRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIARALVTEPDVLVA 171
Cdd:COG4152 81 -GLYPKMKVGEQLVY-----LARLKglSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 172 DEPVSALD-VSVraqvlNLLNDLVRE---RGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV---YRDPQHVVT 244
Cdd:COG4152 154 DEPFSGLDpVNV-----ELLKDVIRElaaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrrqFGRNTLRLE 228
|
250
....*....|....*.
gi 488473195 245 ----QELLRAIPRIRV 256
Cdd:COG4152 229 adgdAGWLRALPGVTV 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-232 |
5.90e-36 |
|
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: 127.14 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTD--ANAIRELRRSAAMVFQDPRssL 96
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrGRAIPYLRRKIGVVFQDFR--L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEPLRspVARRTTRQQRKdRLAKVMVDVGLDPESASrFPHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:cd03292 90 LPDRNVYENVAFALE--VTGVPPREIRK-RVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 177 ALDVSVRAQVLNLLNDlVRERGLTMIFVSHDlgvvrhlCDTVAVMSVGRIV-ERGKL 232
Cdd:cd03292 166 NLDPDTTWEIMNLLKK-INKAGTTVVVATHA-------KELVDTTRHRVIAlERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-230 |
6.29e-36 |
|
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: 127.22 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTsltDANAIRELRRSAAMVFQDPR--SSLDPRMSIGRA 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRPVSMLFQENNlfAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 106 iteplRSPVARRTTRQQRkdRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQ 185
Cdd:cd03298 95 -----LSPGLKLTAEDRQ--AIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488473195 186 VLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-237 |
8.32e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 8.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPRSSLdprmsI 102
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-VWDVRRQVGMVFQNPDNQF-----V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAIteplRSPVA-----RRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13635 96 GATV----QDDVAfglenIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYR 237
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-239 |
3.95e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.68 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNA-LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDaNAIRElrRSAAMVFQDprSSLDP 98
Cdd:PRK11432 17 GSNTvIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQ--RDICMVFQS--YALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITEPLRSPVARRTTRQQR-KDRLAkvMVDVGldpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEERKQRvKEALE--LVDLA---GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-240 |
1.05e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.10 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG---TSLTDANAIRELRRSAAMVFQDPRSSLD 97
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNLKKLRKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEPLRSPVarrtTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGF----SEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 178 LDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-250 |
1.17e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRS 84
Cdd:PRK09536 4 IDVSDLSV----EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-RAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLDPRmsiGRAITEPLRSPVARRTTRQQRKDRLAkvmVDVGLDPESASRFPH----EFSGGQRQRIAIAR 160
Cdd:PRK09536 79 VASVPQDTSLSFEFD---VRQVVEMGRTPHRSRFDTWTETDRAA---VERAMERTGVAQFADrpvtSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 161 ALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKladvyrdPQ 240
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP-------PA 224
|
250
....*....|
gi 488473195 241 HVVTQELLRA 250
Cdd:PRK09536 225 DVLTADTLRA 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-248 |
1.50e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.97 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDL-HLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRF------------RGT 70
Cdd:PRK13651 2 QIKVKNIvKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 71 SLTDANAI-----------RELRRSAAMVFQDPRSSLDpRMSIGRAItepLRSPVARRTTRQQRKDRLAKVMVDVGLDPE 139
Cdd:PRK13651 82 KVLEKLVIqktrfkkikkiKEIRRRVGVVFQFAEYQLF-EQTIEKDI---IFGPVSMGVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 140 SASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVA 219
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTI 236
|
250 260
....*....|....*....|....*....
gi 488473195 220 VMSVGRIVERGKLADVYRDPQHVVTQELL 248
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSDNKFLIENNME 265
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
2.75e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLgssSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRE 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN-EKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDPrsslDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIAR 160
Cdd:PRK13647 77 VRSKVGLVFQDP----DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 161 ALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-238 |
3.72e-34 |
|
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: 128.77 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGS-SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFR-GTSLTDANAIRELR 82
Cdd:TIGR03269 280 IKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAA-----MVFQDprSSLDPRMSIGRAITEP----LRSPVARRttrqqrkdRLAKVMVDVGLDPESA----SRFPHEFS 149
Cdd:TIGR03269 360 RGRAkryigILHQE--YDLYPHRTVLDNLTEAigleLPDELARM--------KAVITLKMVGFDEEKAeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 150 GGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVER 229
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*....
gi 488473195 230 GKLADVYRD 238
Cdd:TIGR03269 510 GDPEEIVEE 518
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-230 |
5.20e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.92 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQrLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaiRELRRS 84
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssLDPRMSIgraiTEPLR-SPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALV 163
Cdd:cd03264 74 IGYLPQEFG--VYPNFTV----REFLDyIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-207 |
5.86e-34 |
|
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: 121.82 E-value: 5.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLhlhlGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAirELR 82
Cdd:COG4133 1 MMLEAENL----SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE--DYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRssLDPRMSigraITEPLRSpVARRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG4133 75 RRLAYLGHADG--LKPELT----VRENLRF-WAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHD 207
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-238 |
6.15e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.66 E-value: 6.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRSSldprmsI 102
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQ------I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAITE------PLRSPVARRTTRQQRKDRLAKV-MVdvgldpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK13633 99 VATIVEedvafgPENLGIPPEEIRERVDESLKKVgMY------EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 176 SALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-238 |
6.27e-34 |
|
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: 122.25 E-value: 6.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSA 85
Cdd:TIGR03410 2 EVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDprssldpRMSIGR-AITEPLRSPVARRTTRQQRkdrlakvmvdvgLDPESASRFP--HEF--------SGGQRQ 154
Cdd:TIGR03410 78 AYVPQG-------REIFPRlTVEENLLTGLAALPRRSRK------------IPDEIYELFPvlKEMlgrrggdlSGGQQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:TIGR03410 139 QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
....
gi 488473195 235 VYRD 238
Cdd:TIGR03410 219 LDED 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-239 |
2.74e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.18 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDanaIRELRRSAAMVFQDp 92
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH---VPPYQRPINMMFQS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 rSSLDPRMSIGRAITEPLRSPvarRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK11607 100 -YALFPHMTVEQNIAFGLKQD---KLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-237 |
3.81e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.57 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHL--HLGSSSGGT----------------NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDS 62
Cdd:COG1134 1 MSSMIEVENVSKsyRLYHEPSRSlkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 63 GTVRFRG--TSLTDANAI-------RELRRSAAMVFQDPRSSLDPRMS-------IGRAITEPLRSpvarrttrqqrkdr 126
Cdd:COG1134 81 GRVEVNGrvSALLELGAGfhpeltgRENIYLNGRLLGLSRKEIDEKFDeivefaeLGDFIDQPVKT-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 127 lakvmvdvgldpesasrfpheFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSH 206
Cdd:COG1134 147 ---------------------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSH 204
|
250 260 270
....*....|....*....|....*....|.
gi 488473195 207 DLGVVRHLCDTVAVMSVGRIVERGKLADVYR 237
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-238 |
9.30e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 9.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANA---IRELRRSAAMVFQDPRSSLDPR 99
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAITEPLRSPVARRTTRQQRKDRLAKVmvdvGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALV----GISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 180 VSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PRK13649 178 PKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-253 |
1.37e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.61 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 16 SSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG---TSLTDANAIRELRRSAAMVFQDP 92
Cdd:PRK13643 14 NSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVmvdvGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK13643 94 ESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV----GLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 173 EPVSALDVSVRAQVLNLLNDlVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELlrAIP 252
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL--GVP 246
|
.
gi 488473195 253 R 253
Cdd:PRK13643 247 K 247
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-240 |
2.49e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.47 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPRSSLdprmsI 102
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FEKLRKHIGIVFQNPDNQF-----V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAIteplRSPVA-----RRTTRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13648 98 GSIV----KYDVAfglenHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-227 |
2.69e-32 |
|
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: 117.36 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtdanAIRELRRSA 85
Cdd:cd03226 1 RIENISF---SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSSLDpRMSIGRAITEPLRSPVArrttrqqRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTE 165
Cdd:cd03226 74 GYVMQDVDYQLF-TDSVREELLLGLKELDA-------GNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-235 |
6.20e-32 |
|
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: 117.49 E-value: 6.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSG-TVRFRGTSLTDANaIRELRR-----SAAMVFQDP 92
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED-VWELRKriglvSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RSS--LDprM-------SIGRAiteplrspvaRRTTRQQRkDRLAKVMVDVGLDPESASRFpHEFSGGQRQRIAIARALV 163
Cdd:COG1119 93 RDEtvLD--VvlsgffdSIGLY----------REPTDEQR-ERARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDL----GVVRHlcdtVAVMSVGRIVERGKLADV 235
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeeipPGITH----VLLLKDGRVVAAGPKEEV 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-226 |
1.31e-31 |
|
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: 114.84 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHlgsssggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSA 85
Cdd:cd03215 6 EVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSS-LDPRMSIGRAITeplrspvarrttrqqrkdrlakvmvdvgldpesasrFPHEFSGGQRQRIAIARALVT 164
Cdd:cd03215 78 AYVPEDRKREgLVLDLSVAENIA------------------------------------LSSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-239 |
2.43e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.01 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRSSLdpr 99
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 msIGRAITEPLR-SPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:PRK13644 91 --VGRTVEEDLAfGPENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 179 DVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVrHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK13644 168 DPDSGIAVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-231 |
2.51e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 115.34 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTdanAIRELRRSAAMVFQDprSSLDPRMSIGRAIT 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT---GLAPYQRPVSMLFQE--NNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 108 EPLRsPVARRTTRQQRKdrLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVL 187
Cdd:TIGR01277 93 LGLH-PGLKLNAEQQEK--VVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488473195 188 NLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-256 |
2.85e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.27 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVfqdP 92
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLALL---P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDR--LAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNarVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKladvyrdPQHVVTQELLRA 250
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-------PEEVMTPGLLRT 233
|
....*.
gi 488473195 251 IPRIRV 256
Cdd:PRK11231 234 VFDVEA 239
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
24-230 |
3.08e-31 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 121.59 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQD-------PRSSL 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVLANSVAMVDQDiflfegtVRDNL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 ---DPRMSIGR--------AITEPLRSpvarrttrqqRKDRLAKVMVDVGLDpesasrfpheFSGGQRQRIAIARALVTE 165
Cdd:TIGR03796 574 tlwDPTIPDADlvrackdaAIHDVITS----------RPGGYDAELAEGGAN----------LSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLnllnDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIID----DNLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-227 |
3.27e-31 |
|
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: 114.91 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSL-TDANAIrelRRSAAMVFQDprSS 95
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAA---RQSLGYCPQF--DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 96 LDPRMSigraITEPLR--SPVaRRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:cd03263 86 LFDELT----VREHLRfyARL-KGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-231 |
8.41e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 114.56 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPrssldprMSIG 103
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQIGLVSQEP-------VLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLRSPVARRTTRQQrkdrlakvmvdvgldpESASRFP--HEF-------------------SGGQRQRIAIARAL 162
Cdd:cd03249 91 GTIAENIRYGKPDATDEEV----------------EEAAKKAniHDFimslpdgydtlvgergsqlSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGK 231
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-240 |
1.09e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 117.05 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDanaIRELRRSAAMVFQD----PRSSLDPRMSI 102
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND---VPPAERGVGMVFQSyalyPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GraitepLRSPVARRTTRQQRKDRLAKVM-VDVGLDpesasRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:PRK11000 99 G------LKLAGAKKEEINQRVNQVAEVLqLAHLLD-----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 182 VRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-222 |
2.00e-30 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL 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 C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 113.25 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLH----LHLgssSGGTN--ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFR----GTSLTD 74
Cdd:TIGR02324 2 LEVEDLSktftLHQ---QGGVRlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRhegaWVDLAQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 75 ANA--IRELRR-SAAMVFQDPRssLDPRMSIGRAITEPLRS-PVARRTTRQQRKDRLAKVMVDVGLDPESasrfPHEFSG 150
Cdd:TIGR02324 79 ASPreVLEVRRkTIGYVSQFLR--VIPRVSALEVVAEPLLErGVPREAARARARELLARLNIPERLWHLP----PATFSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 151 GQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMS 222
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRVMDVT 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-235 |
2.44e-30 |
|
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: 112.94 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelrrsaAMVFQDprSSLDPRMSIG 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR------MVVFQN--YSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLRSPVARRTTRQQRKdrlakvMVD-----VGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRA------IVEehialVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-246 |
2.95e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQ--PDSgtvRFRGTSLTDANAI-- 78
Cdd:PRK14247 2 NKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEA---RVSGEVYLDGQDIfk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 ---RELRRSAAMVFQDPRSSldPRMSI--GRAITEPLRSPVARRTTRQQR-KDRLAKVM----VDVGLDPESASrfpheF 148
Cdd:PRK14247 75 mdvIELRRRVQMVFQIPNPI--PNLSIfeNVALGLKLNRLVKSKKELQERvRWALEKAQlwdeVKDRLDAPAGK-----L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|....*...
gi 488473195 229 RGKLADVYRDPQHVVTQE 246
Cdd:PRK14247 226 WGPTREVFTNPRHELTEK 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-236 |
4.16e-30 |
|
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: 112.32 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDP---RSSL 96
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQIGLVSQDVflfNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRaiteplrspvaRRTTRQQRKD--RLAKVM-----VDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVL 169
Cdd:cd03251 93 AENIAYGR-----------PGATREEVEEaaRAANAHefimeLPEGYDTVIGER-GVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 170 VADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVY 236
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-227 |
4.70e-30 |
|
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: 118.04 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIrELRRSAAMVFQDPR---SSL 96
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPA-DLRRNIGYVPQDPRlfyGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEplrspvarrTTRQQRKDRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:TIGR03375 556 RDNIALGAPYAD---------DEEILRAAELAGVTEFVRRHPDGLDMQIGErgrsLSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRhLCDTVAVMSVGRIV 227
Cdd:TIGR03375 627 EPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIV 678
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-232 |
4.90e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 7 VEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG----------TSLTDAN 76
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqePPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 77 AIRElrrSAAMVFQDPRSSLDPRMSIGRAITEPLRSP--VARRTTRQQRKD------RLAKVMVDVGLDPESASRFPHEF 148
Cdd:COG0488 77 TVLD---TVLDGDAELRALEAELEELEAKLAEPDEDLerLAELQEEFEALGgweaeaRAEEILSGLGFPEEDLDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDV-SVRaqvlnLLNDLVRERGLTMIFVSHDlgvvRHLCDTVavmsVGRIV 227
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD----RYFLDRV----ATRIL 220
|
....*..
gi 488473195 228 E--RGKL 232
Cdd:COG0488 221 EldRGKL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-214 |
9.33e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.45 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELR-RSAAMVFQdpRSSLD 97
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAELRnQKLGFIYQ--FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEPLrspVARRTTRQQRKDRLAKVMVDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK11629 100 PDFTALENVAMPL---LIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHL 214
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-230 |
1.78e-29 |
|
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: 110.54 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsLTDANAIRELRRS 84
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMvDVGldpESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:cd03266 80 LGFVSDSTG--LYDRLTARENLEYFAGLYGLKGDELTARLEELADRL-GME---ELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-207 |
2.38e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.98 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAI 78
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtlDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELRRSA-AMVFQdpRSSLDPRMSIGRAITEPlrsPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:PRK10535 81 AQLRREHfGFIFQ--RYHLLSHLTAAQNVEVP---AVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHD 207
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-230 |
2.86e-29 |
|
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: 110.50 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTsLTDANAIRELRRSAAMVFQDPRSSLD-PRMS 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFGQKTQLWWDlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IGRAITEPLRSPVARrttRQQRKDRLAKvMVDVGLDPESASRfphEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:cd03267 115 SFYLLAAIYDLPPAR---FKKRLDELSE-LLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488473195 182 VRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-237 |
3.87e-29 |
|
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: 115.18 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHLHLGSSSGgTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiREL 81
Cdd:TIGR02204 335 RGEIEFEQVNFAYPARPD-QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP-AEL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPrssldprmsigraitePLRSPVARRTTRQQRKDRLAKVMVDVGLDPESA---SRFPHEF---------- 148
Cdd:TIGR02204 413 RARMALVPQDP----------------VLFAASVMENIRYGRPDATDEEVEAAARAAHAHefiSALPEGYdtylgergvt 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 -SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIV 227
Cdd:TIGR02204 477 lSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIV 553
|
250
....*....|
gi 488473195 228 ERGKLADVYR 237
Cdd:TIGR02204 554 AQGTHAELIA 563
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-227 |
3.98e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.58 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DANAIRELRRSAAMVFQDPRSSL 96
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DprmsigRAITEPLRSP--VARRTTRQQRKdRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:PRK10908 93 D------RTVYDNVAIPliIAGASGDDIRR-RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473195 175 VSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-248 |
4.16e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSsggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD-----SGTVRFRGTSL--T 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 74 DANAIrELRRSAAMVFQDPRSSldPRMSI--GRAITEPLRSPVarrTTRQQRKDRLAKVMVDVGLDPESASR---FPHEF 148
Cdd:PRK14267 77 DVDPI-EVRREVGMVFQYPNPF--PHLTIydNVAIGVKLNGLV---KSKKELDERVEWALKKAALWDEVKDRlndYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|
gi 488473195 229 RGKLADVYRDPQHVVTQELL 248
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYV 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-235 |
6.42e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.97 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT-----DANA--IrelrrsaAMVFQD 91
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprDAIAlgI-------GMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 92 PrsSLDPRMS------IGRaitEPLRSPVARRttRQQRKdRLAKVMVDVGL--DPEsasRFPHEFSGGQRQRIAIARALV 163
Cdd:COG3845 89 F--MLVPNLTvaenivLGL---EPTKGGRLDR--KAARA-RIRELSERYGLdvDPD---AKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 164 TEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-230 |
7.07e-29 |
|
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: 108.83 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDPR---SSLD 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQDVTlfyGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEplrspvarrTTRQQRKDRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:cd03245 96 DNITLGAPLAD---------DERILRAAELAGVTDFVNKHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRhLCDTVAVMSVGRIVERG 230
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-231 |
9.50e-29 |
|
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: 108.86 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:cd03253 1 IEFENVTF---AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLDprmSIGRAITeplrspVARRTTRQQRKDRLAKV-MVDvgldpESASRFPHEF-----------SGGQ 152
Cdd:cd03253 77 IGVVPQDTVLFND---TIGYNIR------YGRPDATDEEVIEAAKAaQIH-----DKIMRFPDGYdtivgerglklSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 153 RQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGK 231
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-230 |
1.33e-28 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 114.07 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:TIGR01193 474 IVINDVSYSYGY---GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-RHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDP---RSSLDPRMSIGraiteplrspvARRTTRQQRKDR---LAKVMVDV-----GLDPESASRfPHEFSGGQR 153
Cdd:TIGR01193 550 INYLPQEPyifSGSILENLLLG-----------AKENVSQDEIWAaceIAEIKDDIenmplGYQTELSEE-GSSISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 154 QRIAIARALVTEPDVLVADEPVSALDVSVRAQVL-NLLNdlVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVnNLLN--LQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-208 |
1.62e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTdanAIRELRRSA--AMVFQDPRSSLDPRM 100
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT---KLPEYKRAKyiGRVFQDPMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SI--------GRAITEPLRspvaRRTTRQQR---KDRLAKV-------MVD-VGLdpesasrfpheFSGGQRQRIAIARA 161
Cdd:COG1101 98 TIeenlalayRRGKRRGLR----RGLTKKRRelfRELLATLglglenrLDTkVGL-----------LSGGQRQALSLLMA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488473195 162 LVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDL 208
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-229 |
2.68e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.25 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRelrrsaAMVFQDp 92
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 rSSLDPRMSIGRAITEPLRspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK11248 79 -EGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMS--VGRIVER 229
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-230 |
2.70e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.75 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPrssldp 98
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDA------ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 rMSIGRAITEPLR--------SPVARRTTRQQRKDRLAKVmvDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:PRK13657 419 -GLFNRSIEDNIRvgrpdatdEEMRAAAERAQAHDFIERK--PDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-239 |
2.86e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 110.32 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDanaiRELR-RSAAMVFQDprSSLD 97
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----LEPAdRDIAMVFQN--YALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEPLRSpvaRRTTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK11650 89 PHMSVRENMAYGLKI---RGMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK11650 165 LDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-251 |
3.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDS---GTVRFRGTSLTdANAIRELRRSAAMVFQDPRSSLdpr 99
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLT-AKTVWDIREKVGIVFQNPDNQF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 msIGRAITEPlrspVA-----RRTTRQQRKDRLAKVMVDVG-LDPESASrfPHEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:PRK13640 98 --VGATVGDD----VAfglenRAVPRPEMIKIVRDVLADVGmLDYIDSE--PANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDPqhvvtqELLRAI 251
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV------EMLKEI 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-251 |
6.17e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:COG4604 2 IEIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLDPRMSIgraitEPL----RSPVAR-RTTRQQRKdrlakvMVD-----VGLDPeSASRFPHEFSGGQRQ 154
Cdd:COG4604 77 LAILRQEN--HINSRLTV-----RELvafgRFPYSKgRLTAEDRE------IIDeaiayLDLED-LADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKlad 234
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT--- 219
|
250
....*....|....*..
gi 488473195 235 vyrdPQHVVTQELLRAI 251
Cdd:COG4604 220 ----PEEIITPEVLSDI 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-240 |
1.02e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.81 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 41 GGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA-NAIR---ELRRsAAMVFQDPRssLDPRMSI-GRaitepLRSPVA 115
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAeKGIClppEKRR-IGYVFQDAR--LFPHYKVrGN-----LRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 116 RrtTRQQRKDRLAKVMvdvGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVR 195
Cdd:PRK11144 103 K--SMVAQFDKIVALL---GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488473195 196 ERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-227 |
2.55e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLhlhlgsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSA 85
Cdd:COG1129 258 EVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSS-LDPRMSIGRAITEPLRSPVARR--TTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARAL 162
Cdd:COG1129 330 AYVPEDRKGEgLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-226 |
2.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSSGgTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRE 80
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQE-KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDPRSSLdprmsIGRAITEPlrspVA-----RRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQR 155
Cdd:PRK13650 79 IRHKIGMVFQNPDNQF-----VGATVEDD----VAfglenKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRhLCDTVAVMSVGRI 226
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-227 |
3.97e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS- 84
Cdd:COG3845 259 EVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS-PRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDP-RSSLDPRMSIGR--AITEPLRSPVARRTTRQQRK-DRLAKVMV---DV-GLDPESASRFpheFSGGQRQRI 156
Cdd:COG3845 335 VAYIPEDRlGRGLVPDMSVAEnlILGRYRRPPFSRGGFLDRKAiRAFAEELIeefDVrTPGPDTPARS---LSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-246 |
4.41e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.13 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQP-DS-----GTVRFRGTSLTDANAIReLRRSAAMVFQDPRSSld 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIK-LRKEVGMVFQQPNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRMSIGRAITEPLRSPVARRttRQQRKDRLAKVMVDVGLDPESASRF---PHEFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKE--KREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 175 VSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQE 246
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-230 |
5.18e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 5.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDPRSSLDpr 99
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-TLASLRRQVALVSQDVVLFND-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 mSIGRAITEPLRSPVARRTTRQQRKDRLAKVMVD---VGLDP---ESASRFphefSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:TIGR02203 421 -TIANNIAYGRTEQADRAEIERALAAAYAQDFVDklpLGLDTpigENGVLL----SGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-254 |
6.09e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVR------------FRGTSLTDANAIR---ELRRSAAM 87
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknnHELITNPYSKKIKnfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 88 VFQDPRSSLDpRMSIGRAItepLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPD 167
Cdd:PRK13631 121 VFQFPEYQLF-KDTIEKDI---MFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 168 VLVADEPVSALDVSVRAQVLNLLNDlVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQEL 247
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSI 275
|
....*..
gi 488473195 248 lrAIPRI 254
Cdd:PRK13631 276 --QVPRV 280
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-230 |
6.10e-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: 103.51 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA--NAI------RELRRSaamvfq 90
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAarNRIgylpeeRGLYPK------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 91 dpRSSLDPRMSIGRaitepLRSpVARRTTRQQRKDRLAKVmvdvGLDPESASRFpHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:cd03269 85 --MKVIDQLVYLAQ-----LKG-LKKEEARRRIDEWLERL----ELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-226 |
8.47e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 104.37 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnaiRELRRsaaMVFQDPRssLDP 98
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTR---LMFQDAR--LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITEPLRSpvarrttrqQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:PRK11247 95 WKKVIDNVGLGLKG---------QWRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-221 |
1.16e-26 |
|
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: 107.76 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDP---RSS 95
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIAWVPQHPflfAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 96 LDPRMSIGRAITEPLRSpvaRRTTRQQRKDRLAKVMVDvGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:TIGR02857 412 IAENIRLARPDASDAEI---REALERAGLDEFVAALPQ-GLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488473195 176 SALDVSVRAQVLNLLNDLVRERglTMIFVSHDLgVVRHLCDTVAVM 221
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGR--TVLLVTHRL-ALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-230 |
1.81e-26 |
|
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: 102.69 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:cd03254 3 IEFENVNF---SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrssldprMSIGRAITEPLRspVARRTTRQQRKDRLAKVmvdVGLDPEsASRFP-----------HEFSGGQR 153
Cdd:cd03254 79 IGVVLQDT-------FLFSGTIMENIR--LGRPNATDEEVIEAAKE---AGAHDF-IMKLPngydtvlgengGNLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 154 QRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-219 |
4.16e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfRGTSLTDAnairelrrs 84
Cdd:COG0488 316 LELEGLSK----SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVKIG--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 aamVF-QDpRSSLDPRMSIGRAITEplrspVARRTTRQQRKDRLAkvmvDVGLDPESASRFPHEFSGGQRQRIAIARALV 163
Cdd:COG0488 382 ---YFdQH-QEELDPDKTVLDELRD-----GAPGGTEQEVRGYLG----RFLFSGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 164 TEPDVLVADEPVSALDVsvraQVLNLLNDLVRERGLTMIFVSHDlgvvRHLCDTVA 219
Cdd:COG0488 449 SPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHD----RYFLDRVA 496
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-218 |
4.64e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 10 LHL-HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMV 88
Cdd:PRK10247 8 LQLqNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 89 FQDPrssldprMSIGRAITEPLRSPVARRTTRQQRKdRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDV 168
Cdd:PRK10247 87 AQTP-------TLFGDTVYDNLIFPWQIRNQQPDPA-IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473195 169 LVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTV 218
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-246 |
5.65e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.16 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQI-EVEDLHLHLGSSSggtnALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAM--MALRQPD---SGTVRFRGTSLTD 74
Cdd:PRK14239 1 MTEPIlQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 75 ANA-IRELRRSAAMVFQDPrsslDP-RMSIGRAITEPLR----------SPVARRTTRQ-----QRKDRLAKVMVdvGLd 137
Cdd:PRK14239 77 PRTdTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRlkgikdkqvlDEAVEKSLKGasiwdEVKDRLHDSAL--GL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 138 pesasrfphefSGGQRQRIAIARALVTEPDVLVADEPVSALD-VS---VRAQVLNLLNDlvrergLTMIFVSHDLGVVRH 213
Cdd:PRK14239 150 -----------SGGQQQRVCIARVLATSPKIILLDEPTSALDpISagkIEETLLGLKDD------YTMLLVTRSMQQASR 212
|
250 260 270
....*....|....*....|....*....|...
gi 488473195 214 LCDTVAVMSVGRIVERGKLADVYRDPQHVVTQE 246
Cdd:PRK14239 213 ISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-230 |
6.56e-26 |
|
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: 101.07 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG--TSLTDANA-------IRELRRSAAMVFQDPR 93
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGgfnpeltGRENIYLNGRLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 SSLDPRMS-------IGRAITEPLRspvarrttrqqrkdrlakvmvdvgldpesasrfphEFSGGQRQRIAIARALVTEP 166
Cdd:cd03220 117 KEIDEKIDeiiefseLGDFIDLPVK-----------------------------------TYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 167 DVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-246 |
7.74e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDS-----GTVRFRGTSLTDANA-IRELRRSAAMVFqdPRSSLD 97
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVnLNRLRRQVSMVH--PKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PrMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASRFPH---EFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:PRK14258 101 P-MSVYDNVAYGVK--IVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 175 VSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMS-----VGRIVERGKLADVYRDPQHVVTQE 246
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-258 |
1.01e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.01 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPD---SGTVRFRGTSLTdANAIRELRRSA-AMVFQDprS 94
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQ-ASNIRDTERAGiAIIHQE--L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 95 SLDPRMSIGRAI---TEPLRSPVARRTTRQQRKDR-LAKVMVDVglDPESASRfphEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:PRK13549 92 ALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKlLAQLKLDI--NPATPVG---NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAV----------------------MSVGRive 228
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVirdgrhigtrpaagmteddiitMMVGR--- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488473195 229 rgKLADVYRDPQHVVTQELLRA---------IPRI-RVDD 258
Cdd:PRK13549 243 --ELTALYPREPHTIGEVILEVrnltawdpvNPHIkRVDD 280
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-212 |
1.11e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfrgtsltdanaiRELRRSAAMVFQdpRSSL 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQ--RSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPR--------MSIGRAitePLRSPVaRRTTRQQRKdRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDV 168
Cdd:NF040873 67 PDSlpltvrdlVAMGRW---ARRGLW-RRLTRDDRA-AVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488473195 169 LVADEPVSALDVSVRAQVLNLLNDLVReRGLTMIFVSHDLGVVR 212
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVR 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-238 |
1.25e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.99 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRssLDPR 99
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELH--LVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAI---TEPLRSP-VARRTTRQQRKDRLAKVMVDVglDPESASRfphEFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK11288 94 MTVAENLylgQLPHKGGiVNRRLLNYEAREQLEHLGVDI--DPDTPLK---YLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 176 SALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVER-GKLADVYRD 238
Cdd:PRK11288 169 SSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRD 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-230 |
1.41e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALR--QPDSGTVRFRGTSLTDAnAIRElrR 83
Cdd:COG0396 2 EIKNLHV----SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILEL-SPDE--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAA---MVFQDPrssldprMSI-GRAITEPLRSPV-ARRTTRQQRKD---RLAKVMVDVGLDPESASRFPHE-FSGGQRQ 154
Cdd:COG0396 75 ARAgifLAFQYP-------VEIpGVSVSNFLRTALnARRGEELSAREflkLLKEKMKELGLDEDFLDRYVNEgFSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDV-SVRAqVLNLLNDLvRERGLTMIFVSHDLGVVRHL-CDTVAVMSVGRIVERG 230
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKL-RSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSG 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-251 |
1.83e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGT---SLTDANaIRELRRSA-AMVFQDprSSLDPRMSI- 102
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAE-LREVRRKKiAMVFQS--FALMPHMTVl 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 -GRAITEPLRSPVArrttrQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:PRK10070 125 dNTAFGMELAGINA-----EERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 182 VRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVTQELLRAI 251
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-230 |
3.06e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 104.27 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEdlHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:TIGR03797 452 IEVD--RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD-VQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPR---SSLDPRMSIGRAITEPLRSPVARRttrqqrkdrlakvmvdVGLDpESASRFP---H--------EFSG 150
Cdd:TIGR03797 529 LGVVLQNGRlmsGSIFENIAGGAPLTLDEAWEAARM----------------AGLA-EDIRAMPmgmHtvisegggTLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 151 GQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvrerGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-230 |
4.03e-25 |
|
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: 99.11 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDP---- 92
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSRISIIPQDPvlfs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 ---RSSLDPrmsIGRAITEPLRSPVAR---RTTRQQRKDRLAKVMVDVGLDpesasrfpheFSGGQRQRIAIARALVTEP 166
Cdd:cd03244 92 gtiRSNLDP---FGEYSDEELWQALERvglKEFVESLPGGLDTVVEEGGEN----------LSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 167 DVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-230 |
6.23e-25 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 98.25 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHLHLGSSSggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIREL 81
Cdd:cd03369 4 HGEIEVENLSVRYAPDL--PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDP-------RSSLDP-RMSIGRAITEPLRspvarrttrqqrkdrlakvMVDVGLDpesasrfpheFSGGQR 153
Cdd:cd03369 81 RSSLTIIPQDPtlfsgtiRSNLDPfDEYSDEEIYGALR-------------------VSEGGLN----------LSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 154 QRIAIARALVTEPDVLVADEPVSALDVSVRAqvlnLLNDLVRE--RGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDA----LIQKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-207 |
9.68e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 98.31 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQ--IEVEDLHLHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT--DAN 76
Cdd:PRK10584 1 MPAEniVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 77 AIRELR-RSAAMVFQDprSSLDPRMSIGRAITEPlrsPVARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQR 155
Cdd:PRK10584 81 ARAKLRaKHVGFVFQS--FMLIPTLNALENVELP---ALLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD 207
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-230 |
9.79e-25 |
|
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: 97.00 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAirELRRS 84
Cdd:cd03247 1 LSINNVSFSYPEQE--QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssldprmsigrAITEPLRSPVARRttrqqrkdrlakvmvdvgldpesasrfpheFSGGQRQRIAIARALVT 164
Cdd:cd03247 77 ISVLNQRPY-----------LFDTTLRNNLGRR------------------------------FSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHLcDTVAVMSVGRIVERG 230
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-231 |
1.51e-24 |
|
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: 102.13 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIrELRRSAAMVFQD----PRSSLD-- 97
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA-WLRRQMGVVLQEnvlfSRSIRDni 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 ----PRMSIGRAITEPlrspvarrttrqqrkdRLAKVMvdvgldpESASRFPHEF-----------SGGQRQRIAIARAL 162
Cdd:TIGR01846 552 alcnPGAPFEHVIHAA----------------KLAGAH-------DFISELPQGYntevgekganlSGGQRQRIAIARAL 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGK 231
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICRGR--TVIIIAHRLSTVRA-CDRIIVLEKGQIAESGR 674
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-231 |
1.62e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtdANAIRE 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQdpRSSLDPRMSigraITEPLRspVARR---TTRQQRKDRLAKVMVDVGLDPESASRFpHEFSGGQRQRIA 157
Cdd:PRK13537 78 ARQRVGVVPQ--FDNLDPDFT----VRENLL--VFGRyfgLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-243 |
1.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLHLGSSSGgTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRE 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDPRSSLdprmsIGRAITEPLRSPVARR-TTRQQRKDRLAKVMVDVGLdPESASRFPHEFSGGQRQRIAIA 159
Cdd:PRK13642 79 LRRKIGMVFQNPDNQF-----VGATVEDDVAFGMENQgIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 160 RALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
....
gi 488473195 240 QHVV 243
Cdd:PRK13642 232 EDMV 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-236 |
1.89e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.54 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLT-DANAIRELRRSAAMVFQDPRSSLDpRMSI 102
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPEQQIF-YTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAITEPLRS------PVARRttrqqrkdrlakvmVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK13638 96 DSDIAFSLRNlgvpeaEITRR--------------VDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVY 236
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-226 |
2.49e-24 |
|
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: 95.75 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNA--LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtdanairelr 82
Cdd:cd03246 1 LEVENVSF----RYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 rsaamvfqdprSSLDPRmsigraiteplrspvarrttrqQRKDRLAKVMVDVGLDPESASRfpHEFSGGQRQRIAIARAL 162
Cdd:cd03246 67 -----------SQWDPN----------------------ELGDHVGYLPQDDELFSGSIAE--NILSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRhLCDTVAVMSVGRI 226
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
2.80e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 101.28 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLGsssGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELR 82
Cdd:TIGR02868 333 PTLELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ-DEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPR---SSLDPRMSIGRA-ITEPLRSPVARRTTRQQRKDRLAKvmvdvGLDP---ESASRFphefSGGQRQR 155
Cdd:TIGR02868 409 RRVSVCAQDAHlfdTTVRENLRLARPdATDEELWAALERVGLADWLRALPD-----GLDTvlgEGGARL----SGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473195 156 IAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvrERGLTMIFVSHDL 208
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-234 |
3.57e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.62 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 22 NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKaMMA-LRQPDSGTVRFRGtsLTDANAIRELRRSAAMVF-QdpRSSL--D 97
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIK-MLTgILVPTSGEVRVLG--YVPFKRRKEFARRIGVVFgQ--RSQLwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 --PRMS--IGRAITE-PlrspvarRTTRQQRKDRLAKVMvDVGldpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:COG4586 111 lpAIDSfrLLKAIYRiP-------DAEYKKRLDELVELL-DLG---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-219 |
4.53e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 94.05 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfrgtsltdanairelrrs 84
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 aamvfqdprssLDPRMSIGRaiteplrspvarrttrqqrkdrlakvmvdvgldpesasrFPHeFSGGQRQRIAIARALVT 164
Cdd:cd03221 59 -----------WGSTVKIGY---------------------------------------FEQ-LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 165 EPDVLVADEPVSALDVSVRAQVLNLLNDLvreRGlTMIFVSHDlgvvRHLCDTVA 219
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEY---PG-TVILVSHD----RYFLDQVA 134
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-251 |
6.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVrFRGTSLTDAN-----AIRELRRSAAMVFQDPRSSLD 97
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANlkkikEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 pRMSIGRAITeplRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13645 105 -QETIEKDIA---FGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDpqhvvtQELLRAI 251
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKI 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-244 |
7.14e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.09 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQP-----DSGTVRFRGTSLTDANAIRELRRSAAMVFQDPr 93
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 sslDP-RMSIGRAITEPLRSP--VARRTTRQQRKDRLAKV-MVDVGLDPESASrfPHEFSGGQRQRIAIARALVTEPDVL 169
Cdd:PRK14271 111 ---NPfPMSIMDNVLAGVRAHklVPRKEFRGVAQARLTEVgLWDAVKDRLSDS--PFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 170 VADEPVSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQHVVT 244
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-247 |
8.36e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 99.51 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDS--GTVRFRGTSLTdANAIRELRRsAAMVFQDPRSSL 96
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLK-ASNIRDTER-AGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSI------GRAITEPlrspvARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:TIGR02633 90 VPELSVaeniflGNEITLP-----GGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMsvgrivergkladvyRDPQHVVTQEL 247
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVI---------------RDGQHVATKDM 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-230 |
1.13e-23 |
|
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: 94.52 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALR--QPDSGTVRFRGTSLTDANAIRELR 82
Cdd:cd03217 1 LEIKDLHV----SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPrssldPRMSiGRAITEPLRSpvarrttrqqrkdrlakvmVDVGldpesasrfpheFSGGQRQRIAIARAL 162
Cdd:cd03217 77 LGIFLAFQYP-----PEIP-GVKNADFLRY-------------------VNEG------------FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHL-CDTVAVMSVGRIVERG 230
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-231 |
1.30e-23 |
|
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: 95.63 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQ--------- 90
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQenvlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 91 -DPRSSLDPRMSIGRAITEPlrspvarrttrqqrkdRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTE 165
Cdd:cd03252 93 rDNIALADPGMSMERVIEAA----------------KLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGK 231
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-252 |
1.74e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.62 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRS---SL 96
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAegmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAitePLRSPVARrtTRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:PRK10575 103 RELVAIGRY---PWHGALGR--FGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 177 ALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPqhvvTQELLRAIP 252
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE----TLEQIYGIP 248
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-239 |
3.94e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPDSGTVRFRGTSLTDANaIRELRRS 84
Cdd:PRK11174 350 IEAEDLEIL---SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELD-PESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPrsSLdPRMSIGRAITepLRSPVArrtTRQQRKDRLAKVMVD-------VGLD---PESASRFphefSGGQRQ 154
Cdd:PRK11174 425 LSWVGQNP--QL-PHGTLRDNVL--LGNPDA---SDEQLQQALENAWVSeflpllpQGLDtpiGDQAAGL----SVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVreRGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLAD 234
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
....*
gi 488473195 235 VYRDP 239
Cdd:PRK11174 570 LSQAG 574
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-240 |
7.58e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.99 E-value: 7.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 29 LHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtdanaiRELRRSAAMVFQDPRSSLDPRMSI------ 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASP------GKGWRHIGYVPQRHEFAWDFPISVahtvms 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRA-ITEPLRSPvaRRTTRQQRKDRLAKVMVDvgldpESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:TIGR03771 75 GRTgHIGWLRRP--CVADFAAVRDALRRVGLT-----ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 182 VRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSvGRIVERGKLADVyRDPQ 240
Cdd:TIGR03771 148 TQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL-QDPA 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-239 |
3.26e-22 |
|
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: 91.45 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDP 92
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 rssldprmSIGRAIT--EPLRSPVARRT-TRQQRKDRLAKVMVDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVL 169
Cdd:cd03218 85 --------SIFRKLTveENILAVLEIRGlSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 170 VADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDlgvVRH---LCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-239 |
4.80e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDPrssLDPRMSIG 103
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH-HYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLRspvarrttrQQRKDRLAKVMVDVGLDpESASRFPHEF-----------SGGQRQRIAIARALVTEPDVLVAD 172
Cdd:TIGR00958 573 ENIAYGLT---------DTPDEEIMAAAKAANAH-DFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 173 EPVSALDvsvrAQVLNLLNDLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-258 |
6.33e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHLHLGSSSGGTNaldgVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIREL 81
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAEN----LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRS----SLDPRMSIGRAITEPLRSpvarrTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGGQRQRIA 157
Cdd:PRK10253 80 ARRIGLLAQNATTpgdiTVQELVARGRYPHQPLFT-----RWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKladvyr 237
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA------ 227
|
250 260
....*....|....*....|....
gi 488473195 238 dPQHVVTQELLRAIPRIR---VDD 258
Cdd:PRK10253 228 -PKEIVTAELIERIYGLRcmiIDD 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-239 |
6.69e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.20 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQI-EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIR 79
Cdd:PRK11300 1 MSQPLlSVSGLMMRFG----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 80 ELRRSAAMVFQDPRssLDPRMSI-------------GRAITEPLRSPVARRTTRQQRkDRLAKVMVDVGLDpESASRFPH 146
Cdd:PRK11300 77 IARMGVVRTFQHVR--LFREMTVienllvaqhqqlkTGLFSGLLKTPAFRRAESEAL-DRAATWLERVGLL-EHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 147 EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 488473195 227 VERGKLADVYRDP 239
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-230 |
7.75e-22 |
|
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: 89.53 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 15 GSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQP--DSGTVRFRGTSLTDanaiRELRRSAAMVFQDp 92
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK----RSFRKIIGYVPQD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 rSSLDPRMSIgraiteplrspvaRRTTRQQRKDRlakvmvdvGLdpesasrfphefSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:cd03213 91 -DILHPTLTV-------------RETLMFAAKLR--------GL------------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDL-GVVRHLCDTVAVMSVGRIVERG 230
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-231 |
1.01e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD---SGTVRFRGTSLTdanaIRELRRSAAMVFQDprssldpRM 100
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID----AKEMRAISAYVQQD-------DL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEP-------LRSPvaRRTTRQQRKDRLAKVMVDVGLDPESASRFPHE-----FSGGQRQRIAIARALVTEPDV 168
Cdd:TIGR00955 110 FIPTLTVREhlmfqahLRMP--RRVTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 169 LVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGV-VRHLCDTVAVMSVGRIVERGK 231
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGS 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-227 |
1.03e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRssLDP 98
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR--VFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITepLRSPVARRTTRQQRKDRLakvmvdVGLDPESASRFPHE---FSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK11614 94 RMTVEENLA--MGGFFAERDQFQERIKWV------YELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473195 176 SALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-246 |
3.37e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSggtnALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMalRQPD-------SGTVRFRGTSLTDANA 77
Cdd:PRK14243 11 LRTENLNVYYGSFL----AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFN--RLNDlipgfrvEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 78 -IRELRRSAAMVFQDPR---SSLDPRMSIGRAIT--EPLRSPVARRTTRQ-----QRKDRLAkvmvDVGLdpesasrfph 146
Cdd:PRK14243 85 dPVEVRRRIGMVFQKPNpfpKSIYDNIAYGARINgyKGDMDELVERSLRQaalwdEVKDKLK----QSGL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 147 EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErgLTMIFVSHDLGVVRHLCDTVAVMSV--- 223
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVelt 228
|
250 260
....*....|....*....|....*....
gi 488473195 224 ------GRIVERGKLADVYRDPQHVVTQE 246
Cdd:PRK14243 229 egggryGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-230 |
4.83e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMAL----RQPDSGTVRFRGTSLTDANAIRELRRSAAM---VFQD---- 91
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRLARDIRKSRANtgyIFQQfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 92 PRSSLDPRMSIGRAITEPLRSPVARRTTRQQrKDRLAKVMVDVGLdpesaSRFPHE----FSGGQRQRIAIARALVTEPD 167
Cdd:PRK09984 99 NRLSVLENVLIGALGSTPFWRTCFSWFTREQ-KQRALQALTRVGM-----VHFAHQrvstLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473195 168 VLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERG 230
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-206 |
5.30e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 3 AQIEVEDLHLHLgssSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfrgtsltdanaireLR 82
Cdd:COG4178 361 GALALEDLTLRT---PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVF--QDPRssldprMSIGRaitepLRSPVAR-RTTRQQRKDRLAKVMVDVGLDP-----ESASRFPHEFSGGQRQ 154
Cdd:COG4178 424 AGARVLFlpQRPY------LPLGT-----LREALLYpATAEAFSDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDlvRERGLTMIFVSH 206
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-246 |
5.76e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRS 84
Cdd:PLN03232 1235 IKFEDVHLRY--RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-GLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDP-------RSSLDPrmsigraITEPLRSPVARRTTRQQRKDRLAKVmvDVGLDPEsASRFPHEFSGGQRQRIA 157
Cdd:PLN03232 1312 LSIIPQSPvlfsgtvRFNIDP-------FSEHNDADLWEALERAHIKDVIDRN--PFGLDAE-VSEGGENFSVGQRQLLS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAqvlnLLNDLVRE--RGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVErgkladv 235
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE------- 1449
|
250
....*....|.
gi 488473195 236 YRDPQHVVTQE 246
Cdd:PLN03232 1450 YDSPQELLSRD 1460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-238 |
5.87e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQD- 91
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 92 ---PRSSLDPRMSIGRAITEPLR--SPVARRTTRQQRKDRLAKVMVDVGLDPESAsrfphEFSGGQRQRIAIARALVTEP 166
Cdd:PRK09700 90 sviDELTVLENLYIGRHLTKKVCgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVA-----NLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 167 DVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-240 |
6.67e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDanaireL---RRSaamvf 89
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH------LpmhKRA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 90 qdprssldpRMSIG------------------RAITEplrspvARRTTRQQRKDRLAKVMVDVGLDpESASRFPHEFSGG 151
Cdd:COG1137 77 ---------RLGIGylpqeasifrkltvedniLAVLE------LRKLSKKEREERLEELLEEFGIT-HLRKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALD-VSVrAQVLNLLNDLvRERGltmifvshdLGV------VRH---LCDTVAVM 221
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL-KERG---------IGVlitdhnVREtlgICDRAYII 209
|
250
....*....|....*....
gi 488473195 222 SVGRIVERGKLADVYRDPQ 240
Cdd:COG1137 210 SEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-226 |
8.54e-21 |
|
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: 87.53 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDPrsSLDPRm 100
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-KYLHSKVSLVGQEP--VLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEPLRS-PVARRTTRQQRKDRLAKVM-VDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:cd03248 103 SLQDNIAYGLQScSFECVKEAAQKAHAHSFISeLASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 179 DVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRI 226
Cdd:cd03248 182 DAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-235 |
1.15e-20 |
|
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: 90.58 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 2 TAQIEVEDLHLHlgsSSGGTNA-LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRE 80
Cdd:COG4618 328 KGRLSVENLTVV---PPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR-EE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDP------------R-SSLDPRMSIGRAiteplrspvarrttrqqrkdRLAKV--MVdvgldpesaSRFP 145
Cdd:COG4618 404 LGRHIGYLPQDVelfdgtiaeniaRfGDADPEKVVAAA--------------------KLAGVheMI---------LRLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 146 HEF-----------SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHl 214
Cdd:COG4618 455 DGYdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA- 532
|
250 260
....*....|....*....|.
gi 488473195 215 CDTVAVMSVGRIVERGKLADV 235
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-227 |
1.86e-20 |
|
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: 86.56 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMAlRQPD----SGTVRFRGTSLTdanaIRELRRSAAMVFQDPR--SSLD 97
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggttSGQILFNGQPRK----PDQFQKCVAYVRQDDIllPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 98 PRmsigraitEPLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHEF----SGGQRQRIAIARALVTEPDVLVADE 173
Cdd:cd03234 98 VR--------ETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVReRGLTMIFVSHDLGV-VRHLCDTVAVMSVGRIV 227
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSdLFRLFDRILLLSSGEIV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-260 |
1.93e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDP 92
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RssLDPRMSIGRAITepLRSPvARRTTRQQRKDRLAKVMVDVGLDPESASrfpheFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK15439 96 L--LFPNLSVKENIL--FGLP-KRQASMQKMKQLLAALGCQLDLDSSAGS-----LEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 173 EPVSALdvsVRAQVLNLLNDL--VRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDpqhvvtqELLRA 250
Cdd:PRK15439 166 EPTASL---TPAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD-------DIIQA 235
|
250
....*....|.
gi 488473195 251 I-PRIRVDDST 260
Cdd:PRK15439 236 ItPAAREKSLS 246
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-230 |
2.56e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.88 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDPrsSL--DprmS 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ-ASLRAAIGIVPQDT--VLfnD---T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 I------GRaiteplrsPVArrtTRQQRKD--RLAKVmvdvgldpesasrfpHEF-------------------SGGQRQ 154
Cdd:COG5265 448 IayniayGR--------PDA---SEEEVEAaaRAAQI---------------HDFieslpdgydtrvgerglklSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 155 RIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-229 |
2.84e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTdanairelrrsaamvFQDPRSS---- 95
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT---------------FNGPKSSqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 96 ---------LDPRMSI------GRAITEPLRSPVARRTTRQQRKdRLAKVMVdvgldPESASRFPHEFSGGQRQRIAIAR 160
Cdd:PRK10762 81 igiihqelnLIPQLTIaeniflGREFVNRFGRIDWKKMYAEADK-LLARLNL-----RFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 161 ALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGR-IVER 229
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-230 |
7.47e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.62 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDPRSSLDprmSI 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVVSQTPFLFSD---TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAITepLRSPVArrtTRQQ--RKDRLAKVMVDV-----GLDPESASRFPHeFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK10789 406 ANNIA--LGRPDA---TQQEieHVARLASVHDDIlrlpqGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 176 SALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERG 230
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-231 |
1.56e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRS 84
Cdd:PRK11160 339 LTLNNVSF--TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDP-------RSSLdpRMSIGRAITEplrspvarrttrqqrkdRLAKVMVDVGL-----DPESASRFPHE----F 148
Cdd:PRK11160 416 ISVVSQRVhlfsatlRDNL--LLAAPNASDE-----------------ALIEVLQQVGLeklleDDKGLNAWLGEggrqL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHLcDTVAVMSVGRIVE 228
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
...
gi 488473195 229 RGK 231
Cdd:PRK11160 554 QGT 556
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-247 |
3.32e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIR--ELR 82
Cdd:PRK11831 8 VDMRGVSF----TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDprSSLDPRMSIGRAITEPLR------SPVARRTtrqqrkdrlakVMVD---VGLDPeSASRFPHEFSGGQR 153
Cdd:PRK11831 84 KRMSMLFQS--GALFTDMNVFDNVAYPLRehtqlpAPLLHST-----------VMMKleaVGLRG-AAKLMPSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 154 QRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLA 233
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
250
....*....|....
gi 488473195 234 DVYRDPQHVVTQEL 247
Cdd:PRK11831 230 ALQANPDPRVRQFL 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-234 |
3.68e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRRSAAMVFQDPRSSLDprm 100
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASLRNQVALVSQNVHLFND--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEPLRspvaRRTTRQQ--RKDRLAKVM-----VDVGLDP----ESASrfpheFSGGQRQRIAIARALVTEPDVL 169
Cdd:PRK11176 432 TIANNIAYART----EQYSREQieEAARMAYAMdfinkMDNGLDTvigeNGVL-----LSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 170 VADEPVSALDV-SVRAqVLNLLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLAD 234
Cdd:PRK11176 503 ILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-235 |
9.38e-19 |
|
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: 85.09 E-value: 9.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDprssldprmsig 103
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR-ETFGKHIGYLPQD------------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 raiTEPLRSPVARRTTR-----QQRKDRLAKVMVDVGldpESASRFPHEF-----------SGGQRQRIAIARALVTEPD 167
Cdd:TIGR01842 401 ---VELFPGTVAENIARfgenaDPEKIIEAAKLAGVH---ELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 168 VLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVrHLCDTVAVMSVGRIVERGKLADV 235
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-230 |
2.99e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDA---NAIRELRRSAAMVFQDPRSSL 96
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqkNLVAYVPQSEEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEPLRSPVARrtTRQQRKDRLAKV-MVDVgldpesASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKR--DRQIVTAALARVdMVEF------RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 176 SALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDtVAVMSVGRIVERG 230
Cdd:PRK15056 171 TGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-256 |
3.85e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLkAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQdpRSSLDPRMSIG 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLL-ARMAGLLPGQGEILLNGRPLSDWSA-AELARHRAYLSQ--QQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLRSPVArrttRQQRKDRLAKVMVDVGLDPEsASRFPHEFSGGQRQRIAIARALV-----TEPD--VLVADEPVS 176
Cdd:COG4138 88 QYLALHQPAGAS----SEAVEQLLAQLAEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 177 ALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLG-VVRHlCDTVAVMSVGRIVERGKladvyrdPQHVVTQELLRAIPRIR 255
Cdd:COG4138 163 SLDVAQQAALDRLLRELC-QQGITVVMSSHDLNhTLRH-ADRVWLLKQGKLVASGE-------TAEVMTPENLSEVFGVK 233
|
.
gi 488473195 256 V 256
Cdd:COG4138 234 F 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-243 |
4.55e-18 |
|
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: 83.31 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQ--PDSGTVRFR-------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 69 ---------GTSLT---------DANAIRELRRSAAMVFQDPRSSLDPRmsigRAITEPLRSPVARRTTRQQRKDRLAKV 130
Cdd:TIGR03269 77 kvgepcpvcGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFALYGDD----TVLDNVLEALEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 131 MVDVGLDpesaSRFPH---EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD 207
Cdd:TIGR03269 153 IEMVQLS----HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 488473195 208 LGVVRHLCDTVAVMSVGRIVERGkladvyrDPQHVV 243
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEG-------TPDEVV 257
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-228 |
1.49e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.09 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDP-------RSSL 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-GLMDLRKVLGIIPQAPvlfsgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRA-ITEPLRSP----VARRTTRqqrkdrlakvmvdvGLDPEsASRFPHEFSGGQRQRIAIARALVTEPDVLVA 171
Cdd:PLN03130 1334 DPFNEHNDAdLWESLERAhlkdVIRRNSL--------------GLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 172 DEPVSALDVSVRAqvlnLLNDLVRE--RGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVE 228
Cdd:PLN03130 1399 DEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-225 |
1.63e-17 |
|
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: 78.28 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTN-ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsltdanairelrr 83
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDP--RSsldprMSIGRAIT--EPLRspvarrttrqqrKDRLAKVMVDVGLDPESASrFPH-------E----F 148
Cdd:cd03250 67 SIAYVSQEPwiQN-----GTIRENILfgKPFD------------EERYEKVIKACALEPDLEI-LPDgdlteigEkginL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLN--LLNDLVRERglTMIFVSHDLGVVRHlCDTVAVMSVGR 225
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-228 |
1.76e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRS-------SLDPR 99
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDngffpnfSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAI-------TEPLRSPVARRTTRQQRKDRLAkvmvdvgLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK09700 362 MAISRSLkdggykgAMGLFHEVDEQRTAENQRELLA-------LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-231 |
1.88e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 1 MTAQIEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAiRE 80
Cdd:PRK10790 337 QSGRIDIDNVSF---AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH-SV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDP---RSSLDPRMSIGRAITEplrSPVARRTTRQQRKDrLAKVMVDvGLDPESASRfPHEFSGGQRQRIA 157
Cdd:PRK10790 413 LRQGVAMVQQDPvvlADTFLANVTLGRDISE---EQVWQALETVQLAE-LARSLPD-GLYTPLGEQ-GNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNdLVRERgLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGK 231
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-246 |
2.47e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 25 DGVSLHVNEGQRLGLVGGSGAGKSTLLKAMM-ALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQD-PRSSLDPRMSI 102
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDrKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAITEPLRSPVARR---------TTRQQRKDRL----AKVMVDVGldpesasrfphEFSGGQRQRIAIARALVTEPDVL 169
Cdd:PRK13549 359 GKNITLAALDRFTGGsriddaaelKTILESIQRLkvktASPELAIA-----------RLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 170 VADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIveRGKLadvyrdPQHVVTQE 246
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL--KGDL------INHNLTQE 495
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-231 |
3.57e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 17 SSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnaIRELRRSAAMVFQdpRSSL 96
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARARIGVVPQ--FDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITeplrspVARRTTRQQRKDRLAKV--MVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:PRK13536 126 DLEFTVRENLL------VFGRYFGMSTREIEAVIpsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 175 VSALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGK 231
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-232 |
5.02e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRF-----------------RGTSLT--------DANAI 78
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvEGTVYDfvaegieeQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 79 RELRRSAAMVFQDPRSSLDPRMSIGRAITEPLRSpvarrttrQQRKDRLAKVMVDVGLDPESASRfphEFSGGQRQRIAI 158
Cdd:PRK11147 99 KRYHDISHLVETDPSEKNLNELAKLQEQLDHHNL--------WQLENRINEVLAQLGLDPDAALS---SLSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 159 ARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvreRGlTMIFVSHDLGVVRHlcdtvavMSVgRIV--ERGKL 232
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QG-SIIFISHDRSFIRN-------MAT-RIVdlDRGKL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-226 |
6.50e-17 |
|
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: 79.87 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMM-ALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQD-PRSSLDPRMS 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IGRAITeplRSPVARRTTRQQRKDRLAKVMVDVG---LDPESASRF--PHEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:TIGR02633 356 VGKNIT---LSVLKSFCFKMRIDAAAELQIIGSAiqrLKVKTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473195 177 ALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-228 |
7.47e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDS--GTVRFRGtsltdanairELRRsaamvFQDPRSS- 95
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG----------EVCR-----FKDIRDSe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 96 ------------LDPRMSIGRAI---TEPLRSPVA-RRTTRQQRKDRLAKVmvdvGLDpESASRFPHEFSGGQRQRIAIA 159
Cdd:NF040905 77 algiviihqelaLIPYLSIAENIflgNERAKRGVIdWNETNRRARELLAKV----GLD-ESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 160 RALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-247 |
1.26e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQD-----PRS 94
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQElnlvlQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 95 SLDpRMSIGRAitePLRSP-VARRTTRQQRKDRLAKVMVDVglDPESASRfphEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:PRK10982 90 VMD-NMWLGRY---PTKGMfVDQDKMYRDTKAIFDELDIDI--DPRAKVA---TLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 174 PVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMsvgrivergkladvyRDPQHVVTQEL 247
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL---------------RDGQWIATQPL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-240 |
1.29e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDP 92
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 rsSLDPRMSIGRAITEPLRspVARRTTRQQRKDRLAKVMVDVGLDPESASrFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:PRK10895 88 --SIFRRLSVYDNLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHLRDS-MGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-218 |
1.36e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 13 HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfrgtsltdanaiRELRRSAAMVFQdp 92
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIGYVPQ-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 RSSLDPRM--SIGRAITepLRSPVARRTTRQQRKDRLAKVMVDVGLdpesasrfpHEFSGGQRQRIAIARALVTEPDVLV 170
Cdd:PRK09544 75 KLYLDTTLplTVNRFLR--LRPGTKKEDILPALKRVQAGHLIDAPM---------QKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 171 ADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTV 218
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-206 |
1.95e-16 |
|
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: 74.50 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVrfrgtsltdanairELRRS 84
Cdd:cd03223 1 IELENLSL---ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRssldPRMSIGraiteplrspvarrTTRQQrkdrlakvmvdvgldpesaSRFP--HEFSGGQRQRIAIARAL 162
Cdd:cd03223 64 EDLLFLPQR----PYLPLG--------------TLREQ-------------------LIYPwdDVLSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488473195 163 VTEPDVLVADEPVSALDVSVRAQVLNLLndlvRERGLTMIFVSH 206
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-226 |
2.76e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRSS---LDPRMSIG 103
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSglyLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 R-AITEPLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRfphEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSV 182
Cdd:PRK15439 362 VcALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488473195 183 RAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:PRK15439 439 RNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-250 |
7.07e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAN---AIR-------ELRRSAAMVfqdPRSSL 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdAIRagimlcpEDRKAEGII---PVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIG-RAITEPLRSPVARRTTRQQRKDRLAKVMVDVGlDPESASRFpheFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PRK11288 349 ADNINISaRRHHLRAGCLINNRWEAENADRFIRSLNIKTP-SREQLIMN---LSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 176 SALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVerGKLADVYRDPQHVVTQELLRA 250
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAREQATERQALSLALPRT 496
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-211 |
9.11e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 14 LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtdaNAIRELRRSAaMVFQDPR 93
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---AEQRDEPHEN-ILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 94 SSLDPRMSIgraiTEPLRSPVA-RRTTRQQRKDRLAkvmvDVGLDpESASRFPHEFSGGQRQRIAIARALVTEPDVLVAD 172
Cdd:TIGR01189 82 PGLKPELSA----LENLHFWAAiHGGAQRTIEDALA----AVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 488473195 173 EPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVV 211
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-235 |
1.90e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTllKAMMA-LRQPDSGTVRFRGTSLTdANAiRELRR 83
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**R--GALPAhV*GPDAGRRPWRF*TWC-ANR-RALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAM---VFQDPRSSLDPRMS---IGRAITeplrspVARRTTRQQRKDRLAKVMVDvgldpESASRFPHEFSGGQRQRIA 157
Cdd:NF000106 86 TIG*hrpVR*GRRESFSGRENlymIGR*LD------LSRKDARARADELLERFSLT-----EAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 158 IARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-234 |
1.98e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSgtvrFRGTSLTDANAI-RELRRSAAMVFQDprSSLDPRMSI 102
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPtKQILKRTGFVTQD--DILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAIT--EPLRSPvarRTTRQQRKDRLAK-VMVDVGL----DPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPV 175
Cdd:PLN03211 158 RETLVfcSLLRLP---KSLTKQEKILVAEsVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 176 SALDVSVRAQVLNLLNDLVrERGLTMIFVSHDLGV-VRHLCDTVAVMSVGRIVERGKLAD 234
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-207 |
1.91e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 6 EVEDLHLHLGsssgGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfRGTSLTDAnairelrrsa 85
Cdd:PRK11147 321 EMENVNYQID----GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVA---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 amVFQDPRSSLDPRMSIgraiteplrspvarrttrqqrKDRLAK----VMV------------DVGLDPESAsRFP-HEF 148
Cdd:PRK11147 386 --YFDQHRAELDPEKTV---------------------MDNLAEgkqeVMVngrprhvlgylqDFLFHPKRA-MTPvKAL 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVsvraQVLNLLNDLVRERGLTMIFVSHD 207
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-224 |
2.72e-14 |
|
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: 70.05 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSaamvfqdprssldpR 99
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN--------------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAITEP--LRSPVARRTTRQQ--RKDRLAKVMVDVGLDPEsASRFPH-----------EFSGGQRQRIAIARALVT 164
Cdd:cd03290 79 YSVAYAAQKPwlLNATVEENITFGSpfNKQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 165 EPDVLVADEPVSALDVSV-----RAQVLNLLNDLVRerglTMIFVSHDLGVVRHlCDTVAVMSVG 224
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-226 |
3.06e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLhlhlgSSSGgtnaLDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRS 84
Cdd:PRK10762 258 LKVDNL-----SGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQD-PRSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGL----DPeSASRFPHEFSGGQRQRIAIA 159
Cdd:PRK10762 329 IVYISEDrKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfnikTP-SMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 160 RALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-235 |
3.26e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.85 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsltdanairelrrSAAMVFQDprSSLDPRMSi 102
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAIS--SGLNGQLT- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 grAITEPLRSPVARRTTRQQRKDRLAKVM--VDVGldpesasRFPHE----FSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:PRK13545 102 --GIENIELKGLMMGLTKEKIKEIIPEIIefADIG-------KFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 177 ALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-221 |
3.99e-14 |
|
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: 70.09 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 33 EGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVR-----------FRGTSLTdaNAIRELRRSAAMVFQDPRS-SLDPRM 100
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQ--NYFTKLLEGDVKVIVKPQYvDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITeplrspVARRTTRQQRKDRLAKVMvdvGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDV 180
Cdd:cd03236 103 VKGKVGE------LLKKKDERGKLDELVDQL---ELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488473195 181 SVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVM 221
Cdd:cd03236 173 KQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-211 |
6.12e-14 |
|
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: 68.67 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 14 LGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSltDANAIRELRRSAAMVFQDP- 92
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYLGHAPg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 -RSSLDPRmsigraitEPLRSpVARRTTRQQRKDRLAkvmvDVGLDPESASRFpHEFSGGQRQRIAIARALVTEPDVLVA 171
Cdd:cd03231 84 iKTTLSVL--------ENLRF-WHADHSDEQVEEALA----RVGLNGFEDRPV-AQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488473195 172 DEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVV 211
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-207 |
9.51e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEdlhlHLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSltdanairelrrS 84
Cdd:TIGR03719 323 IEAE----NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV------------K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDpRSSLDPRMSIGRAITE------------PLRSPVAR---RTTRQQRKdrlakvmvdVGldpesasrfphEFS 149
Cdd:TIGR03719 387 LAYVDQS-RDALDPNKTVWEEISGgldiiklgkreiPSRAYVGRfnfKGSDQQKK---------VG-----------QLS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473195 150 GGQRQRIAIARALVTEPDVLVADEPVSALDV-SVRAqvlnlLNDLVRERGLTMIFVSHD 207
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-226 |
1.07e-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: 70.81 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSL-TDANAIRElrrSAAMVFQdpRSSLDP 98
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQ---SLGMCPQ--HNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAItepLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:TIGR01257 1017 HLTVAEHI---LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 179 DVSVRAQVLNLLndLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:TIGR01257 1093 DPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-187 |
1.41e-13 |
|
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: 70.32 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDsGTVRFRGTSLtDANAIRELRR 83
Cdd:TIGR01271 1217 QMDVQGLTAKY--TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSW-NSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDP-------RSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGldpesasrfpHEFSGGQRQRI 156
Cdd:TIGR01271 1293 AFGVIPQKVfifsgtfRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG----------YVLSNGHKQLM 1362
|
170 180 190
....*....|....*....|....*....|.
gi 488473195 157 AIARALVTEPDVLVADEPVSALDvSVRAQVL 187
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-242 |
2.01e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 11 HLHLGSSSGGTnaLDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMA-LRQPD-------SGTVRFRGTSLTDANAIRELR 82
Cdd:PRK13547 6 HLHVARRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 RSAAMVFQDPRS---SLDPRMSIGRaiteplrSPVARRTTRQQRKDR--LAKVMVDVGLDPeSASRFPHEFSGGQRQRIA 157
Cdd:PRK13547 84 LRAVLPQAAQPAfafSAREIVLLGR-------YPHARRAGALTHRDGeiAWQALALAGATA-LVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 158 IARAL---------VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVE 228
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|....
gi 488473195 229 RGKLADVYRdPQHV 242
Cdd:PRK13547 236 HGAPADVLT-PAHI 248
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-230 |
2.24e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsltdanairelrrSAAMVFQDP---RSSLDPRM 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQAwiqNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAITEPlrspvarrttRQQRKDRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:TIGR00957 720 LFGKALNEK----------YYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 177 ALDVSVRAQVL-NLLNDLVRERGLTMIFVSHDLGVVRHLcDTVAVMSVGRIVERG 230
Cdd:TIGR00957 790 AVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-238 |
3.18e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMA-LRQPDSGTVRFRGtsltdanairelrrSAAMVFQDP---RSSLDPR 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG--------------SVAYVPQVSwifNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAItEPLRSPVARRTTRQQRK-DRLAkvmvdvGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:PLN03232 699 ILFGSDF-ESERYWRAIDVTALQHDlDLLP------GRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 179 DVSVRAQVlnlLNDLVRE--RGLTMIFVSHDLGVVRhLCDTVAVMSVGRIVERGKLADVYRD 238
Cdd:PLN03232 772 DAHVAHQV---FDSCMKDelKGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-190 |
3.55e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 19 GGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIrelrrsAAMVFQDPRSSLDP 98
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA------EACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSigraITEPLRspvARRTTRQQRKDRLAKVMVDVGLDPESASRFpHEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:PRK13539 87 ALT----VAENLE---FWAAFLGGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|..
gi 488473195 179 DVSVRAQVLNLL 190
Cdd:PRK13539 159 DAAAVALFAELI 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-214 |
4.70e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 25 DGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSltdanaIRELRRS--AAMVFQDPRSSLDPRMSi 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP------IRRQRDEyhQDLLYLGHQPGIKTELT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 graITEPLR--SPVARRTTRQQRKDRLAKvmvdVGLdpesaSRF---P-HEFSGGQRQRIAIARALVTEPDVLVADEPVS 176
Cdd:PRK13538 91 ---ALENLRfyQRLHGPGDDEALWEALAQ----VGL-----AGFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488473195 177 ALDVSVRAQVLNLLNDLVrERGLTMIFVSH-DLGV----VRHL 214
Cdd:PRK13538 159 AIDKQGVARLEALLAQHA-EQGGMVILTTHqDLPVasdkVRKL 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-206 |
5.49e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMM--ALRQPDSGTVRFRGTSLTDANAIRElrrsaamvfqdprsSLDP 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAgaLKGTPVAGCVDVPDNQFGREASLID--------------AIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAIteplrspvarrttrqqrkdrlaKVMVDVGL-DPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:COG2401 109 KGDFKDAV----------------------ELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180
....*....|....*....|....*....
gi 488473195 178 LDVSVRAQVLNLLNDLVRERGLTMIFVSH 206
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-230 |
6.39e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHlhlgSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMAlrQPD----SGTVRFRGTSLTDANAIRE 80
Cdd:CHL00131 8 LEIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 81 LRRSAAMVFQDPrssldprMSI-GRAITEPLRSPV-ARRTTRQQRK-DRLA--KVMVD----VGLDPESASRFPHE-FSG 150
Cdd:CHL00131 82 AHLGIFLAFQYP-------IEIpGVSNADFLRLAYnSKRKFQGLPElDPLEflEIINEklklVGMDPSFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 151 GQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLC-DTVAVMSVGRIVER 229
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
.
gi 488473195 230 G 230
Cdd:CHL00131 234 G 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-220 |
9.39e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQR-----LGLVGGSGAGKSTLLKAMMALRQPDSGTVrfrGTSLTDANAIRELRRSAAMVFQDPRSSLDP 98
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKISYKPQYIKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSigraiTEPLRSPVARRTtrqqRKDRLAKVMVDvgldpesasrfphEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:PRK13409 427 DLG-----SSYYKSEIIKPL----QLERLLDKNVK-------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAV 220
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-228 |
1.06e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRRSAAMVFQDPRSS-LDPRMSIG-R 104
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRSTgIYAYLDIGfN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 105 AITEPLRS---PVARRTTRQQRKDrlAKVMVDvGLDPESASRFPH--EFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK10982 347 SLISNIRNyknKVGLLDNSRMKSD--TQWVID-SMRVKTPGHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473195 180 VSVRAQVLNLLNDLVRE-RGLTMIfvSHDLGVVRHLCDTVAVMSVGR---IVE 228
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKdKGIIII--SSEMPELLGITDRILVMSNGLvagIVD 474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
1.15e-12 |
|
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: 65.89 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHV-----NEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVrfrGTSLTDanairelrrsaaMVFQDPRSSLDP 98
Cdd:cd03237 10 LGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDT------------VSYKPQYIKADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIgRAItepLRSPVARRTTRQQRKDRLAKVMvdvGLDPESASRFPhEFSGGQRQRIAIARALVTEPDVLVADEPVSAL 178
Cdd:cd03237 75 EGTV-RDL---LSSITKDFYTHPYFKTEIAKPL---QIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488473195 179 DVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAV 220
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-206 |
2.54e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 7 VEDLHL-HLGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMmALRQPD-----------------SGTVRFR 68
Cdd:PLN03073 175 IKDIHMeNFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM-AMHAIDgipkncqilhveqevvgDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 69 GTSLTDANAIRELRRSAAMVFQ--DPRSSLDPRMSIGRAITEPLRSPVARRTTRQQRK----------DRLAKVMVDVGL 136
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVAQqrELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRlelidaytaeARAASILAGLSF 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 137 DPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVraqVLNLLNDLVRERGlTMIFVSH 206
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPK-TFIVVSH 399
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-235 |
2.68e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.84 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG-TSLTDANAirelrrsaamvfqdprsSLDPRMS 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISA-----------------GLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IGRAITEPLrspVARRTTRQQRKDRLAKVmvdvgLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVADEPVSA 177
Cdd:PRK13546 102 GIENIEFKM---LCMGFKRKEIKAMTPKI-----IEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 178 LDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-240 |
2.82e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGT-SLTDANaIRELRRSAAMVFQDP------------- 92
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDIN-LKWWRSKIGVVSQDPllfsnsiknniky 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 93 ----------------------RSSLDPRMSIgRAITEPLRSPVARRTTR----QQRKDRLA---KVMVDVG---LDPES 140
Cdd:PTZ00265 483 slyslkdlealsnyynedgndsQENKNKRNSC-RAKCAGDLNDMSNTTDSneliEMRKNYQTikdSEVVDVSkkvLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 141 ASRFPHEF-----------SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLG 209
Cdd:PTZ00265 562 VSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
250 260 270
....*....|....*....|....*....|.
gi 488473195 210 VVRHlCDTVAVMSvGRivERGKLADVYRDPQ 240
Cdd:PTZ00265 642 TIRY-ANTIFVLS-NR--ERGSTVDVDIIGE 668
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-240 |
3.51e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLkAMMALRQPDSGTVRFRGTSLTDANAiRELRRSAAMVFQDPRSSldPRMSIGRAI 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLL-ARMAGLLPGSGSIQFAGQPLEAWSA-AELARHRAYLSQQQTPP--FAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 107 TepLRSPVARRTtrQQRKDRLAKVMVDVGLDPEsASRFPHEFSGG--QRQRIA-----IARALVTEPDVLVADEPVSALD 179
Cdd:PRK03695 91 T--LHQPDKTRT--EAVASALNEVAEALGLDDK-LGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 180 VsvrAQVlNLLNDLVRE---RGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PRK03695 166 V---AQQ-AALDRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-220 |
5.55e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQ-----RLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFrgtsltdanairELRRSAAMVFQDPRSSLDP 98
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE------------DLKISYKPQYISPDYDGTV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 RMSIGRAITEPLRSP-----VARRTtrqqRKDRLAKVMVDvgldpesasrfphEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:COG1245 419 EEFLRSANTDDFGSSyykteIIKPL----GLEKLLDKNVK-------------DLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAV 220
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-240 |
7.50e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTdANAIRELRRSAAMVFQDP-------RSSL 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG-AYGLRELRRQFSMIPQDPvlfdgtvRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPRMSIGRAITEP------LRSPVARRTTrqqrkdrlakvmvdvGLDP---ESASrfphEFSGGQRQRIAIARALVTE-P 166
Cdd:PTZ00243 1405 DPFLEASSAEVWAalelvgLRERVASESE---------------GIDSrvlEGGS----NYSVGQRQLMCMARALLKKgS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 167 DVLVADEPVS----ALDVSVRAQVLNLLNdlvrerGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDPQ 240
Cdd:PTZ00243 1466 GFILMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-221 |
7.97e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 33 EGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTV-----------RFRGTSLtdANAIRELRRsaamvfQDPRSSLDPRM- 100
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTEL--QNYFKKLYN------GEIKVVHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 -SIGRAITEPLRSpVARRTTRQQRKDRLAKvmvDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:PRK13409 170 dLIPKVFKGKVRE-LLKKVDERGKLDEVVE---RLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488473195 180 VSVRAQVLNLLNDLVRERglTMIFVSHDLGVVRHLCDTVAVM 221
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-235 |
1.20e-11 |
|
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: 64.58 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRRSAAMVFQDP-------RSSL 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLHDLRFKITIIPQDPvlfsgslRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 97 DPrmsIGRAITEPLRSPVarrttrqqrkdRLAKVMVDV-----GLDPESASRfPHEFSGGQRQRIAIARALVTEPDVLVA 171
Cdd:TIGR00957 1381 DP---FSQYSDEEVWWAL-----------ELAHLKTFVsalpdKLDHECAEG-GENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 172 DEPVSALDVsvraQVLNLLNDLVRER--GLTMIFVSHDLGVVRHLCdTVAVMSVGRIVERGKLADV 235
Cdd:TIGR00957 1446 DEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-224 |
2.16e-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: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 15 GSSSggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTdaNAIRELRRSaaMVFQDPRS 94
Cdd:TIGR01257 1949 GTSS---PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TNISDVHQN--MGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 95 SLDPRMSiGRaitEPLRSPVARRTTRQQRKDRLAKVMV-DVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:TIGR01257 2022 AIDDLLT-GR---EHLYLYARLRGVPAEEIEKVANWSIqSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473195 174 PVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVG 224
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-221 |
2.25e-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: 63.26 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 33 EGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTV-----------RFRGTSLTDanairELRRSAAmvfQDPRSSLDPRM- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQD-----YFKKLAN---GEIKVAHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 -SIGRAITEPLRSpVARRTTRQQRKDRLAKvmvDVGLDPeSASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALD 179
Cdd:COG1245 170 dLIPKVFKGTVRE-LLEKVDERGKLDELAE---KLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488473195 180 VSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVM 221
Cdd:COG1245 245 IYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-202 |
7.04e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSssggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIREL-RR 83
Cdd:NF033858 2 ARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMvfqdPR---SSLDPRMSigraITEPLRSpVAR-----RTTRQQRKDRLAKvmvDVGLDPesasrFPH----EFSGG 151
Cdd:NF033858 78 IAYM----PQglgKNLYPTLS----VFENLDF-FGRlfgqdAAERRRRIDELLR---ATGLAP-----FADrpagKLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRER-GLTMI 202
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVL 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-231 |
7.91e-11 |
|
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: 61.87 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTsltdanairelrRSAAMVFQDPRssLDPRMSIG 103
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------------IKVGYLPQEPQ--LDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLRSPV----------ARRTTRQQRKDRLAKVM------------------VDVGLDpesASRFP------HEFS 149
Cdd:TIGR03719 87 ENVEEGVAEIKdaldrfneisAKYAEPDADFDKLAAEQaelqeiidaadawdldsqLEIAMD---ALRCPpwdadvTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 150 GGQRQRIAIARALVTEPDVLVADEPVSALDvsvrAQVLNLLNDLVRERGLTMIFVSHDlgvvRHLCDTVAvmsvGRIVE- 228
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD----RYFLDNVA----GWILEl 231
|
....
gi 488473195 229 -RGK 231
Cdd:TIGR03719 232 dRGR 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-187 |
9.38e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.64 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDsGTVRFRGTSLtDANAIRELRR 83
Cdd:cd03289 2 QMTVKDLTAKY--TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSW-NSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDP-------RSSLDPRMSIGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGldpesasrfpHEFSGGQRQRI 156
Cdd:cd03289 78 AFGVIPQKVfifsgtfRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGG----------CVLSHGHKQLM 147
|
170 180 190
....*....|....*....|....*....|.
gi 488473195 157 AIARALVTEPDVLVADEPVSALDvSVRAQVL 187
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLD-PITYQVI 177
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-207 |
1.36e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRG----------TSLTDANAI-------RELRRSAA 86
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqeTPALPQPALeyvidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 87 MVfQDPRSSLDprmsiGRAIT--EPLRSPVARRTTRQqrkdRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVT 164
Cdd:PRK10636 97 QL-HDANERND-----GHAIAtiHGKLDAIDAWTIRS----RAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488473195 165 EPDVLVADEPVSALDVSVraqVLNLLNDLVRERGlTMIFVSHD 207
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-207 |
1.68e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLhlhlgSSSGGTNAL-DGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGT-SLtdanairelr 82
Cdd:PRK11819 325 IEAENL-----SKSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKL---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 83 rsaAMVFQDpRSSLDPRMSIGRAITE------------PLRSPVAR---RTTRQQRKdrlakvmvdVGldpesasrfphE 147
Cdd:PRK11819 390 ---AYVDQS-RDALDPNKTVWEEISGgldiikvgnreiPSRAYVGRfnfKGGDQQKK---------VG-----------V 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473195 148 FSGGQRQRIAIARALVTEPDVLVADEPVSALDV-SVRAqvlnLLNDLVRERGLTMIfVSHD 207
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA----LEEALLEFPGCAVV-ISHD 501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-230 |
2.24e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPdsgtvrfrgtsLTDANAIreLRRSAAMVfqdPRSSLDPRMSIG 103
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----------RSDASVV--IRGTVAYV---PQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAIT-----EPLRSPVARRTTRQQRkdrlakvmvDVGLDP-----ESASRFPHeFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:PLN03130 697 DNILfgspfDPERYERAIDVTALQH---------DLDLLPggdltEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 174 PVSALDVSVRAQVLNllNDLVRE-RGLTMIFVSHDLGVVRHLcDTVAVMSVGRIVERG 230
Cdd:PLN03130 767 PLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-214 |
2.26e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFrgtsltdANAIReLRRSAAMVFQDPRSSLDPRMSIG 103
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------AKGIK-LGYFAQHQLEFLRADESPLQHLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RaiteplrspVARRTTRQQRKDRLAkvmvDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVR 183
Cdd:PRK10636 400 R---------LAPQELEQKLRDYLG----GFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190
....*....|....*....|....*....|.
gi 488473195 184 AQVLNLLNDLvrERGLtmIFVSHDlgvvRHL 214
Cdd:PRK10636 467 QALTEALIDF--EGAL--VVVSHD----RHL 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-206 |
2.34e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALR-QPDSGTV----RFRGTSLTdanaIRELRRSAAMVfqdprSS--- 95
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLtlfgRRRGSGET----IWDIKKHIGYV-----SSslh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 96 LDPRM--------------SIG--RAITEPLRSPVarrttrQQRKDRLakvmvdvGLDPESASRFPHEFSGGQrQRIA-I 158
Cdd:PRK10938 347 LDYRVstsvrnvilsgffdSIGiyQAVSDRQQKLA------QQWLDIL-------GIDKRTADAPFHSLSWGQ-QRLAlI 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 159 ARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSH 206
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
42-212 |
5.82e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 42 GSGAGKSTLLKammalrqpDSGTVRFRGTSLTDANaIRELRRSAAMVFQDP---RSSLDPRMSIGRAitEPLRSPVaRRT 118
Cdd:PTZ00265 1264 GGSGEDSTVFK--------NSGKILLDGVDICDYN-LKDLRNLFSIVSQEPmlfNMSIYENIKFGKE--DATREDV-KRA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 119 TRQQRKDRLAKVM---VDVGLDPESASrfpheFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVR 195
Cdd:PTZ00265 1332 CKFAAIDEFIESLpnkYDTNVGPYGKS-----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
170
....*....|....*..
gi 488473195 196 ERGLTMIFVSHDLGVVR 212
Cdd:PTZ00265 1407 KADKTIITIAHRIASIK 1423
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-230 |
8.75e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLhlgsSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLlKAMMALRQP---DSGTVRFRGTSLTDANAIREL 81
Cdd:PRK09580 2 LSIKDLHV----SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL-SATLAGREDyevTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 82 RRSAAMVFQDPRS--SLDPRMSIGRAITeplrspvARRTTRQQR-------KDRLAKVMVDVGLDPESASRFPHE-FSGG 151
Cdd:PRK09580 77 GEGIFMAFQYPVEipGVSNQFFLQTALN-------AVRSYRGQEpldrfdfQDLMEEKIALLKMPEDLLTRSVNVgFSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 152 QRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHL-CDTVAVMSVGRIVERG 230
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-207 |
1.26e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLGSSSggtNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaIRELRR 83
Cdd:PRK10522 322 TLELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ-PEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDprSSLDPRMsIGRAITEPLRSPVARRTTRQQRKDrlaKVMVDVG--LDPesasrfphEFSGGQRQRIAIARA 161
Cdd:PRK10522 398 LFSAVFTD--FHLFDQL-LGPEGKPANPALVEKWLERLKMAH---KLELEDGriSNL--------KLSKGQKKRLALLLA 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488473195 162 LVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHD 207
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-226 |
2.02e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 23 ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLtDANAIrELRRsaamvfqdprssldpR--- 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDI-ATRR---------------Rvgy 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MSIGRAITEPLrspvarrTTRQ--------------QRKDRLAKVMVDVGLDPESASRfPHEFSGGQRQRIAIARALVTE 165
Cdd:NF033858 344 MSQAFSLYGEL-------TVRQnlelharlfhlpaaEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 166 PDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTmIFVShdlgvvRHL------CDTVAVMSVGRI 226
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS------THFmneaerCDRISLMHAGRV 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-239 |
2.04e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRfrgtsltdanaireLRRSAAMVFQDPRssldprmsIG 103
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAW--------IM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAItepLRSPV----ARRTTRQQRKDRLAKVMVDV-----GLDPESASRFPHeFSGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:PTZ00243 734 NAT---VRGNIlffdEEDAARLADAVRVSQLEADLaqlggGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 175 VSALDVSVRAQVLNLLNdLVRERGLTMIFVSHDLGVVRHlCDTVAVMSVGRIVERGKLADVYRDP 239
Cdd:PTZ00243 810 LSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-187 |
2.99e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsltdanairelrrsaamvfqdpRSSLDPR 99
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------------RISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MS--IGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:TIGR01271 495 TSwiMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170
....*....|....
gi 488473195 174 PVSALDVSVRAQVL 187
Cdd:TIGR01271 575 PFTHLDVVTEKEIF 588
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-235 |
3.06e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 21 TNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSG--TVRFRGTSLTdanAIRELRRSAAMVFQDPRSSLdp 98
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFSHITRL---SFEQLQKLVSDEWQRNNTDM-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 99 rMSIGRAITEplrspvarRTTRQ---------QRKDRLAKVMvdvGLDPESASRFPHeFSGGQRQRIAIARALVTEPDVL 169
Cdd:PRK10938 91 -LSPGEDDTG--------RTTAEiiqdevkdpARCEQLAQQF---GITALLDRRFKY-LSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473195 170 VADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVERGKLADV 235
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-251 |
3.39e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLlkAM----MALRQPDSGTVRFRGTSL---TDANAIR-------ELRRSAAMVF 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL--AMsvfgRSYGRNISGTVFKDGKEVdvsTVSDAIDaglayvtEDRKGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 90 QDprssldprmSIGRAITEPLRSPVARRTT-------------RQQRKDRLAKVMVDVGldpesasrfphEFSGGQRQRI 156
Cdd:NF040905 354 ID---------DIKRNITLANLGKVSRRGVideneeikvaeeyRKKMNIKTPSVFQKVG-----------NLSGGNQQKV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 157 AIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRHLCDTVAVMSVGRIVerGKLadvy 236
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT--GEL---- 486
|
250
....*....|....*.
gi 488473195 237 rdPQHVVTQE-LLRAI 251
Cdd:NF040905 487 --PREEASQErIMRLI 500
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-206 |
1.02e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANAIRELRrsaaMVFQDPRSSLDPRMSIG 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ----LCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAITEPLR-SPVARRTTRQQRKDRLAKVM-VDVGLdpesasrfpheFSGGQRQRIAIARALVTEPDVLVADEPVSALDVS 181
Cdd:PRK13540 93 ENCLYDIHfSPGAVGITELCRLFSLEHLIdYPCGL-----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 488473195 182 VRAQVLNLLNDLvRERGLTMIFVSH 206
Cdd:PRK13540 162 SLLTIITKIQEH-RAKGGAVLLTSH 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-218 |
1.65e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 27 VSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVrfrgtSLTDANAIRELRRS---------------------A 85
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDPNERLGKLRQDqfafeeftvldtvimghtelwE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 86 AMVFQDPRSSLdPRMS--IGRAITEpLRSPVARRT--TRQQRKDRLakvMVDVGLDPESASRFPHEFSGGQRQRIAIARA 161
Cdd:PRK15064 95 VKQERDRIYAL-PEMSeeDGMKVAD-LEVKFAEMDgyTAEARAGEL---LLGVGIPEEQHYGLMSEVAPGWKLRVLLAQA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 162 LVTEPDVLVADEPVSALDV-SVR--AQVLNllndlvrERGLTMIFVSHDlgvvRHLCDTV 218
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDInTIRwlEDVLN-------ERNSTMIIISHD----RHFLNSV 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-228 |
1.65e-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: 54.80 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLHLHLGSSSGGTN-ALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANaiRELRR 83
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN--REAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 ---SAamVFQD---------PRSSLDPrmsigRAITEPLRspvarrttrqqrkdRLA---KVMVDVGldpesasRF-PHE 147
Cdd:COG4615 406 qlfSA--VFSDfhlfdrllgLDGEADP-----ARARELLE--------------RLEldhKVSVEDG-------RFsTTD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 148 FSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRA----QVLNLLndlvRERGLTMIFVSHDlgvVR--HLCDTVAVM 221
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRvfytELLPEL----KARGKTVIAISHD---DRyfDLADRVLKM 530
|
....*..
gi 488473195 222 SVGRIVE 228
Cdd:COG4615 531 DYGKLVE 537
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-202 |
1.77e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKaMMALRQpDSGTVrfRGTSLTDANAIRE-LRRSAAMVFQdprssldprmsi 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLAGRK-TAGVI--TGEILINGRPLDKnFQRSTGYVEQ------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 graiteplrspvarrttrqqrkdrlakvmVDVgLDPESASRFPHEFSG-------GQRQRIAIARALVTEPDVLVADEPV 175
Cdd:cd03232 87 -----------------------------QDV-HSPNLTVREALRFSAllrglsvEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180
....*....|....*....|....*..
gi 488473195 176 SALDVSVRAQVLNLLNDLVRErGLTMI 202
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADS-GQAIL 162
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-207 |
2.03e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 5 IEVEDLhlhlGSSSGGTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFrgtslTDANAIRELRRS 84
Cdd:PRK15064 320 LEVENL----TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----SENANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 85 AAMVFQDPRSSLDpRMSIGRAITE---PLRSPVARRTTRQQRKDRLAKVMvdvgldpesasrfphefSGGQRQRIAIARA 161
Cdd:PRK15064 391 HAYDFENDLTLFD-WMSQWRQEGDdeqAVRGTLGRLLFSQDDIKKSVKVL-----------------SGGEKGRMLFGKL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488473195 162 LVTEPDVLVADEPVSALDV-SVRAqvLNllNDLVRERGlTMIFVSHD 207
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMeSIES--LN--MALEKYEG-TLIFVSHD 494
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-227 |
2.08e-08 |
|
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: 53.04 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD---SGTVRFRGtsLTDANAIRELRRSAAMVFQDprSSLDPRM 100
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYPGEIIYVSEE--DVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 101 SIGRAIteplrspvarRTTRQQRKDRLAKVmvdvgldpesasrfpheFSGGQRQRIAIARALVTEPDVLVADEPVSALDV 180
Cdd:cd03233 99 TVRETL----------DFALRCKGNEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473195 181 SVRAQVLNLLNDLVRERGLT-MIFVSHDLGVVRHLCDTVAVMSVGRIV 227
Cdd:cd03233 152 STALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-186 |
3.28e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.32 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 20 GTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGtsltdanairelrrsaamvfqdpRSSLDPR 99
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 100 MS--IGRAITEPLRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRFPHE----FSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:cd03291 106 FSwiMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|...
gi 488473195 174 PVSALDVSVRAQV 186
Cdd:cd03291 186 PFGYLDVFTEKEI 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-232 |
9.38e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 24 LDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFR-GTSLtdanairelrrsaAMVFQDPRssLDPRMSI 102
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-------------GYLPQEPQ--LDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 103 GRAITEPlrspVARRTTRQQR--------------KDRLAKVMVDV--------GLDPES-------ASRFPH------E 147
Cdd:PRK11819 88 RENVEEG----VAEVKAALDRfneiyaayaepdadFDALAAEQGELqeiidaadAWDLDSqleiamdALRCPPwdakvtK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 148 FSGGQRQRIAIARALVTEPDVLVADEPVSALDvsvrAQ-VLNLLNDLVRERGlTMIFVSHDlgvvRHLCDTVAvmsvGRI 226
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPG-TVVAVTHD----RYFLDNVA----GWI 230
|
....*...
gi 488473195 227 VE--RGKL 232
Cdd:PRK11819 231 LEldRGRG 238
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-228 |
1.18e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.45 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 4 QIEVEDLHLHLGSSSggTNALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDAnAIRELRR 83
Cdd:cd03288 19 EIKIHDLCVRYENNL--KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 84 SAAMVFQDP-------RSSLDPRmsigraiteplrspvarrttRQQRKDRL--------AKVMVDV---GLDPeSASRFP 145
Cdd:cd03288 96 RLSIILQDPilfsgsiRFNLDPE--------------------CKCTDDRLwealeiaqLKNMVKSlpgGLDA-VVTEGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 146 HEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRaqvlNLLNDLVRE--RGLTMIFVSHDLGVVRHlCDTVAVMSV 223
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKVVMTafADRTVVTIAHRVSTILD-ADLVLVLSR 229
|
....*
gi 488473195 224 GRIVE 228
Cdd:cd03288 230 GILVE 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-194 |
2.53e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 30 HVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFRGTSLTDANairelrRSAAMVFQDPRSSLDPRMSIgraiTEP 109
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD------RSRFMAYLGHLPGLKADLST----LEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 110 LRSPVARRTTRQQRKDRLAKVMVDVGLDPESASRfphEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVsvraQVLNL 189
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITL 175
|
....*
gi 488473195 190 LNDLV 194
Cdd:PRK13543 176 VNRMI 180
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-220 |
2.58e-07 |
|
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: 49.49 E-value: 2.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473195 147 EFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVRERGLTMIFVSHDLGVVRHLCDTVAV 220
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-212 |
3.43e-07 |
|
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: 48.52 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 34 GQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVRFrgtslTDANAIRElrrsaamvfqdprssldprmsigraiteplrsp 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----IDGEDILE--------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 114 varrttrqqrkdrlakvMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDL 193
Cdd:smart00382 44 -----------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
170 180
....*....|....*....|....
gi 488473195 194 V-----RERGLTMIFVSHDLGVVR 212
Cdd:smart00382 107 LllllkSEKNLTVILTTNDEKDLG 130
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-226 |
9.12e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 36 RLGLVGGSGAGKSTLLKAMMALRQPDSGTVrfrgtsltdanaIRELRRSAAMVFQDPRSSLD----PRMSIGRAITEPLr 111
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTV------------FRSAKVRMAVFSQHHVDGLDlssnPLLYMMRCFPGVP- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 112 spvarrttrqqrKDRLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTEPDVLVADEPVSALDV-SVRAQVLNLl 190
Cdd:PLN03073 604 ------------EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGL- 670
|
170 180 190
....*....|....*....|....*....|....*.
gi 488473195 191 ndLVRERGLTMifVSHDLGVVRHLCDTVAVMSVGRI 226
Cdd:PLN03073 671 --VLFQGGVLM--VSHDEHLISGSVDELWVVSEGKV 702
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
60-247 |
1.46e-06 |
|
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: 48.86 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 60 PDSGTVRFRGTSLTDANAIrELRRSAAMVFQdprSSLDPRmsiGRAITEPLRspvarrttrQQRKDRLaKVMVDVGLDPE 139
Cdd:TIGR00630 418 PEALAVTVGGKSIADVSEL-SIREAHEFFNQ---LTLTPE---EKKIAEEVL---------KEIRERL-GFLIDVGLDYL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 140 SASRFPHEFSGGQRQRIAIARALVTE-PDVL-VADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHDLGVVRHlCDT 217
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADY 558
|
170 180 190
....*....|....*....|....*....|....*.
gi 488473195 218 VAVMSV------GRIVERGKLADVYRDPQHVVTQEL 247
Cdd:TIGR00630 559 VIDIGPgagehgGEVVASGTPEEILANPDSLTGQYL 594
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-230 |
4.72e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 22 NALDGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMAlrqpDSGTVRFRGTSltdanairelrrsaamvfqdPRSSLDPRMS 101
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISFL--------------------PKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 102 IgraiteplrspvarrttrqqrkDRLaKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALV--TEPDVLVADEPVSALD 179
Cdd:cd03238 65 I----------------------DQL-QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473195 180 VSVRAQVLNLLNDLVRErGLTMIFVSHDLGVVRhLCDTVAVM------SVGRIVERG 230
Cdd:cd03238 122 QQDINQLLEVIKGLIDL-GNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
41-213 |
8.33e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 41 GGSGAGKSTL----LKAMMALRQPDSGTVRFR----GTSLTDANAIRELrrSAAMVFQDPRSSLDPRMSIGrAITE---P 109
Cdd:cd03270 28 GVSGSGKSSLafdtIYAEGQRRYVESLSAYARqflgQMDKPDVDSIEGL--SPAIAIDQKTTSRNPRSTVG-TVTEiydY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 110 LRSPVARRTTRQqrkdRLaKVMVDVGLDPESASRFPHEFSGGQRQRIAIARALVTE-PDVL-VADEPVSALDVSVRAQVL 187
Cdd:cd03270 105 LRLLFARVGIRE----RL-GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLI 179
|
170 180
....*....|....*....|....*.
gi 488473195 188 NLLNDLvRERGLTMIFVSHDLGVVRH 213
Cdd:cd03270 180 ETLKRL-RDLGNTVLVVEHDEDTIRA 204
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-212 |
1.18e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 126 RLAKVMVDVGLDPESASRFPHEFSGGQRQRIAIARAL---VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMI 202
Cdd:cd03271 148 RKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVV 226
|
90
....*....|
gi 488473195 203 FVSHDLGVVR 212
Cdd:cd03271 227 VIEHNLDVIK 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-206 |
2.81e-05 |
|
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: 45.12 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 28 SLHVNEGQRLGLVGGSGAGKSTLLKAMMALrQPdsgtvrFRGTSLTdanaireLRRSAAMVFQDPRssldPRMSIGrait 107
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGEL-WP------VYGGRLT-------KPAKGKLFYVPQR----PYMTLG---- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 108 ePLRSPVARRTTRQQRKDR------LAKVMVDVGLDP--------ESASRFPHEFSGGQRQRIAIARALVTEPDVLVADE 173
Cdd:TIGR00954 530 -TLRDQIIYPDSSEDMKRRglsdkdLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 488473195 174 PVSALDVSVRAQVLNLLndlvRERGLTMIFVSH 206
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
20-56 |
3.34e-05 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 44.09 E-value: 3.34e-05
10 20 30
....*....|....*....|....*....|....*..
gi 488473195 20 GTNALDGVsLHVNEGQRLGLVGGSGAGKSTLLkAMMA 56
Cdd:cd01136 54 GVRAIDGL-LTCGEGQRIGIFAGSGVGKSTLL-GMIA 88
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
23-56 |
4.46e-05 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 44.25 E-value: 4.46e-05
10 20 30
....*....|....*....|....*....|....
gi 488473195 23 ALDGVsLHVNEGQRLGLVGGSGAGKSTLLkAMMA 56
Cdd:COG1157 147 AIDGL-LTVGRGQRIGIFAGSGVGKSTLL-GMIA 178
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-231 |
7.48e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 31 VNEGQRLGLVGGSGAGKSTLLKAMMA----LRQPDSGTVRFRGTSLTDanaIRELRRsAAMVFQdprSSLD---PRMSIG 103
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEE---IKKHYR-GDVVYN---AETDvhfPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 104 RAI--TEPLRSPVAR--RTTRQQRKDRLAKV-MVDVGLDPESASRFPHEF----SGGQRQRIAIARALVTEPDVLVADEP 174
Cdd:TIGR00956 157 ETLdfAARCKTPQNRpdGVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473195 175 VSALDVSVRAQVLNLLNDLVRERGLTmIFV-----SHDlgvVRHLCDTVAVMSVGRIVERGK 231
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANILDTT-PLVaiyqcSQD---AYELFDKVIVLYEGYQIYFGP 294
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-212 |
1.65e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 129 KVMVDVGLDPESASRFPHEFSGGQRQRIAIARAL---VTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVS 205
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIE 889
|
....*..
gi 488473195 206 HDLGVVR 212
Cdd:TIGR00630 890 HNLDVIK 896
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
20-56 |
2.55e-04 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 42.02 E-value: 2.55e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488473195 20 GTNALDGVsLHVNEGQRLGLVGGSGAGKSTLLkAMMA 56
Cdd:PRK07721 145 GVRAIDSL-LTVGKGQRVGIFAGSGVGKSTLM-GMIA 179
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-67 |
2.56e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.35 E-value: 2.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488473195 25 DGVSLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPdSGTVRF 67
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARF 54
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
66-207 |
4.90e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 66 RFRGTSLTD-ANAIRELRRSAAMvFQdpRSSLDPRMSIGRAITEPLRSPvarRTTRQQRKDRLAkVMVDVGLDPESASRF 144
Cdd:PRK00635 401 RCQGTGLGDyANAATWHGKTFAE-FQ--QMSLQELFIFLSQLPSKSLSI---EEVLQGLKSRLS-ILIDLGLPYLTPERA 473
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473195 145 PHEFSGGQRQRIAIARALVTEPD--VLVADEPVSALDVSVRAQVLNLLNDLvRERGLTMIFVSHD 207
Cdd:PRK00635 474 LATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD 537
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
225-254 |
8.37e-04 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 37.34 E-value: 8.37e-04
10 20 30
....*....|....*....|....*....|
gi 488473195 225 RIVERGKLADVYRDPQHVVTQELLRAIPRI 254
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTI 30
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-214 |
1.28e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 39 LVGGSGAGKSTLLKAM-MALrqpdSGTVRFRGTSLT-DANAIRELRRSAA--MVFqdpRSSLDPRMSIGRAItEPLRSPV 114
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYAL----TGELPPNSKGGAhDPKLIREGEVRAQvkLAF---ENANGKKYTITRSL-AILENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 115 arrTTRQQRKDRLAKVMVDvgldpesasrfphEFSGGQRQ------RIAIARALVTEPDVLVADEPVSALDV-SVRAQVL 187
Cdd:cd03240 99 ---FCHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLA 162
|
170 180
....*....|....*....|....*..
gi 488473195 188 NLLNDLVRERGLTMIFVSHDLGVVRHL 214
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
227-255 |
1.51e-03 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 36.22 E-value: 1.51e-03
10 20
....*....|....*....|....*....
gi 488473195 227 VERGKLADVYRDPQHVVTQELLRAIPRIR 255
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLD 29
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
34-56 |
2.46e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 38.83 E-value: 2.46e-03
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
20-55 |
3.02e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 38.53 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|....*.
gi 488473195 20 GTNALDGVsLHVNEGQRLGLVGGSGAGKSTLLkAMM 55
Cdd:PRK08972 149 GVRAINAM-LTVGKGQRMGLFAGSGVGKSVLL-GMM 182
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
21-66 |
3.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 3.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488473195 21 TNALDGVSL-----HVNEGQRLGLVGGSGAGKSTLLKAMMALRQPDSGTVR 66
Cdd:PRK01889 177 VSALDGEGLdvlaaWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
149-206 |
3.64e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 3.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473195 149 SGGQRQRIAIARALVTEPDVLVADEPVSALDVSVRAQVLNLLNDLVrERGLTMIFVSH 206
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
22-61 |
4.11e-03 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 38.23 E-value: 4.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488473195 22 NALdgvsLHVNEGQRLGLVGGSGAGKSTLLKAMMALRQPD 61
Cdd:PRK07960 167 NAL----LTVGRGQRMGLFAGSGVGKSVLLGMMARYTQAD 202
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
33-87 |
6.55e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 36.95 E-value: 6.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473195 33 EGQRLGLVGGSGAGKSTLLkAMMAlRQPDSGTVRF-----RGTSLtdANAIRELRRSAAM 87
Cdd:pfam00006 13 RGQRIGIFGGSGVGKTVLA-GMIA-RQASADVVVYaligeRGREV--REFIEELLGSGAL 68
|
|
| |
