|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-228 |
1.50e-100 |
|
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: 292.09 E-value: 1.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALR 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDPYASLHPLHRIRRSLREPRQINGLPFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPK 162
Cdd:COG1124 79 RRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 163 LLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDRA 228
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-221 |
4.07e-80 |
|
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: 239.72 E-value: 4.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTGALR 82
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDPYASLHPLHRIRRSLREPRQINGLPFDEASL----MASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkeavLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-221 |
4.75e-76 |
|
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: 238.26 E-value: 4.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFK-RGPSHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTG 79
Cdd:COG1123 261 LEVRNLSKRYPvRGKGGVRAV--DDvsLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQDPYASLHPLHRIRRSLREPRQINGLpFDEASLMASV----EQVGLPGNILDRYPHQLSGGQRQRVAIVR 155
Cdd:COG1123 339 ELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGL-LSRAERRERVaellERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-212 |
3.48e-70 |
|
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: 217.61 E-value: 3.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDW---QGEVQVLGQPLNA--QKA 76
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAV--DGvsFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlsEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 77 FTGALRQQVQMVFQDPYASLHPLHRIRRSLREPRQINGlPFDEASLMASV----EQVGLPG--NILDRYPHQLSGGQRQR 150
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHG-GLSKAEARERAiellERVGLPDpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDR 212
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-221 |
8.85e-65 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 209.54 E-value: 8.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDwQGEVQVLGQPLNA--QKAFTgALRQQVQMVFQ 90
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGlsRRALR-PLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYASLHPLHRIRRSLREPRQINGLPFDEASLMASV----EQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLL 166
Cdd:COG4172 370 DPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVaealEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 167 DEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-212 |
9.83e-65 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 203.81 E-value: 9.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRGPSHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTGALRQQVQMVF 89
Cdd:COG4608 24 FGRTVGVVKAV--DGvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItGLSGRELRPLRRRMQMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QDPYASLHPLHRIRRSLREPRQINGLpFDEASLMASV----EQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:COG4608 102 QDPYASLNPRMTVGDIIAEPLRIHGL-ASKAERRERVaellELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDR 212
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDR 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
5.53e-55 |
|
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: 183.57 E-value: 5.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAV-DINHLTVTFKRGPSHfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRD---WQGEVQVLGQPLNAQKA 76
Cdd:COG1123 1 MTPLlEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 77 ftGALRQQVQMVFQDPYASLHPLhRIRRSLREPRQINGLPFDEASLMA--SVEQVGLPGnILDRYPHQLSGGQRQRVAIV 154
Cdd:COG1123 79 --ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARARVleLLEAVGLER-RLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 155 RALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-221 |
3.31e-53 |
|
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: 179.11 E-value: 3.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKS----TLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGA 80
Cdd:COG4172 8 SVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE--RE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQ----QVQMVFQDPYASLHPLHRIRRSLREP-RQINGLPFDEASLMAS--VEQVGL--PGNILDRYPHQLSGGQRQRV 151
Cdd:COG4172 86 LRRirgnRIAMIFQEPMTSLNPLHTIGKQIAEVlRLHRGLSGAAARARALelLERVGIpdPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
8.84e-51 |
|
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: 164.81 E-value: 8.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPshfNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqKAFTGAL 81
Cdd:COG1122 1 IELENLSFSYPGGT---PAL--DDvsLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDPYASLhplhrIRRSLRE-----PRQInGLPFDEAS--LMASVEQVGLPGnILDRYPHQLSGGQRQRVAI- 153
Cdd:COG1122 74 RRKVGLVFQNPDDQL-----FAPTVEEdvafgPENL-GLPREEIRerVEEALELVGLEH-LADRPPHELSGGQKQRVAIa 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 154 ----------VralqlnpklllLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1122 147 gvlamepevlV-----------LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-221 |
9.05e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 163.70 E-value: 9.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALRQQVQMVFQDPYASLHPLHRIRRSL 106
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDSISAVNPRKTVREII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REP-RQINGLpfDEASLMASV----EQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEI 181
Cdd:PRK10419 113 REPlRHLLSL--DKAERLARAsemlRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520926077 182 LNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10419 191 IRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
2.72e-49 |
|
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: 160.73 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTGAL 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDPYasLHPlhriRRSLRE----PRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVR 155
Cdd:cd03255 81 RRHIGFVFQSFN--LLP----DLTALEnvelPLLLAGVPKKERRERAEelLERVGL-GDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNtVAHLCDRALLINQGRV 221
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-229 |
5.47e-49 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 163.34 E-value: 5.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTFK---------RGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQK 75
Cdd:PRK15079 10 EVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 76 AFT-GALRQQVQMVFQDPYASLHPLHRIRRSLREPRQINGLPFDEASLMASVE----QVGLPGNILDRYPHQLSGGQRQR 150
Cdd:PRK15079 90 DDEwRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKammlKVGLLPNLINRYPHEFSGGQCQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VERHLDRAV 229
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHaVELGTYDEV 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-221 |
8.04e-49 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 162.83 E-value: 8.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 15 RGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQP-LNAQKAFTGALRQQVQMVFQDPY 93
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDlLKADPEAQKLLRQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 94 ASLHPLHRIRRSLREPRQIN-GLPFDE--ASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:PRK11308 103 GSLNPRKKVGQILEEPLLINtSLSAAErrEKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 171 SALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
2.04e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.67 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAV-DINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAF 77
Cdd:COG1136 1 MSPLlELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 78 TGALRQQVQMVFQDPYasLHPlhriRRSLRE----PRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRV 151
Cdd:COG1136 81 ARLRRRHIGFVFQFFN--LLP----ELTALEnvalPLLLAGVSRKERRERARelLERVGL-GDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNtVAHLCDRALLINQGRVER 223
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-221 |
6.29e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.90 E-value: 6.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgALRQQVQMVFQDPYAslhPLHRIRRSLR 107
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP--EWRRQVAYVPQEPAL---WGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:COG4619 96 FPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLRE 175
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 188 LRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4619 176 YLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-222 |
9.67e-48 |
|
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: 157.36 E-value: 9.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALR 82
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQ--DPYASL-------HPL--HRIRRSLREpRQINGLpfdeaslmasVEQVGLPGNIlDRYPHQLSGGQRQRV 151
Cdd:cd03258 82 RRIGMIFQhfNLLSSRtvfenvaLPLeiAGVPKAEIE-ERVLEL----------LELVGLEDKA-DAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-221 |
3.28e-47 |
|
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: 156.89 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQK-AFTGALRQQVQMVFQDPYASLHPLHRIRRSL 106
Cdd:TIGR02769 32 LSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrKQRRAFRRDVQLVFQDSPSAVNPRMTVRQII 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REP-RQINGLPFDE--ASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:TIGR02769 112 GEPlRHLTSLDESEqkARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILE 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR02769 192 LLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-236 |
6.83e-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: 156.03 E-value: 6.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 9 LTVTFKRGPSHFnALEMDgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL--NAQKAFTGALRQQVQ 86
Cdd:COG4148 3 LEVDFRLRRGGF-TLDVD-FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 87 MVFQDpyASLHPLHRIRRSL-----REPRQINGLPFDEAslmasVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:COG4148 81 YVFQE--ARLFPHLSVRGNLlygrkRAPRAERRISFDEV-----VELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH------LDRAVLGELAG 235
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASgplaevLSRPDLLPLAG 232
|
.
gi 520926077 236 G 236
Cdd:COG4148 233 G 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
7.46e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.62 E-value: 7.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkaFTG-- 79
Cdd:COG1135 2 IELENLSKTFPTKGGPVTAL--DDvsLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA---LSEre 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 --ALRQQVQMVFQdpyaslHP--LHRirRSLRE----PRQINGLPFDE-----ASLMasvEQVGLPGNIlDRYPHQLSGG 146
Cdd:COG1135 77 lrAARRKIGMIFQ------HFnlLSS--RTVAEnvalPLEIAGVPKAEirkrvAELL---ELVGLSDKA-DAYPSQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
28-221 |
1.00e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.46 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVFQDpyASLHPlHRirrSLR 107
Cdd:COG1126 22 LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGMVFQQ--FNLFP-HL---TVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 E-----PRQINGLPFDEASL--MASVEQVGLPGNIlDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD--MTvq 178
Cdd:COG1126 96 EnvtlaPIKVKKMSKAEAEEraMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeLV-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1126 173 GEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-221 |
2.30e-45 |
|
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: 150.70 E-value: 2.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGalrq 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 qvqMVFQDPyaSLHPLHRIRRSLREPRQINGLPFDEAS--LMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03293 77 ---YVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARerAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQ--GRV 221
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-220 |
2.72e-45 |
|
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: 150.31 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgALRQQVQMVFQ 90
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK--ELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYASLhplhrIRRSLRE-----PRQiNGLPFDEAS--LMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:cd03225 83 NPDDQF-----FGPTVEEevafgLEN-LGLPEEEIEerVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
3.32e-45 |
|
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: 148.87 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKrgpsHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQ 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPyaslhplhrirrslreprqinGLPfdeaSLMASVEQVGLPgnildryphqLSGGQRQRVAIVRALQLNPKL 163
Cdd:cd03229 77 RIGMVFQDF---------------------ALF----PHLTVLENIALG----------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
3.96e-45 |
|
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: 151.84 E-value: 3.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRG-PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG-ALRQ 83
Cdd:TIGR04521 3 LKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPYASLHplhrirrslrE----------PRQInGLPFDEASLMA--SVEQVGLPGNILDRYPHQLSGGQRQRV 151
Cdd:TIGR04521 83 KVGLVFQFPEHQLF----------EetvykdiafgPKNL-GLSEEEAEERVkeALELVGLDEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
28-221 |
1.54e-44 |
|
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: 148.45 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVFQ--DPYASLHPLHRIRRS 105
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMVFQqfNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 lrePRQINGLPFDEA--SLMASVEQVGLPGNIlDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:cd03262 101 ---PIKVKGMSKAEAeeRALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03262 177 VMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-222 |
3.63e-43 |
|
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: 145.72 E-value: 3.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTGALRQQVQMVFQDP--YASLHPLHRIRR 104
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsGLSEAELYRLRRRMGMLFQSGalFDSLTVFENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLREPRQINGLPFDEASLMAsVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNL 184
Cdd:cd03261 101 PLREHTRLSEEEIREIVLEK-LEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDL 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 185 LQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03261 179 IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
7.46e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRgpshFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgAL 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTAL--DGvsLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA---EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDPyaSLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQL 159
Cdd:COG1131 72 RRRIGYVPQEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDelLELFGLTD-AADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
28-221 |
9.57e-43 |
|
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: 144.74 E-value: 9.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTgALRQQVQMVFQDP--YASLhplhrir 103
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsEKELY-ELRRRIGMLFQGGalFDSL------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 rSLRE----P-RQINGLPFDEASLMAS--VEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD-- 174
Cdd:COG1127 98 -TVFEnvafPlREHTDLSEAEIRELVLekLELVGLPG-AADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpi 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 175 MTvqAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1127 176 TS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
4.37e-42 |
|
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: 142.27 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkAFTGALRQ 83
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPyaSLHPLHRIRRSLREPRQINGLPFDE--ASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03259 73 NIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEirARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-226 |
7.78e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.92 E-value: 7.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALE-MDgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG 79
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDdVS-LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 alrqqvqMVFQDPyaSLHPLHRIRRSLREPRQINGLPFDEAS--LMASVEQVGLPGNiLDRYPHQLSGGQRQRVAIVRAL 157
Cdd:COG1116 84 -------VVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRerARELLELVGLAGF-EDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 158 QLNPKLLLLDEPTSALD-MTvqAEILN-LLQALRRDTGMTMILVSHDMNTVAHLCDRALLI--NQGRVERHLD 226
Cdd:COG1116 154 ANDPEVLLMDEPFGALDaLT--RERLQdELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
28-221 |
1.10e-41 |
|
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: 142.49 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGALRQQVQMVFQDPYASL----------- 96
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR--RELARRIAYVPQEPPAPFgltvrelvalg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 -HPLHRIRRSLREPrqinglpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:COG1120 100 rYPHLGLFGRPSAE--------DREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 176 TVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
1.38e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDP-----------YASLHPLHRIRRSLREprqinglpfdeaSLMASVEQVGLpGNILDRYPHQLSGGQRQ 149
Cdd:COG1121 80 VPQRAEVDWDFPitvrdvvlmgrYGRRGLFRRPSRADRE------------AVDEALERVGL-EDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 150 RVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-223 |
1.46e-41 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 141.35 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKST----LLRVLAGLQRDWQGEVQVLGQPLNAQkaftgALRQ-QVQMVFQDPYASLHPLHRI 102
Cdd:TIGR02770 7 LSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPL-----SIRGrHIATIMQNPRTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 103 RRSLREPRQINGLPFDEAS--LMASVEQVGLPG--NILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARalILEALEAVGLPDpeEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 179 AEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VER 223
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRiVER 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-221 |
4.08e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 4.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNAlemdGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQqVQMVFQ 90
Cdd:COG3840 7 LTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERP-VSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 D----PYAS--------LHPlhrirrSLREPRQinglpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:COG3840 79 EnnlfPHLTvaqniglgLRP------GLKLTAE------QRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-221 |
4.82e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 144.08 E-value: 4.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKST----LLRVLAGlqrdwQGEVQVLGQPL---NAQKAFtgALRQQV 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLhnlNRRQLL--PVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQDPYASLHP----LHRIRRSLREPRQINGLPFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:PRK15134 365 QVVFQDPNSSLNPrlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-230 |
6.33e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 138.05 E-value: 6.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSA-VDINHLTVTFKR-----GPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN-- 72
Cdd:COG4167 1 MSAlLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 73 --AQKAftgalrQQVQMVFQDPYASLHPLHRIRRSLREPRQINGLpFDEAS----LMASVEQVGLPGNILDRYPHQLSGG 146
Cdd:COG4167 81 dyKYRC------KHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTD-LTAEEreerIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VERHL 225
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEvVEYGK 233
|
....*
gi 520926077 226 DRAVL 230
Cdd:COG4167 234 TAEVF 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
28-221 |
6.96e-40 |
|
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: 135.26 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGALRQQVQMVFQdpyaslhplhrirrslr 107
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP--KELARKIAYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqinglpfdeaslmaSVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:cd03214 81 -----------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 188 LRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03214 143 LARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-222 |
2.71e-39 |
|
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: 135.64 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA----QKAf 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 78 tgALR-QQVQMVFQdpyaSLH-------------PLHriRRSLREPRQinglpfdEAslMASVEQVGLpGNILDRYPHQL 143
Cdd:COG4181 86 --RLRaRHVGFVFQ----SFQllptltalenvmlPLE--LAGRRDARA-------RA--RALLERVGL-GHRLDHYPAQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 144 SGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNtVAHLCDRALLINQGRVE 222
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLV 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-222 |
2.86e-39 |
|
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: 138.71 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN--AQKAFTGALRQQVQMVFQDpyASLHPLHRIRRS 105
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsRKGIFLPPEKRRIGYVFQE--ARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLL 185
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 520926077 186 QALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
5.56e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.26 E-value: 5.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKrGPSHFNALEmdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQV------LGQPLNAQ 74
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 75 KAFTGALRQQVQMVFQDpyASLHPlHR--IRRSLREPRQINGLPFDEASLMAS--VEQVGLPGNiLDRYPHQLSGGQRQR 150
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQN--FNLFP-HRtvLENIIEGPVIVKGEPKEEATARARelLAKVGLAGK-ETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-236 |
9.99e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 9.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFkrgPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQK-AFTGA 80
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDPY---------ASLHP-LHRIR--RSLReprqiNGLPFDEASL-MASVEQVGLPGNILDRyPHQLSGGQ 147
Cdd:COG3638 78 LRRRIGMIFQQFNlvprlsvltNVLAGrLGRTStwRSLL-----GLFPPEDRERaLEALERVGLADKAYQR-ADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 148 RQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE----- 222
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVfdgpp 231
|
250
....*....|....
gi 520926077 223 RHLDRAVLGELAGG 236
Cdd:COG3638 232 AELTDAVLREIYGG 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-221 |
1.25e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.06 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALE-MDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQM 87
Cdd:PRK09493 2 IEFKNVSKHFGPTQvLHNidLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 88 VFQDPYasLHP-LHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLL 164
Cdd:PRK09493 82 VFQQFY--LFPhLTALENVMFGPLRVRGASKEEAEKQARelLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 165 LLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-230 |
1.45e-38 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 140.23 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKS-TLLRVLAGLQRD----WQGEVQVLGQP-LNAQKAFT 78
Cdd:PRK15134 7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESlLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 GALR-QQVQMVFQDPYASLHPLHRIRRSLREPRQIN-GLPFDEA--SLMASVEQVGL--PGNILDRYPHQLSGGQRQRVA 152
Cdd:PRK15134 87 RGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRREAArgEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 153 IVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VERHLDRAVL 230
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQNRAATLF 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-220 |
6.26e-38 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 134.85 E-value: 6.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDwQGEV---------QVLGQP- 70
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIggsatfngrEILNLPe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 71 --LNAQKAftgalrQQVQMVFQDPYASLHPLHRIRRSLREPRQIN-GL----PFDEASLMasVEQVGLPG--NILDRYPH 141
Cdd:PRK09473 89 keLNKLRA------EQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMskaeAFEESVRM--LDAVKMPEarKRMKMYPH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 142 QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-227 |
6.27e-38 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 131.92 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL-----QRDWQGEVQVLGQPLNAQKAFTGALRQQV 85
Cdd:cd03260 6 LNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQDPYaslhPLHR-IRRSLREPRQINGLPfDEASLMASVEQ----VGLPGNILDR-YPHQLSGGQRQRVAIVRALQL 159
Cdd:cd03260 84 GMVFQKPN----PFPGsIYDNVAYGLRLHGIK-LKEELDERVEEalrkAALWDEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDRALLINQGRVERHLDR 227
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
1.36e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKrgpsHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFt 78
Cdd:COG3842 3 MPALELENVSKRYG----DVTAL--DDvsLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 galRQQVQMVFQDpYAsLHPlH-----------RIRRslREPRQInglpfdEASLMASVEQVGLPGnILDRYPHQLSGGQ 147
Cdd:COG3842 76 ---KRNVGMVFQD-YA-LFP-HltvaenvafglRMRG--VPKAEI------RARVAELLELVGLEG-LADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 148 RQRVAIVRAlqlnpkllllDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMN---TVAhlcDRALLINQGRVE 222
Cdd:COG3842 141 QQRVALARAlapeprvlllDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEealALA---DRIAVMNDGRIE 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-222 |
1.61e-37 |
|
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: 130.82 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 19 HFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGALRQQVQMVFQDpYAsLHP 98
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNTVFQN-YA-LFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 99 LHRIRRSLREPRQINGLPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEikERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 177 VQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
1.83e-37 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 129.05 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPshfnALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgAL 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----AL--DDisLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE---EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDP--YASLhplhrirrslreprqinglpfdeaslmaSVEQvglpgNIldryphQLSGGQRQRVAIVRALQL 159
Cdd:cd03230 72 KRRIGYLPEEPslYENL----------------------------TVRE-----NL------KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-235 |
5.28e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 129.98 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQQV 85
Cdd:COG4555 4 VENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQDPYasLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:COG4555 77 GVLPDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEelIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDRAVLGELAG 235
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-223 |
6.89e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.02 E-value: 6.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEmdgLQIKAGE-CFgLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQK----AFt 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVS---LEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreiPY- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 gaLRQQVQMVFQDpyaslhplHRI--RRSLRE----PRQINGLPFDEAS--LMASVEQVGLpGNILDRYPHQLSGGQRQR 150
Cdd:COG2884 77 --LRRRIGVVFQD--------FRLlpDRTVYEnvalPLRVTGKSRKEIRrrVREVLDLVGL-SDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRVER 223
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-219 |
1.07e-36 |
|
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: 128.42 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFkrgpSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQV 85
Cdd:cd03235 2 VEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQDP-----------YASLHPLHRIRRSlreprqinglpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIV 154
Cdd:cd03235 78 SIDRDFPisvrdvvlmglYGHKGLFRRLSKA------------DKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 155 RALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQG 219
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-220 |
1.79e-36 |
|
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: 126.34 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALRQQVQMVFQ 90
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPyaslhplHRIRRSLREprqinglpfdeaslmasveqvglpgNILdryphqlSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:cd03228 84 DP-------FLFSGTIRE-------------------------NIL-------SGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 171 SALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGR 220
Cdd:cd03228 125 SALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-221 |
2.54e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 130.69 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTGAl 81
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsEKELRKA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQdpyaslhplHRIRRSLRE-------PRQINGLPfdEASLMASVEQ----VGLpGNILDRYPHQLSGGQRQR 150
Cdd:PRK11153 81 RRQIGMIFQ---------HFNLLSSRTvfdnvalPLELAGTP--KAEIKARVTEllelVGL-SDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-222 |
2.58e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.40 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSaVDINHLTVTFKRG-PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG 79
Cdd:PRK13637 1 MS-IKIENLTHIYMEGtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQdpyaslHPLHRIRRSLRE------PRQInGLPFDEAS--LMASVEQVGLPGN-ILDRYPHQLSGGQRQR 150
Cdd:PRK13637 80 DIRKKVGLVFQ------YPEYQLFEETIEkdiafgPINL-GLSEEEIEnrVKRAMNIVGLDYEdYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-222 |
1.74e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSaVDINHLTVTFKRgpshFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgA 80
Cdd:COG1118 1 MS-IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDpYAsLHPlH-----------RIRrslreprqinglPFDEASLMASVEQ----VGLPGnILDRYPHQLSG 145
Cdd:COG1118 73 RERRVGFVFQH-YA-LFP-HmtvaeniafglRVR------------PPSKAEIRARVEEllelVQLEG-LADRYPSQLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 146 GQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-221 |
2.34e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 125.97 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 27 GLQIKAGECFGLIGGSGSGKS----TLLRVL-AGLQRDwQGEVQVLGQPLNAQkaftgALR-QQVQMVFQDPYASLHPLH 100
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPC-----ALRgRKIATIMQNPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 101 RIRRSLREPRQINGLPFDEASLMASVEQVGL--PGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-221 |
2.37e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 126.39 E-value: 2.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG-QPLNAQKAFTgaLRQQVQMVF 89
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWE--IRKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QDPyaslhplhrirrslrePRQI---------------NGLPFDEaslM-----ASVEQVGLpGNILDRYPHQLSGGQRQ 149
Cdd:TIGR04520 84 QNP----------------DNQFvgatveddvafglenLGVPREE---MrkrvdEALKLVGM-EDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 150 RVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAhLCDRALLINQGRV 221
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-229 |
2.56e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.90 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFT-GALRQQVQMVFQD 91
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlQALRRDIQFIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 92 PYASLHPLHRIRRSLREPRQINGL-PFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDE 168
Cdd:PRK10261 410 PYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAwlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 169 PTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VERHLDRAV 229
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQiVEIGPRRAV 551
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-222 |
2.98e-35 |
|
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: 125.14 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 20 FNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgaLRQQVQMVFQDpYASLHPL 99
Cdd:cd03296 15 FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV----QERNVGFVFQH-YALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 H---------RIRRSLREPrqinglpfDEASLMASVEQ----VGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLL 166
Cdd:cd03296 90 TvfdnvafglRVKPRSERP--------PEAEIRAKVHEllklVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 167 DEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-220 |
1.30e-34 |
|
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: 121.20 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqKAFTGALRQQV 85
Cdd:cd00267 2 IENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQdpyaslhplhrirrslreprqinglpfdeaslmasveqvglpgnildryphqLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd00267 76 GYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
28-222 |
5.53e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 122.60 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGAL----RQQVQ-------MVFQ--DPYA 94
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpadRRQLQrirtrlgMVFQsfNLWS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 95 SLHPLHRIrrsLREPRQINGLPFDEASL--MASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:COG4598 109 HMTVLENV---IEAPVHVLGRPKAEAIEraEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 173 LDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:COG4598 185 LDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-222 |
1.12e-33 |
|
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: 120.48 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 33 GECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN--AQKAFTGALRQQVQMVFQDpyASLHPLHRIRRSLrepr 110
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsRKKINLPPQQRKIGLVFQQ--YALFPHLNVRENL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 111 qINGLPFDE-ASLMASVEQV----GLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLL 185
Cdd:cd03297 97 -AFGLKRKRnREDRISVDELldllGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 520926077 186 QALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-221 |
2.50e-33 |
|
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: 126.87 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqKAFTGALRQQVQMVFQ 90
Cdd:COG2274 479 VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR--QIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYasLhplhrIRRSLREprqiN---GLP-FDEASLMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAIVR 155
Cdd:COG2274 557 DVF--L-----FSGTIRE----NitlGDPdATDEEIIEAARLAGL-HDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-220 |
6.93e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 125.35 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQV 85
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 Q------------MVFQDPYASLHPLHRIRRSLREP-RQINGLPFDEASLMAS--VEQVGLPGN--ILDRYPHQLSGGQR 148
Cdd:PRK10261 95 AaqmrhvrgadmaMIFQEPMTSLNPVFTVGEQIAESiRLHQGASREEAMVEAKrmLDQVRIPEAqtILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 149 QRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-221 |
1.05e-32 |
|
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: 119.67 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTGALRQQVQMVFQDpyASLHPlHR-IRR 104
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsRKELRELRRKKISMVFQS--FALLP-HRtVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLREPRQINGLPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEIL 182
Cdd:cd03294 122 NVAFGLEVQGVPRAEreERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 183 NLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03294 201 DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-221 |
1.46e-32 |
|
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: 118.44 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGpshFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALRQQ 84
Cdd:cd03256 3 VENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 85 VQMVFQDP----------------YASLHPLHRIRRSLREPRQINGLpfdeaslmASVEQVGLPGNILDRyPHQLSGGQR 148
Cdd:cd03256 80 IGMIFQQFnlierlsvlenvlsgrLGRRSTWRSLFGLFPKEEKQRAL--------AALERVGLLDKAYQR-ADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 149 QRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
2.08e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 120.23 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQVLGQPLNAQ--KAFT 78
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVMAEKLEFNGQdlQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 GALRQQ-----VQMVFQDPYASLHPLHRI--------------RRSLREPRQINGLpfdeaslmasvEQVGLP--GNILD 137
Cdd:PRK11022 80 EKERRNlvgaeVAMIFQDPMTSLNPCYTVgfqimeaikvhqggNKKTRRQRAIDLL-----------NQVGIPdpASRLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 138 RYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLIN 217
Cdd:PRK11022 149 VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMY 228
|
....
gi 520926077 218 QGRV 221
Cdd:PRK11022 229 AGQV 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-171 |
3.74e-32 |
|
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: 114.67 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGALRQQVQMVFQDPyaSLHPLHRIRRSLR 107
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER--KSLRKEIGYVFQDP--QLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 108 EPRQINGLPFDEAS-----LMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:pfam00005 82 LGLLLKGLSKREKDaraeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-221 |
4.81e-32 |
|
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: 116.68 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 9 LTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALR-QQVQ 86
Cdd:TIGR02211 7 LGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlSSNERAKLRnKKLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 87 MVFQdpYASLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLL 164
Cdd:TIGR02211 87 FIYQ--FHHLLPDFTALENVAMPLLIGKKSVKEAKERAYemLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 165 LLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMnTVAHLCDRALLINQGRV 221
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQL 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-221 |
1.34e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.65 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA----QKAftg 79
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALR-QQVQMVFQDpyASLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRA 156
Cdd:PRK10584 84 KLRaKHVGFVFQS--FMLIPTLNALENVELPALLRGESSRQSRNGAKalLEQLGL-GKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 157 LQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDmNTVAHLCDRALLINQGRV 221
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-222 |
2.14e-31 |
|
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: 115.48 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgALRQQVQMVFQ 90
Cdd:cd03295 6 VTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV--ELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DpyASLHPLHRIRRSLREPRQINGLPfdEASLMASVEQ----VGL-PGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd03295 83 Q--IGLFPHMTVEENIALVPKLLKWP--KEKIRERADEllalVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-212 |
2.29e-31 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 114.25 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKrgpsHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ---PLNAQKAFTgALR 82
Cdd:TIGR03608 1 LKNISKKFG----DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASK-FRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDpYASLH----------PLHRIRRSLREPRQinglpfdeasLMASV-EQVGLpGNILDRYPHQLSGGQRQRV 151
Cdd:TIGR03608 76 EKLGYLFQN-FALIEnetveenldlGLKYKKLSKKEKRE----------KKKEAlEKVGL-NLKLKQKIYELSGGEQQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMnTVAHLCDR 212
Cdd:TIGR03608 144 ALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP-EVAKQADR 202
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-223 |
2.66e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 114.90 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 20 FNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgaLRQQVQMVFQDpYAsLHPL 99
Cdd:TIGR00968 13 FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA----RDRKIGFVFQH-YA-LFKH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLREPRQIngLPFDEASLMASVEQ----VGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:TIGR00968 87 LTVRDNIAFGLEI--RKHPKAKIKARVEEllelVQLEG-LGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520926077 176 TVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVER 223
Cdd:TIGR00968 164 KVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQ 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-222 |
4.12e-31 |
|
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: 113.89 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 20 FNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGALRQQVQMVFQDpYAsLHPL 99
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAMVFQN-YA-LYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLREPRQINGLPFDEASlmASVEQV----GLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEID--ERVREVaellQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 176 TVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-212 |
7.81e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 116.16 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRD----------WQGeVQVLGQP 70
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrWNG-IDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 71 LNAQKAFTGalrQQVQMVFQDPYASLHPLHRIRRSLREprqinGLPFDEAS-------------LMASVEQVGL--PGNI 135
Cdd:COG4170 80 PRERRKIIG---REIAMIFQEPSSCLDPSAKIGDQLIE-----AIPSWTFKgkwwqrfkwrkkrAIELLHRVGIkdHKDI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 136 LDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDR 212
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-222 |
9.55e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 9.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 7 NHLTVT--FKRGPSHfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN-----------A 73
Cdd:PRK10619 4 NKLNVIdlHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 74 QKAFTGALRQQVQMVFQDPYASLHpLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRV 151
Cdd:PRK10619 83 DKNQLRLLRTRLTMVFQHFNLWSH-MTVLENVMEAPIQVLGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-221 |
1.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRG-PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKA--FTGA 80
Cdd:PRK13646 3 IRFDNVSYTYQKGtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDPYASLHPLHRIRRSLREPRQINgLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIFGPKNFK-MNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.08e-30 |
|
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: 118.71 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVtfkRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGAL 81
Cdd:COG4988 335 PSIELEDVSF---SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP--ASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDPYasLHPLhrirrSLREprqiN---GLP-FDEASLMASVEQVGLpGNILDRYPH-----------QLSGG 146
Cdd:COG4988 410 RRQIAWVPQNPY--LFAG-----TIRE----NlrlGRPdASDEELEAALEAAGL-DEFVAALPDgldtplgeggrGLSGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-221 |
1.18e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 113.14 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPSHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGALRQQV 85
Cdd:PRK10771 4 LTDITWLYHHLPMRFD------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT----TPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQD----PYAS--------LHPLHRIRRSLREprqinglpfdeaSLMASVEQVGLpGNILDRYPHQLSGGQRQRVAI 153
Cdd:PRK10771 74 SMLFQEnnlfSHLTvaqniglgLNPGLKLNAAQRE------------KLHAIARQMGI-EDLLARLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-221 |
2.31e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgaLRQ 83
Cdd:PRK13635 6 IRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD--VRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDP---YASLHPLHRIRRSLREprqiNGLPFDE--ASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:PRK13635 82 QVGMVFQNPdnqFVGATVQDDVAFGLEN----IGVPREEmvERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-223 |
7.15e-30 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 112.19 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRgpSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALRQQVQMVFQDP 92
Cdd:PRK15112 21 FRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGDYSYRSQRIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 93 YASLHPLHRIRRSLREPRQIN---GLPFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEP 169
Cdd:PRK15112 97 STSLNPRQRISQILDFPLRLNtdlEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 170 TSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR-VER 223
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEvVER 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-224 |
8.51e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG--ALRQQVQMVFQDPYASLHPlHRIRRSLR 107
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkPLRKKVGIVFQFPEHQLFE-ETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLL 185
Cdd:PRK13634 109 FGPMNFGVSEEDAKQKARemIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 186 QALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:PRK13634 189 YKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-202 |
8.96e-30 |
|
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: 110.26 E-value: 8.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQQVQMVFQDP--YASLhplhrirrS 105
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---DYRRRLAYLGHADglKPEL--------T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREP----RQINGLPFDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEI 181
Cdd:COG4133 92 VRENlrfwAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180
....*....|....*....|.
gi 520926077 182 LNLLQALRRDTGMTmILVSHD 202
Cdd:COG4133 171 AELIAAHLARGGAV-LLTTHQ 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-221 |
1.09e-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: 110.37 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQ 90
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPyaslhplHRIRRSLREPRQINGLPFDEASLMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAIVRALQL 159
Cdd:cd03245 86 DV-------TLFYGTLRDNITLGAPLADDERILRAAELAGV-TDFVNKHPNgldlqigergrGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAhLCDRALLINQGRV 221
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-226 |
2.66e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG----ALRQQVQMVFQDpYaSLHPLHRIR 103
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkairELRRNVGMVFQQ-Y-NLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLRE-PRQINGLPFDEA--SLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:PRK11124 101 QNLIEaPCRVLGLSKDQAlaRAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 181 ILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLD 226
Cdd:PRK11124 180 IVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.71e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHltVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgaL 81
Cdd:PRK13632 6 VMIKVEN--VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDP---YASLHPLHRIRRSLrEPRQInglPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRA 156
Cdd:PRK13632 82 RKKIGIIFQNPdnqFIGATVEDDIAFGL-ENKKV---PPKKmkDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 157 LQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAhLCDRALLINQGRV 221
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-221 |
5.77e-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: 108.96 E-value: 5.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ-PLNAQKAF----TGA 80
Cdd:cd03267 20 IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKFlrriGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDPyaslhplhrIRRSLREPRQINGLPFDEA--SLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:cd03267 100 FGQKTQLWWDLP---------VIDSFYLLAAIYDLPPARFkkRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-221 |
7.53e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.88 E-value: 7.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 14 KRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALRQQVQMVFQDp 92
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 93 yASLHPLHRIRRSLREPRQINGLPFDEAS--LMASVEQVGLPGNIlDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:cd03292 87 -FRLLPDRNVYENVAFALEVTGVPPREIRkrVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 171 SALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-221 |
1.02e-28 |
|
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: 107.58 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkAFTGALRQ 83
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD------LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDP--YASLHPLHRIRRSLREPRQINglPFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03298 71 PVSMLFQENnlFAHLTVEQNVGLGLSPGLKLT--AEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-221 |
1.33e-28 |
|
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: 113.04 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQ 90
Cdd:TIGR03375 469 VSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG--VDIRQIDPADLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYAslhplhrIRRSLREPRQINGLPFDEASLMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAIVRALQL 159
Cdd:TIGR03375 547 DPRL-------FYGTLRDNIALGAPYADDEEILRAAELAGV-TEFVRRHPDgldmqigergrSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMnTVAHLCDRALLINQGRV 221
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-221 |
1.66e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.79 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG------QPLNAQKAFtgALRQQVQMVFQDpYaSLHPLHR 101
Cdd:COG4161 23 LECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR--LLRQKVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 IRRSLRE-PRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:COG4161 99 VMENLIEaPCKVLGLSKEQAREKAMklLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4161 178 AQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-223 |
1.75e-28 |
|
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: 109.51 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgalRQQVQMVFQDpYAsLHPLHRIRRSLREPRQINGLPF 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH----LRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 118 DE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMT 195
Cdd:TIGR01187 75 AEikPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*...
gi 520926077 196 MILVSHDMNTVAHLCDRALLINQGRVER 223
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQ 181
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-221 |
2.02e-28 |
|
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: 105.20 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqkaFTG---ALRQQVQMVfqdpyaslhplhrirr 104
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----FASprdARRAGIAMV---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 slreprqinglpfdeaslmasveqvglpgnildrypHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDmtvQAEILNL 184
Cdd:cd03216 81 ------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALT---PAEVERL 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 185 LQALRR--DTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03216 122 FKVIRRlrAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
2.32e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.78 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFkrgpSHFNALE-MDgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTG 79
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKdID-LDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQDpYAsLHPlH-----------RIRRslreprqinglpFDEASLMASVEQV----GLpGNILDRYPHQLS 144
Cdd:COG3839 72 PKDRNIAMVFQS-YA-LYP-HmtvyeniafplKLRK------------VPKAEIDRRVREAaellGL-EDLLDRKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 145 GGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHD----MnTVAhlcDRALLINQGR 220
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM-TLA---DRIAVMNDGR 211
|
..
gi 520926077 221 VE 222
Cdd:COG3839 212 IQ 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
28-222 |
4.01e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.65 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgaLRQQVQMVFQDpYAsLHPLHRIRRSLR 107
Cdd:PRK09452 35 LTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA----ENRHVNTVFQS-YA-LFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDE-------ASLMASVEQVGlpgnilDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:PRK09452 109 FGLRMQKTPAAEitprvmeALRMVQLEEFA------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520926077 181 ILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK09452 183 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-221 |
8.14e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 8.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGA-----LRQQVQMVFqdPYaslhPLHRI 102
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArrravLPQHSSLSF--PF----TVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 103 RRSLREPRQINGLPFDEAsLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLL------DEPTSALDMT 176
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDAL-VAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPprwlllDEPTSALDLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 177 VQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.82e-27 |
|
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: 104.51 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQ 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK---AARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQD--------PYASLHPLHRIRrslreprqinGLPFDEASLMASV--EQVGLPGnILDRYPHQLSGGQRQRVAI 153
Cdd:cd03263 76 SLGYCPQFdalfdeltVREHLRFYARLK----------GLPKSEIKEEVELllRVLGLTD-KANKRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
2.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNaLEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTga 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDP---YASLHPLHRIRRSLREprqiNGLPFDE--ASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVR 155
Cdd:PRK13650 79 IRHKIGMVFQNPdnqFVGATVEDDVAFGLEN----KGIPHEEmkERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAhLCDRALLINQGRVE 222
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
6-221 |
4.15e-27 |
|
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: 103.40 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPSHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGALRQQV 85
Cdd:TIGR01277 3 LDKVRYEYEHLPMEFD------LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG----LAPYQRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 QMVFQDP--YASLHPLHRIRRSLREPRQINGLpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:TIGR01277 73 SMLFQENnlFAHLTVRQNIGLGLHPGLKLNAE--QQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR01277 150 LLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-220 |
4.30e-27 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 103.48 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTvtfKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALR 82
Cdd:TIGR02673 2 IEFHNVS---KAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDPYASLH---------PLHRIRRSLREPRQinglpfdeaSLMASVEQVGLPGNIlDRYPHQLSGGQRQRVAI 153
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDrtvyenvalPLEVRGKKEREIQR---------RVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:TIGR02673 149 ARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-221 |
4.48e-27 |
|
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: 108.35 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQV-LGQ---------PLNAQKA--FTGALRQQVqmvfqdpyaS 95
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvdmtkpgPDGRGRAkrYIGILHQEY---------D 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LHPLHRIRRSLREPRQINgLPfDEASLMASVEQVGLPG-------NILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDE 168
Cdd:TIGR03269 376 LYPHRTVLDNLTEAIGLE-LP-DELARMKAVITLKMVGfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520926077 169 PTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-221 |
4.79e-27 |
|
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: 101.91 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDpyaslhplhrirrslr 107
Cdd:cd03246 23 FSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD--PNELGDHVGYLPQD---------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqinglpfDEAslmasveqvgLPGNILDRYphqLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:cd03246 85 ----------DEL----------FSGSIAENI---LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 188 LRRdTGMTMILVSHDMNTVAhLCDRALLINQGRV 221
Cdd:cd03246 142 LKA-AGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
5.34e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDglqIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQ 83
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININ---IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPYASLHPLHRIRRSLREPRQInGLPFDEAS--LMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSFGAVNL-KLPEDEVRkrVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-221 |
6.17e-27 |
|
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: 102.72 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTFKRGPShfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkaftGALRQQ 84
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-----KERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 85 VQMVFQDPYaslHPLHR--IRRSLREprqinGLPFDEASLmASVEQV----GLpgNIL-DRYPHQLSGGQRQRVAIVRAL 157
Cdd:cd03226 73 IGYVMQDVD---YQLFTdsVREELLL-----GLKELDAGN-EQAETVlkdlDL--YALkERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 158 QLNPKLLLLDEPTSALD---MTVQAEILNLLQAlrrdTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDyknMERVGELIRELAA----QGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-221 |
8.17e-27 |
|
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: 103.53 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFkrgPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTGALRQQ 84
Cdd:TIGR02315 4 VENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 85 VQMVFQDpYASLHPLHRIRRSL--REPRQ--INGL--PF---DEASLMASVEQVGLPGNILDRyPHQLSGGQRQRVAIVR 155
Cdd:TIGR02315 81 IGMIFQH-YNLIERLTVLENVLhgRLGYKptWRSLlgRFseeDKERALSALERVGLADKAYQR-ADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-221 |
1.71e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 104.96 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 36 FGLiggSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN--AQKAFTGALRQQVQMVFQDpyASLHPLHRIRRSLREprqin 113
Cdd:PRK11144 30 FGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaEKGICLPPEKRRIGYVFQD--ARLFPHYKVRGNLRY----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 114 GL-PFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDT 192
Cdd:PRK11144 100 GMaKSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180
....*....|....*....|....*....
gi 520926077 193 GMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-221 |
2.66e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.45 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkaftgaLRQQVQMVFQDpyASLHPLHRIrrslr 107
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-------AREDTRLMFQD--ARLLPWKKV----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqIN----GLPFD--EASLMAsVEQVGLPgnilDR---YPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:PRK11247 99 ----IDnvglGLKGQwrDAALQA-LAAVGLA----DRaneWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11247 170 IEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-221 |
4.25e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQV---LGQPLNAQKAFTgALRQQVQMVFQDPYASLHPLHRIRR 104
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdiVVSSTSKQKEIK-PVRKKVGVVFQFPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLREPRQInGLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEIL 182
Cdd:PRK13643 106 VAFGPQNF-GIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 183 NLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13643 185 QLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-224 |
4.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGL-----QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG--ALRQQVQMVFQDPYAS 95
Cdd:PRK13641 18 MEKKGLdnisfELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkKLRKKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LHPLHRIRRSLREPRQInGLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSAL 173
Cdd:PRK13641 98 LFENTVLKDVEFGPKNF-GFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 174 DMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
4.50e-26 |
|
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: 100.43 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRgpshFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFT-GALR 82
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQvqmvfqdpyASLHPLHRIRRSLREPRQINGLPFDEA--SLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLN 160
Cdd:cd03269 77 EE---------RGLYPKMKVIDQLVYLAQLKGLKKEEArrRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-221 |
5.35e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.63 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDPYaslhplhRIRRSLR 107
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT--LESLRRQIGVVPQDTF-------LFSGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EprqiN---GLP-FDEASLMASVEQVGLpGNILDRYPHQ-----------LSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:COG1132 432 E----NiryGRPdATDEEVEEAAKAAQA-HEFIEALPDGydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 173 LDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:COG1132 507 LDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-221 |
1.28e-25 |
|
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: 99.75 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQ 83
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA---EARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDpyASLHPLHRIRRSLREPRQINGLPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03266 79 RLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDEltARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-223 |
1.29e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSaVDINHLTVTFKRGpshfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGA 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDpYA-------------SLHPLHRIRR-SLREPRQinglpfdeaSLMASVEQVGLpGNILDRYPHQLSGG 146
Cdd:PRK10851 72 RDRKVGFVFQH-YAlfrhmtvfdniafGLTVLPRRERpNAAAIKA---------KVTQLLEMVQL-AHLADRYPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVER 223
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
28-221 |
1.38e-25 |
|
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: 100.50 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALR------QQVQ--------------M 87
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiartfQNPRlfpeltvlenvlvaA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 88 VFQDPYASLHPLHRIRRSLREPRQINglpfDEAslMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLD 167
Cdd:COG0411 105 HARLGRGLLAALLRLPRARREEREAR----ERA--EELLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 520926077 168 EPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-221 |
1.44e-25 |
|
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: 99.54 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVFQDPYASLHPLHRIRRS-- 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGhi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 --LREPRQInglpfDEASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:TIGR03771 81 gwLRRPCVA-----DFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDtGMTMILVSHDMNTVAHLCDRALLINqGRV 221
Cdd:TIGR03771 155 LFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRV 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-221 |
4.46e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.82 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTG--ALRQQVQMVFQDPYASLHPLHRIRRS 105
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikQIRKKVGLVFQFPESQLFEETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPrQINGLPFDEASLMA--SVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:PRK13649 108 AFGP-QNFGVSQEEAEALAreKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13649 187 LFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-222 |
6.92e-25 |
|
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: 98.18 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ---PLNAQKaftgalrQQVQMVFQDpYAsLHPL 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-------RDISYVPQN-YA-LFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIR-------RSLREPRqinglPFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:cd03299 86 MTVYkniayglKKRKVDK-----KEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 173 LDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-212 |
6.97e-25 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 100.26 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRD-WQ--------GEVQVLGQPL 71
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnWRvtadrmrfDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 72 NAQKAFTGalrQQVQMVFQDPYASLHPLHRIRRSL-------------------REPRQINGLpfdeaslmasvEQVGL- 131
Cdd:PRK15093 81 RERRKLVG---HNVSMIFQEPQSCLDPSERVGRQLmqnipgwtykgrwwqrfgwRKRRAIELL-----------HRVGIk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 132 -PGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLC 210
Cdd:PRK15093 147 dHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
..
gi 520926077 211 DR 212
Cdd:PRK15093 227 DK 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-221 |
7.34e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA----QKAFTGA-LRQQVQMVFqdPYAS------- 95
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRRAvLPQHSSLAF--PFTVeevvalg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LHPLHRIRRslrEPRQInglpfdeasLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLL-------DE 168
Cdd:COG4559 100 RAPHGSSAA---QDRQI---------VREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGgprwlflDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520926077 169 PTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
1.87e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.84 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 17 PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVFQDPYASL 96
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 H-----------PLHRirrslreprqinGLPFDEAS--LMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:PRK13639 92 FaptveedvafgPLNL------------GLSKEEVEkrVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-221 |
2.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.23 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 9 LTVTFKRG-PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQ---------------------- 65
Cdd:PRK13651 8 IVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 66 VLGQPLNAQKAFTGALRQQVQMVFQdpYASlhplHRIRRSLRE------PRQInGLPFDEASLMAS--VEQVGLPGNILD 137
Cdd:PRK13651 88 VIQKTRFKKIKKIKEIRRRVGVVFQ--FAE----YQLFEQTIEkdiifgPVSM-GVSKEEAKKRAAkyIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 138 RYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLIN 217
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 520926077 218 QGRV 221
Cdd:PRK13651 240 DGKI 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-221 |
4.13e-24 |
|
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: 95.90 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 20 FNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAfTGALRQQVQMVFQDPyaSLHPL 99
Cdd:cd03265 13 FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVRE-PREVRRRIGIVFQDL--SVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLREPRQINGLPFDEASLMAS--VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTV 177
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDelLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 178 QAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-221 |
6.13e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG-QPLNAQKAFtgaLRQ------QVQMVFQDpyaslHPLh 100
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRRKEF---ARRigvvfgQRSQLWWD-----LPA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 101 riRRSLREPRQINGLPFDEA--SLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:COG4586 114 --IDSFRLLKAIYRIPDAEYkkRLDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-220 |
6.49e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkAFTGALRQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDpYAsLHPLHRIRRSLREPRQINGLPFDEASLMASvEQVGLP--GNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:PRK11607 92 PINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKAEIASRVN-EMLGLVhmQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 162 KLLLLDEPTSALDMTV----QAEILNLLQALrrdtGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK11607 169 KLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-224 |
7.67e-24 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 97.76 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFkrgpsHFNALEMD-GLQIKAGECFGLIGGSGSGKSTLLRVLAGLQR--DWQGEVQVLGQPLNAQKAFt 78
Cdd:TIGR03258 4 GGIRIDHLRVAY-----GANTVLDDlSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKaaGLTGRIAIADRDLTHAPPH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 galRQQVQMVFQDpYA---SLHPLHRIRRSLREPRQINGLPFDEASlmASVEQVGLpGNILDRYPHQLSGGQRQRVAIVR 155
Cdd:TIGR03258 78 ---KRGLALLFQN-YAlfpHLKVEDNVAFGLRAQKMPKADIAERVA--DALKLVGL-GDAAAHLPAQLSGGMQQRIAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQAL-RRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:TIGR03258 151 AIAIEPDVLLLDEPLSALDANIRANMREEIAALhEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAH 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-221 |
8.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRgPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgaLRQ 83
Cdd:PRK13642 5 LEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN--LRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPYASLHPLhRIRRSLREPRQINGLPFDEasLMASVEQVGLPGNILD---RYPHQLSGGQRQRVAIVRALQLN 160
Cdd:PRK13642 82 KIGMVFQNPDNQFVGA-TVEDDVAFGMENQGIPREE--MIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-225 |
9.28e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 95.27 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 7 NHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQ 86
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 87 MVFQDPYASLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLPGNILDRyPHQLSGGQRQRVAIVRALQLNPKLL 164
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALemLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 165 LLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNtVAHLCDRALLINQGRVERHL 225
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGRLTAEL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
28-211 |
1.20e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGEcFGLIGG-SGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGALRQQVQMVFQDPyaSLHPlHRIRRSL 106
Cdd:PRK10247 28 FSLRAGE-FKLITGpSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--EIYRQQVSYCAQTP--TLFG-DTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQINGLPFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQ 186
Cdd:PRK10247 102 IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIH 181
|
170 180
....*....|....*....|....*
gi 520926077 187 ALRRDTGMTMILVSHDMNTVAHlCD 211
Cdd:PRK10247 182 RYVREQNIAVLWVTHDKDEINH-AD 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-235 |
1.30e-23 |
|
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: 98.68 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkAFTGALRQQVQMVFQ 90
Cdd:COG4987 339 VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRIAVVPQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPY---ASlhplhrIRRSLReprqingLPFDEAS---LMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAI 153
Cdd:COG4987 417 RPHlfdTT------LRENLR-------LARPDATdeeLWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRVERHLDRAVLGEL 233
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQ 559
|
..
gi 520926077 234 AG 235
Cdd:COG4987 560 NG 561
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-221 |
1.34e-23 |
|
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: 94.81 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGAlRQQVQMVFQDP--YASLHPL------ 99
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA-RLGIGRTFQIPrlFPELTVLenvmva 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 --HRIRRSLREPRQINGLPFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTV 177
Cdd:cd03219 100 aqARTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 178 QAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03219 179 TEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-219 |
1.83e-23 |
|
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: 94.45 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGALRQqvqMVFQDpyASLHP--------- 98
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE----PGPDRM---VVFQN--YSLLPwltvrenia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 99 --LHRIRRSLREPRQinglpfdEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:TIGR01184 77 laVDRVLPDLSKSER-------RAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 177 VQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQG 219
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-212 |
2.16e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkAFTG---ALRQQVQMVFQDPyaSLHPlhrirr 104
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV----RFRSprdAQAAGIAIIHQEL--NLVP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SL---------REPRqiNGLPFDEASLMASVEQvglpgnILDRY-----PHQ----LSGGQRQRVAIVRALQLNPKLLLL 166
Cdd:COG1129 93 NLsvaeniflgREPR--RGGLIDWRAMRRRARE------LLARLgldidPDTpvgdLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520926077 167 DEPTSALDmtvQAEILNLLQALR--RDTGMTMILVSHDMNTVAHLCDR 212
Cdd:COG1129 165 DEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADR 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-221 |
2.29e-23 |
|
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: 93.44 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGpshfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQplNAQKafTGALRQ 83
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQK--NIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDP--YASLHPLHRIRRSLREPRqinglpFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03268 73 RIGALIEAPgfYPNLTARENLRLLARLLG------IRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-222 |
2.56e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 95.54 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgALRQQVQMVFQDpyASLHPlHRirrSLR 107
Cdd:COG1125 23 LTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPV--ELRRRIGYVIQQ--IGLFP-HM---TVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 E-----PRqINGLPFDEAS-----LMasvEQVGL-PGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:COG1125 95 EniatvPR-LLGWDKERIRarvdeLL---ELVGLdPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 177 VQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:COG1125 171 TREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-224 |
5.88e-23 |
|
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: 92.26 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGpshfNALEMDGLQIKAGeCFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQ 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ---KLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPyaSLHPLHRIRRSLREPRQINGLP---FDEASLMAsVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLN 160
Cdd:cd03264 73 RIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPskeVKARVDEV-LELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-221 |
9.80e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL----NAQKAFtgaLRQQVQMVFQDPYASLH 97
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPF---LRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 98 plHRIRRSLREPRQINGLPFDEAS--LMASVEQVGLpgniLDR---YPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:PRK10908 94 --RTVYDNVAIPLIIAGASGDDIRrrVSAALDKVGL----LDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 173 LDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10908 168 LDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-221 |
1.03e-22 |
|
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: 96.18 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHltVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALR 82
Cdd:TIGR03797 451 AIEVDR--VTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD--VQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDpyASLHP---LHRIRRSlreprqiNGLPFDEAslMASVEQVGLPGNIlDRYPHQ-----------LSGGQR 148
Cdd:TIGR03797 527 RQLGVVLQN--GRLMSgsiFENIAGG-------APLTLDEA--WEAARMAGLAEDI-RAMPMGmhtvisegggtLSGGQR 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 149 QRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRrdtgMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRV 662
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-221 |
1.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTF-KRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVqVLGQ---PLNAQK-AFTGA 80
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaiPANLKKiKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDPYASLH-----------PLHRIRRSLREPRQINGLpfdeaslmasVEQVGLPGNILDRYPHQLSGGQRQ 149
Cdd:PRK13645 88 LRKEIGLVFQFPEYQLFqetiekdiafgPVNLGENKQEAYKKVPEL----------LKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 150 RVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
1.86e-22 |
|
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: 95.05 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFkrgPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftGAL 81
Cdd:TIGR02857 320 SSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA--DSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMVFQDPY---ASLhpLHRIRRSLREPrqinglpfDEASLMASVEQVG-------LPGNI---LDRYPHQLSGGQR 148
Cdd:TIGR02857 395 RDQIAWVPQHPFlfaGTI--AENIRLARPDA--------SDAEIREALERAGldefvaaLPQGLdtpIGEGGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 149 QRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTvAHLCDR 212
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADR 525
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
4.02e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPShfnaleMDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAft 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTV------LDGvdLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 GALRQQVQMVFQDpyASLHPLHRIRRSL---REP---RQINGLPFDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVA 152
Cdd:PRK09536 73 RAASRRVASVPQD--TSLSFEFDVRQVVemgRTPhrsRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 153 IVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-222 |
4.81e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAF----TGALRQQVQMVFQDPYASLH------ 97
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidAIKLRKEVGMVFQQPNPFPHlsiydn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 98 ---PLHRirRSLREPRQINGLpfdeasLMASVEQVGLPGNILDRY---PHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:PRK14246 111 iayPLKS--HGIKEKREIKKI------VEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 520926077 172 ALDMTVQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDR-ALLINQGRVE 222
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYvAFLYNGELVE 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-204 |
5.28e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAG-LQRD--WQGEVQVLGQPLNAQKAftgaLRQQVQMVFQDPYasLHPlH---- 100
Cdd:COG4136 22 LTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPA----EQRRIGILFQDDL--LFP-Hlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 101 ---------RIRRSLREprqinglpfdeASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:COG4136 95 enlafalppTIGRAQRR-----------ARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|...
gi 520926077 172 ALDMTVQAEILNLLQALRRDTGMTMILVSHDMN 204
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-221 |
5.35e-22 |
|
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: 90.19 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGAlRQQVQMVFQDpyaslhplHRIRRSL- 106
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA-RAGIGYVPEG--------RRIFPELt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 -REPRQINGLPFDEASLMASVEQVglpgniLDRYP----------HQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:cd03224 92 vEENLLLGAYARRRAKRKARLERV------YELFPrlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 176 TVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03224 166 KIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-221 |
5.60e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.79 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN----AQKAftgalrqqVQMVFQDpYAsLHPlHRir 103
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvppAERG--------VGMVFQS-YA-LYP-HL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 rSLREPRQInGLPF---DEASLMASVEQVG----LpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD-- 174
Cdd:PRK11000 91 -SVAENMSF-GLKLagaKKEEINQRVNQVAevlqL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 175 MTVQ--AEILNLLQALRRdtgmTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11000 168 LRVQmrIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-221 |
5.62e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFkrgpSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL------QRdWQGEVQVLGQPLNAQK 75
Cdd:COG1117 10 PKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgAR-VEGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 76 AFTGALRQQVQMVFQDP-------Y---ASLHPLHRIRRslrePRQINGLPfdEASLmasvEQVGLPG---NILDRYPHQ 142
Cdd:COG1117 85 VDVVELRRRVGMVFQKPnpfpksiYdnvAYGLRLHGIKS----KSELDEIV--EESL----RKAALWDevkDRLKKSALG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 143 LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-221 |
5.74e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.00 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTgalRQQVQMVFQDPYASlhplhriRRS 105
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFA---RKVAYLPQQLPAAE-------GMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPF----------DEASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:PRK10575 102 VRELVAIGRYPWhgalgrfgaaDREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 176 TVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-221 |
8.41e-22 |
|
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: 88.64 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkaftgalrqqvqmvfqdpyasLHPLHRIRRSLR 107
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR----------------------RSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 ---EPRQINGLpFDEASLMAsveqvglpgNILdrYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNL 184
Cdd:cd03215 79 yvpEDRKREGL-VLDLSVAE---------NIA--LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 520926077 185 LQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03215 147 IRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
1.09e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqkafTGA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG----PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQqvqMVFQDpyASLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQVGLPGNIlDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:COG4525 77 DRG---VVFQK--DALLPWLNVLDNVAFGLRLRGVPKAERRARAEelLALVGLADFA-RRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHD 202
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-216 |
1.35e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFKRGPShfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTG 79
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQDPYASLHPLHRIRRS----LREPRqinglPFDEASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVR 155
Cdd:PRK15056 82 YVPQSEEVDWSFPVLVEDVVMMGRYGhmgwLRRAK-----KRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLI 216
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
11-221 |
1.55e-21 |
|
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: 92.88 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnAQkAFTGALRQQVQMVFQ 90
Cdd:TIGR01846 461 IRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AI-ADPAWLRRQMGVVLQ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYAslhplhrIRRSLREP-RQIN-GLPFDE---ASLMASVEQ--VGLP---GNILDRYPHQLSGGQRQRVAIVRALQLN 160
Cdd:TIGR01846 539 ENVL-------FSRSIRDNiALCNpGAPFEHvihAAKLAGAHDfiSELPqgyNTEVGEKGANLSGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQI 669
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
2.91e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKrgpshfNALEMDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGL-----QRDWQGEVQVLGQPLNa 73
Cdd:PRK14247 1 MNKIEIRDLKVSFG------QVEVLDGvnLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 74 qKAFTGALRQQVQMVFQ--DPYASLH---------PLHRIRRSLREPRQINGLPFDEASLMASVEqvglpgNILDRYPHQ 142
Cdd:PRK14247 74 -KMDVIELRRRVQMVFQipNPIPNLSifenvalglKLNRLVKSKKELQERVRWALEKAQLWDEVK------DRLDAPAGK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 143 LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-221 |
3.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.47 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFKRGPShfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL---QRDWQGEVQVLGQPLNAQKAFT 78
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 gaLRQQVQMVFQDP---YASLHPLHRIRRSLrEPRQInglPFDEA-SLMASV-EQVGLPgNILDRYPHQLSGGQRQRVAI 153
Cdd:PRK13640 82 --IREKVGIVFQNPdnqFVGATVGDDVAFGL-ENRAV---PRPEMiKIVRDVlADVGML-DYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTvAHLCDRALLINQGRV 221
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKL 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-228 |
4.03e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDG---------------LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqkaFTG---ALRQ 83
Cdd:COG3845 5 ALELRGitkrfggvvanddvsLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR----IRSprdAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPyaSLHPlhrirrSL---------REPRQINGLPFDEAS--LMASVEQVGLPGNiLDRYPHQLSGGQRQRVA 152
Cdd:COG3845 81 GIGMVHQHF--MLVP------NLtvaenivlgLEPTKGGRLDRKAARarIRELSERYGLDVD-PDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 153 IVRALQLNPKLLLLDEPTSALdmTVQaEILNLLQALRR--DTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDRA 228
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-221 |
4.37e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 37 GLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVFQDP-----YASLHPlhRIRRSLREprq 111
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPeqqifYTDIDS--DIAFSLRN--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 112 ingLPFDEASLMASVEQvGLPGNILDRYPHQ----LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:PRK13638 106 ---LGVPEAEITRRVDE-ALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 188 LRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13638 182 IVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-222 |
7.07e-21 |
|
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: 86.21 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKaftGALRQQVQMVFQ 90
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 DPYAslhplhrirrslreprqinglpFDeASLMasvEQVGLpgnildryphQLSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:cd03247 83 RPYL----------------------FD-TTLR---NNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520926077 171 SALDMTVQAEILNLL-QALRrdtGMTMILVSHDMNTVAHLcDRALLINQGRVE 222
Cdd:cd03247 127 VGLDPITERQLLSLIfEVLK---DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
8.70e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRGPshfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgaLR 82
Cdd:PRK13647 4 IIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW--VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDP----YAS-------LHPLH-RIRRSLREPRQinglpfdEASLMAsveqVGLPgNILDRYPHQLSGGQRQR 150
Cdd:PRK13647 79 SKVGLVFQDPddqvFSStvwddvaFGPVNmGLDKDEVERRV-------EEALKA----VRMW-DFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-222 |
9.97e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 17 PSHFNALEMDGL--QIKAGECFGLIGGSGSGKSTllrVLAGLQRDWQ---GEVQVLGQPLnaQKAFTGALRQQVQMVFQD 91
Cdd:TIGR00958 489 PNRPDVPVLKGLtfTLHPGEVVALVGPSGSGKST---VAALLQNLYQptgGQVLLDGVPL--VQYDHHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 92 PYAslhplhrIRRSLREpRQINGLPFDEASLMASVEQVGLPGNILDRYPH-----------QLSGGQRQRVAIVRALQLN 160
Cdd:TIGR00958 564 PVL-------FSGSVRE-NIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 161 PKLLLLDEPTSALDmtvqAEILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGRVE 222
Cdd:TIGR00958 636 PRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-221 |
1.17e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRV---LAGLQRDW--QGEVQVLGQPLNAQKAFTGALRQQVQMVFQDPYASLH----- 97
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFPHltiyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 98 ------PLHRIRRSLREPRQINGLPFDEASLMASVEqvglpgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:PRK14267 105 nvaigvKLNGLVKSKKELDERVEWALKKAALWDEVK------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 172 ALDMTVQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-221 |
1.80e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRdWQGEVQVLGQPLNAQKAFTGA-----LRQQVQMVFQDP---YASLHpl 99
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELArhrayLSQQQSPPFAMPvfqYLALH-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 hrIRRSLREPRQinglpfdEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRA-------LQLNPKLLLLDEPTSA 172
Cdd:COG4138 94 --QPAGASSEAV-------EQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVllqvwptINPEGQLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 173 LDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG4138 164 LDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
28-221 |
2.53e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAFTGALRQQVQMVFQDpYASLHPLhRIRRS 105
Cdd:PRK10535 29 LDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldADALAQLRREHFGFIFQR-YHLLSHL-TAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:PRK10535 107 VEVPAVYAGLERKQrlLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALrRDTGMTMILVSHDmNTVAHLCDRALLINQGRV 221
Cdd:PRK10535 186 ILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-222 |
2.79e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.98 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQqVQMVFQDpYAsLHPLHRIRRSLR 107
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRD-IAMVFQN-YA-LYPHMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEasLMASVEQV----GLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD--MTVQ--A 179
Cdd:PRK11650 99 YGLKIRGMPKAE--IEERVAEAarilEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDakLRVQmrL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 180 EIlnllQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK11650 176 EI----QRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
3.72e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTF-KRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGA-- 80
Cdd:PRK13631 22 LRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 ------------LRQQVQMVFQDPYASLHPLHRIRRSLREPRQInGLPFDEASLMAS--VEQVGLPGNILDRYPHQLSGG 146
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKfyLNKMGLDDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
4.92e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MS-AVDINHLTVTFKRGPS------------------HFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRD 59
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHEpsrslkelllrrrrtrreEFWAL--KDvsFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 60 WQGEVQV---------LGQPLNAQkaFTGalRQQVQMvfqdpYASLHPLHRirrslREPRQInglpFDEAslmasVEQVG 130
Cdd:COG1134 79 TSGRVEVngrvsalleLGAGFHPE--LTG--RENIYL-----NGRLLGLSR-----KEIDEK----FDEI-----VEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 131 LpGNILDRyP-HQLSGGQRQRVA------------IVralqlnpkllllDEPTSALDMTVQAEILNLLQALRRDtGMTMI 197
Cdd:COG1134 136 L-GDFIDQ-PvKTYSSGMRARLAfavatavdpdilLV------------DEVLAVGDAAFQKKCLARIRELRES-GRTVI 200
|
250 260
....*....|....*....|....
gi 520926077 198 LVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
5.66e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRgpshFNALemDGL--QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKaftga 80
Cdd:COG4152 1 MLELKGLTKRFGD----KTAV--DDVsfTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 lRQQV-----------------QMVFqdpYASLH--PLHRIRRSLREprqinglpfdeasLMasvEQVGLPGNILDRYpH 141
Cdd:COG4152 70 -RRRIgylpeerglypkmkvgeQLVY---LARLKglSKAEAKRRADE-------------WL---ERLGLGDRANKKV-E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 142 QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDmTVQAEIL-NLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGR 206
|
.
gi 520926077 221 V 221
Cdd:COG4152 207 K 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-221 |
7.13e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAglqRDW---QGEVQVLGQPLNAQKafTGALRQQVQM 87
Cdd:PRK11160 344 VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWdpqQGEILLNGQPIADYS--EAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 88 VFQDPyaslhplHRIRRSLREPRQINGLPFDEASLMASVEQVGLpGNILDRYP----------HQLSGGQRQRVAIVRAL 157
Cdd:PRK11160 419 VSQRV-------HLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 158 QLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHLcDRALLINQGRV 221
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-225 |
8.11e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGalrqqv 85
Cdd:PRK11248 4 ISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 qMVFQDpyASLHPLHRIRRSLREPRQINGLPFDE--ASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:PRK11248 74 -VVFQN--EGLLPWRNVQDNVAFGLQLAGVEKMQrlEIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLI--NQGRVERHL 225
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERL 213
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
28-221 |
8.97e-20 |
|
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: 87.69 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDP-------------YA 94
Cdd:TIGR03796 500 LTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP--REVLANSVAMVDQDIflfegtvrdnltlWD 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 95 SLHPLHRIRRSLREP---RQINGLPFdeaSLMASVEQVGlpGNildryphqLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:TIGR03796 578 PTIPDADLVRACKDAaihDVITSRPG---GYDAELAEGG--AN--------LSGGQRQRLEIARALVRNPSILILDEATS 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 172 ALDMTVQAEIlnlLQALRRdTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:TIGR03796 645 ALDPETEKII---DDNLRR-RGCTCIIVAHRLSTIRD-CDEIIVLERGKV 689
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
34-212 |
9.27e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 34 ECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQVLG------QPLNAQKAFTGALRQQVQMVFQDPyaslHPL-HRIRRSL 106
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSINRMN-DLNPEVTITGsivyngHNIYSPRTDTVDLRKEIGMVFQQP----NPFpMSIYENV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQINGLPfDEASLMASVEQVGLPGNILDRYPHQL-------SGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQA 179
Cdd:PRK14239 107 VYGLRLKGIK-DKQVLDEAVEKSLKGASIWDEVKDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG 185
|
170 180 190
....*....|....*....|....*....|...
gi 520926077 180 EILNLLQALRRDtgMTMILVSHDMNTVAHLCDR 212
Cdd:PRK14239 186 KIEETLLGLKDD--YTMLLVTRSMQQASRISDR 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-221 |
1.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqKAFTGALRQQVQMVFQDPYASLHPLHRIRRSLREPrqINgLPF 117
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGP--IN-LGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 118 DEASLMASVEQ----VGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTG 193
Cdd:PRK13652 110 DEETVAHRVSSalhmLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYG 188
|
170 180
....*....|....*....|....*...
gi 520926077 194 MTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13652 189 MTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-221 |
2.02e-19 |
|
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: 83.69 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN-AQKAFtgaLRQQVQMVF 89
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAW---LRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QDPYAslhplhrIRRSLREprqiNGLPFDEASLMASVEQVG-----------LP---GNILDRYPHQLSGGQRQRVAIVR 155
Cdd:cd03252 83 QENVL-------FNRSIRD----NIALADPGMSMERVIEAAklagahdfiseLPegyDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRrdTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
28-221 |
2.86e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA----QKAFTGALRQQVQMVFQD------------ 91
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrQLARRLALLPQHHLTPEGitvrelvaygrs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 92 PYASLHPlhriRRSLReprqinglpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:PRK11231 103 PWLSLWG----RLSAE----------DNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 172 ALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11231 168 YLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
33-221 |
3.13e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.44 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 33 GECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQplnaqkafTGALRQQVQMvfqdpyaslhPLHRIRRSLR----- 107
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--------DGQLRDLYAL----------SEAERRRLLRtewgf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 ---EPRQinGLPFDEAS-------LMAS---------------VEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPK 162
Cdd:PRK11701 94 vhqHPRD--GLRMQVSAggnigerLMAVgarhygdiratagdwLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 163 LLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-221 |
3.69e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 83.05 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPsHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqKAFT-GALRQQVQMVF 89
Cdd:cd03253 6 VTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTlDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QD----------------PYASLHPLHRIRRSLREPRQINGLPFDEASLmasVEQVGLpgnildryphQLSGGQRQRVAI 153
Cdd:cd03253 82 QDtvlfndtigynirygrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTI---VGERGL----------KLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 154 VRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRrdTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-221 |
3.81e-19 |
|
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: 82.66 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgaLRQQVQMVFQDPYAslhplhrIRRSLR 107
Cdd:cd03254 24 FSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS--LRSMIGVVLQDTFL-------FSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMASVEQVG-------LPgNILDRYP----HQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGahdfimkLP-NGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 177 VQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03254 174 TEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-221 |
4.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAfTGALRQQVQMVFQDPYaslhplHRIRRSLR 107
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN-LWDIRNKAGMVFQNPD------NQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 E------PRQInGLPFDE--ASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQA 179
Cdd:PRK13633 104 EedvafgPENL-GIPPEEirERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520926077 180 EILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
28-221 |
4.60e-19 |
|
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: 82.83 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGlqRDWQG---EVQVLGQPLNAQKAFtgALRQQVQMVfqdpYASLHplHRIRR 104
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTygnDVRLFGERRGGEDVW--ELRKRIGLV----SPALQ--LRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SL-----------------REPRQInglpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLD 167
Cdd:COG1119 94 DEtvldvvlsgffdsiglyREPTDE-----QRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 520926077 168 EPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
28-233 |
5.21e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDPYASL----------- 96
Cdd:COG4604 22 LTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP--SRELAKRLAILRQENHINSrltvrelvafg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 -HPLHRIRRSLREPRQInglpfDEAslmasVEQVGLpGNILDRYPHQLSGGQRQR--VAIVRALQLNPKLLllDEPTSAL 173
Cdd:COG4604 100 rFPYSKGRLTAEDREII-----DEA-----IAYLDL-EDLADRYLDELSGGQRQRafIAMVLAQDTDYVLL--DEPLNNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 174 DMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDR--AL----LINQGRVERHLDRAVLGEL 233
Cdd:COG4604 167 DMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHivAMkdgrVVAQGTPEEIITPEVLSDI 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-219 |
5.37e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLqrdW---QGEVqvlgqplnaqkaftgALRQQVQMVF--QDPYAslh 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL---WpygSGRI---------------ARPAGARVLFlpQRPYL--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 98 PLHRIRRSLREPRQINglPFDEASLMASVEQVGLPG-----NILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:COG4178 438 PLGTLREALLYPATAE--AFSDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 173 LDMTVQAEILNLLQALRRDTgmTMILVSHDmNTVAHLCDRALLINQG 219
Cdd:COG4178 516 LDEENEAALYQLLREELPGT--TVISVGHR-STLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
30-221 |
8.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKaFTgALRQQVQMVFQDP----YASLhplhrIRRS 105
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FE-KLRKHIGIVFQNPdnqfVGSI-----VKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPFDEasLMASVEQVGLPGNILDRY---PHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEIL 182
Cdd:PRK13648 105 VAFGLENHAVPYDE--MHRRVSEALKQVDMLERAdyePNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 183 NLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-221 |
9.23e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQVLGQPLNAQKAFTGALR-----QQvqmvfQDPYASLHPLHRIR 103
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHraylsQQ-----QTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLREPRQINGlpfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRV-------AIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:PRK03695 92 LHQPDKTRTEA---VASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 177 VQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-202 |
1.00e-18 |
|
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: 84.33 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPlnAQKAFTGALRQQVQMVFQDPyaslhplHRIRRSLR 107
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP--VSSLDQDEVRRRVSVCAQDA-------HLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:TIGR02868 427 ENLRLARPDATDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*.
gi 520926077 177 VQAEILNLLQALrrDTGMTMILVSHD 202
Cdd:TIGR02868 506 TADELLEDLLAA--LSGRTVVLITHH 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-221 |
1.01e-18 |
|
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: 84.41 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTFKRGPSHfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALRQQ 84
Cdd:TIGR01193 473 DIVINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 85 VQMVFQDPY---ASL--HPLHRIRRSLREPRQINGLPFdeASLMASVEQVGLP-GNILDRYPHQLSGGQRQRVAIVRALQ 158
Cdd:TIGR01193 550 INYLPQEPYifsGSIleNLLLGAKENVSQDEIWAACEI--AEIKDDIENMPLGyQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 159 LNPKLLLLDEPTSALDMTVQAEILNLLQALrrdTGMTMILVSHDMNtVAHLCDRALLINQGRV 221
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNL---QDKTIIFVAHRLS-VAKQSDKIIVLDHGKI 686
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
1.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQV------LGQPLNAQKAFTGALRQQVQMVFQDPyaSL 96
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVegrvefFNQNIYERRVNLNRLRRQVSMVHPKP--NL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 HPLHRIRRSLREPRQINGLPfdEASLMASVEQVGLPGNILDRYPHQ-------LSGGQRQRVAIVRALQLNPKLLLLDEP 169
Cdd:PRK14258 100 FPMSVYDNVAYGVKIVGWRP--KLEIDDIVESALKDADLWDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520926077 170 TSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCD 211
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-221 |
1.92e-18 |
|
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: 79.90 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNALEMDGLQ--IKAGECFGLIGGSGSGKSTLLRVLAGlQRDW---QGEVQVLGQPLNAQk 75
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSgkAKPGELTAIMGPSGAGKSTLLNALAG-RRTGlgvSGEVLINGRPLDKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 76 aftgALRQQVQMVFQDPYasLHPLHRIRRSLREPRQINGlpfdeaslmasveqvglpgnildryphqLSGGQRQRVAIVR 155
Cdd:cd03213 79 ----SFRKIIGYVPQDDI--LHPTLTVRETLMFAAKLRG----------------------------LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 156 ALQLNPKLLLLDEPTSALDmTVQAeiLNLLQALRR--DTGMTMILVSHD-MNTVAHLCDRALLINQGRV 221
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLD-SSSA--LQVMSLLRRlaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-221 |
1.99e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN--AQKAFTGALRQQVQMVFQDpyASLHPLHRIRRS 105
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRRKKIAMVFQS--FALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPFDEASLMA--SVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:PRK10070 127 TAFGMELAGINAEERREKAldALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-221 |
2.03e-18 |
|
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: 80.59 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQ 83
Cdd:cd03248 12 VKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE--HKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPYASlhplhriRRSLRE--PRQINGLPFDEasLMASVEQVGLPGNI----------LDRYPHQLSGGQRQRV 151
Cdd:cd03248 89 KVSLVGQEPVLF-------ARSLQDniAYGLQSCSFEC--VKEAAQKAHAHSFIselasgydteVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-222 |
2.03e-18 |
|
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: 80.65 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 12 TFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ---PLNAQKAFTGAL--RQQVQ 86
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGLGGGFNPELtgRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 87 MVfqdpyASLHplhrirrslreprqinGLPFDE-ASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd03220 107 LN-----GRLL----------------GLSRKEiDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-220 |
2.68e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.78 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 25 MDGL--QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgalRQQVQMVFQdpYASLHPLHRI 102
Cdd:PRK13537 23 VDGLsfHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---RQRVGVVPQ--FDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 103 RRSLREPRQINGLPFDEA-SLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEI 181
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAArALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 182 LNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK13537 178 WERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
2.97e-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: 82.93 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKrgpsHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVL---------------- 67
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 68 --GQP---------------LNAQKAFTGALRQQVQMVFQDPYAsLHPLHRIRRSLREPRQINGLPFDEASLMAS--VEQ 128
Cdd:TIGR03269 77 kvGEPcpvcggtlepeevdfWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVdlIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 129 VGLPGNILdRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAH 208
Cdd:TIGR03269 156 VQLSHRIT-HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|...
gi 520926077 209 LCDRALLINQGRV 221
Cdd:TIGR03269 235 LSDKAIWLENGEI 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-221 |
3.76e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.07 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkafTGALRQQ--VQMVFQDpYAsLHPLHRIRRS 105
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV------THRSIQQrdICMVFQS-YA-LFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LREPRQINGLPFDE--ASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:PRK11432 99 VGYGLKMLGVPKEErkQRVKEALELVDLAG-FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11432 178 KIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
5.31e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.42 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTfkrgPSHFNALEMDGL--QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAft 78
Cdd:PRK13536 37 MSTVAIDLAGVS----KSYGDKAVVNGLsfTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 79 gALRQQVQMVFQdpYASLHPLHRIRRSL--------REPRQInglpfdEASLMASVEQVGLPgNILDRYPHQLSGGQRQR 150
Cdd:PRK13536 111 -LARARIGVVPQ--FDNLDLEFTVRENLlvfgryfgMSTREI------EAVIPSLLEFARLE-SKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 151 VAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
6.13e-18 |
|
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: 79.40 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAV-DINHLTVTFK---RGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVL--GQPLN-A 73
Cdd:COG4778 1 MTTLlEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 74 QkaftgalrqqvqmvfqdpyASLHPLHRIRRS--------LR------------EPRQINGLPFDEASLMAS--VEQVGL 131
Cdd:COG4778 81 Q-------------------ASPREILALRRRtigyvsqfLRviprvsaldvvaEPLLERGVDREEARARARelLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 132 PGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCD 211
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVAD 220
|
....*....
gi 520926077 212 RALLINQGR 220
Cdd:COG4778 221 RVVDVTPFS 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-215 |
7.35e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG--------QPLNAQKAFTGALRQQVQMVFqdpYASLHPL 99
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpQRSEVPDSLPLTVRDLVAMGR---WARRGLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSlreprqinglpfDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQA 179
Cdd:NF040873 90 RRLTRD------------DRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 520926077 180 EILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALL 215
Cdd:NF040873 157 RIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-221 |
1.63e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 17 PSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGaLRQQVQMVFQDPYASL 96
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQG-IRKLVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 hplhrIRRSLRE-----PRQINGLPFDEASLM-ASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:PRK13644 91 -----VGRTVEEdlafgPENLCLPPIEIRKRVdRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 171 SALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVaHLCDRALLINQGRV 221
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-220 |
2.00e-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: 80.64 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFkrgpSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL--QRDWQGEVQVLGQPLNAQ------K 75
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASnirdteR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 76 AFTGALRQQVQMVfqdpyASLHPLHRIrrSLREPRQINGLPFDEASLM----ASVEQVGLPGNILDRYPHQLSGGQRQRV 151
Cdd:TIGR02633 78 AGIVIIHQELTLV-----PELSVAENI--FLGNEITLPGGRMAYNAMYlrakNLLRELQLDADNVTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-235 |
2.24e-17 |
|
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: 80.56 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEV------------QVLGQplnaqkaFTGALRQQVQMV------- 88
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGR-------HIGYLPQDVELFdgtiaen 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 89 ---FQDPyaslhplhrirrslrEPRQINglpfdEASLMASVEQ--VGLPgnilDRY-------PHQLSGGQRQRVAIVRA 156
Cdd:COG4618 426 iarFGDA---------------DPEKVV-----AAAKLAGVHEmiLRLP----DGYdtrigegGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 157 LQLNPKLLLLDEPTSALDmtVQAEiLNLLQALR--RDTGMTMILVSHDMNTVAHlCDRALLINQGRVERHLDRA-VLGEL 233
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLD--DEGE-AALAAAIRalKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDeVLARL 557
|
..
gi 520926077 234 AG 235
Cdd:COG4618 558 AR 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-223 |
2.26e-17 |
|
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: 80.53 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALRQQVQMVFQ 90
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 91 D------------PYASLH--PLHRIRRSLREPRQ---INGLP--FDEaslmasveQVGLPGNildryphQLSGGQRQRV 151
Cdd:TIGR02203 414 DvvlfndtianniAYGRTEqaDRAEIERALAAAYAqdfVDKLPlgLDT--------PIGENGV-------LLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520926077 152 AIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGR-VER 223
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRiVER 548
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-223 |
3.68e-17 |
|
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: 77.27 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHltVTFKRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqKAFT-GALR 82
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTlASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 83 QQVQMVFQDPY---ASLHPLHRIRRSLREPRQInglpfDEASLMASVEQV------GLPGNILDRyPHQLSGGQRQRVAI 153
Cdd:cd03251 76 RQIGLVSQDVFlfnDTVAENIAYGRPGATREEV-----EEAARAANAHEFimelpeGYDTVIGER-GVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 154 VRALQLNPKLLLLDEPTSALD----MTVQAEILNLLQalrrdtGMTMILVSHDMNTVAHlCDRALLINQGR-VER 223
Cdd:cd03251 150 ARALLKDPPILILDEATSALDteseRLVQAALERLMK------NRTTFVIAHRLSTIEN-ADRIVVLEDGKiVER 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-221 |
6.79e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 2 SAVDINHLTVTFKrgpsHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL---QRDWQGEVQVLGQPLNAQ---- 74
Cdd:PRK09984 3 TIIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 75 ------KAFTGALRQQVQMVFqdpyaslhplhriRRSLREPRQINGL--------------PFDEASLMASVEQVGLPgn 134
Cdd:PRK09984 79 rdirksRANTGYIFQQFNLVN-------------RLSVLENVLIGALgstpfwrtcfswftREQKQRALQALTRVGMV-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 135 ildRYPHQ----LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLC 210
Cdd:PRK09984 144 ---HFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYC 220
|
250
....*....|.
gi 520926077 211 DRALLINQGRV 221
Cdd:PRK09984 221 ERIVALRQGHV 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-223 |
1.02e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQrDW------QGEVQVLGQPLNAQKAFTGALRQQVQMVFQDPYaslhPLHR 101
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLN-DLipgfrvEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPN----PFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 -IRRSLREPRQINGLPFDEASLMA-SVEQVGLPGNILDRYPHQ---LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:PRK14243 106 sIYDNIAYGARINGYKGDMDELVErSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 177 VQAEILNLLQALRRDtgMTMILVSHDMNTVAHLCDRALLINQGRVER 223
Cdd:PRK14243 186 STLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-220 |
1.07e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGL--QRDWQGEVQVLGQPLNAQ------KAFTGALRQQVQMVfqdPYASLhpL 99
Cdd:PRK13549 26 LKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASnirdteRAGIAIIHQELALV---KELSV--L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSlREPRQINGLPFDEASLMAS--VEQVGLPGNILDRYPHqLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTV 177
Cdd:PRK13549 101 ENIFLG-NEITPGGIMDYDAMYLRAQklLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 178 QAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK13549 179 TAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-221 |
1.56e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.65 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTllrVLAGLQRDW---QGEVQVLGQP---LNAQKaftgaLRQQVQMVFQDP---YASLhp 98
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKST---VVSLLERFYdptSGEILLDGVDirdLNLRW-----LRSQIGLVSQEPvlfDGTI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 99 LHRIRRSLREPRQingLPFDEASLMASVEQ--VGLPgnilDRY-----PH--QLSGGQRQRVAIVRALQLNPKLLLLDEP 169
Cdd:cd03249 94 AENIRYGKPDATD---EEVEEAAKKANIHDfiMSLP----DGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 520926077 170 TSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-223 |
1.96e-16 |
|
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: 77.77 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 27 GLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQK-----AFTGALRQQVQMvFQDPYASlhPLHR 101
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfgKHIGYLPQDVEL-FPGTVAE--NIAR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 IRRSLrEPRQINglpfdEASLMASVEQVglpgnILdRYPH-----------QLSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:TIGR01842 415 FGENA-DPEKII-----EAAKLAGVHEL-----IL-RLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520926077 171 SALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAhLCDRALLINQGRVER 223
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLG-CVDKILVLQDGRIAR 533
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-221 |
2.79e-16 |
|
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: 74.84 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA---QKaftgaLRQQVQMVFQDPYAslhplhrIRR 104
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglHD-----LRSRISIIPQDPVL-------FSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLREprqiNGLPFDEAS---LMASVEQVGL-------PGNILDRYPH---QLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:cd03244 93 TIRS----NLDPFGEYSdeeLWQALERVGLkefveslPGGLDTVVEEggeNLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 172 ALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:cd03244 169 SVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
28-221 |
5.84e-16 |
|
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: 74.25 E-value: 5.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFtgalrqqvqmvfqdpyaslhplHRIRRSLR 107
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH----------------------RIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 ---EPRQInglpFdeASLmaSVE---QVGLPGN------------ILDRYPH----------QLSGGQRQRVAIVRALQL 159
Cdd:COG0410 82 yvpEGRRI----F--PSL--TVEenlLLGAYARrdraevradlerVYELFPRlkerrrqragTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 160 NPKLLLLDEPTSALDMTVQAEILNLLQALRRdTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-223 |
6.30e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQV--------LGQPLNAQKAFTgaLRQQVQMVFQDPYASLHPL 99
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigyLPQEPPLDDDLT--VLDTVLDGDAELRALEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLREP----RQINGLP--FDEA---SLMASVEQV----GLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLL 166
Cdd:COG0488 97 EELEAKLAEPdedlERLAELQeeFEALggwEAEARAEEIlsglGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 167 DEPTSALDmtvqAEILNLLQA-LRRDTGmTMILVSHD---MNTVahlCDRALLINQGRVER 223
Cdd:COG0488 177 DEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSHDryfLDRV---ATRILELDRGKLTL 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-226 |
1.03e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAfTGALRQQVQMVFQDpyaslhpLHR 101
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST-TAALAAGVAIIYQE-------LHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 I-RRSLREPRQINGLP-----FDEASLMASV-EQVGLPGNILDryPHQ----LSGGQRQRVAIVRALQLNPKLLLLDEPT 170
Cdd:PRK11288 91 VpEMTVAENLYLGQLPhkggiVNRRLLNYEArEQLEHLGVDID--PDTplkyLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 171 SALDmtvQAEILNLLQALR--RDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLD 226
Cdd:PRK11288 169 SSLS---AREIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFD 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-220 |
1.10e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDpyasLHPLHRirrsLR 107
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLFSAVFTD----FHLFDQ----LL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRqinGLPFDEASLMASVEQVGLP-------GNILDRyphQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:PRK10522 414 GPE---GKPANPALVEKWLERLKMAhkleledGRISNL---KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520926077 181 ILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLINQGR 220
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-221 |
1.27e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRD-----WQGEVQVLGQPLNAQKAFTgALRQQVQMVFQDPyaSLHPLHRIRRSLREPRQI 112
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVL-EFRRRVGMLFQRP--NPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 113 NGLPFDE--ASLMASVEQVGLPGNILDRY---PHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:PRK14271 129 KLVPRKEfrGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 188 LRRDtgMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK14271 209 LADR--LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
3.86e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRG-PSHFNALemDG--LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGA 80
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRAL--DGlnLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 lrQQVQMVFQDPYA------------SLHPLHRIRRSLRePRQINGlpfDEASLMASVEQVGLpG--NILDRYPHQLSGG 146
Cdd:COG1101 80 --KYIGRVFQDPMMgtapsmtieenlALAYRRGKRRGLR-RGLTKK---RRELFRELLATLGL-GleNRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-201 |
8.37e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTgalrqqvQMVFQDPYASLHPLHRIRRSLREP 109
Cdd:PRK13539 25 LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE-------ACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 110 RQINGLpfDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQAlR 189
Cdd:PRK13539 98 AAFLGG--EELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-H 173
|
170
....*....|..
gi 520926077 190 RDTGMTMILVSH 201
Cdd:PRK13539 174 LAQGGIVIAATH 185
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
28-221 |
1.06e-14 |
|
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: 70.63 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALR-----QQVQMVFqdpyaslhPLHRI 102
Cdd:TIGR03410 21 LEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgiayvPQGREIF--------PRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 103 RRSLR-----EPRQINGLPFDEASLMASVEQVglpgniLDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTV 177
Cdd:TIGR03410 93 EENLLtglaaLPRRSRKIPDEIYELFPVLKEM------LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 178 QAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-221 |
1.62e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQplNAQKAFTGALRQQVQMVFQDPYAslhplhrIRRSLREP 109
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT--DIRTVTRASLRRNIAVVFQDAGL-------FNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 110 RQINGLPFDEASLMASVEQV-----------GLPGNILDRyPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:PRK13657 429 IRVGRPDATDEEMRAAAERAqahdfierkpdGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 520926077 179 AEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK13657 508 AKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-220 |
1.75e-14 |
|
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: 69.42 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPSHFN-ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAG-LQRDwQGEVQVLGQplnaqkaftgal 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKL-SGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 rqqVQMVFQDPYAslhplhrIRRSLREprqiN---GLPFDEASLMASVEQVGLpGNILDRYPHQ-----------LSGGQ 147
Cdd:cd03250 68 ---IAYVSQEPWI-------QNGTIRE----NilfGKPFDEERYEKVIKACAL-EPDLEILPDGdlteigekginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 148 RQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN--LLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGR 220
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-224 |
3.37e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA-QKAFTGALRQQVQMVFQDP--YASLHPLHRIRR 104
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYTVRKRMSMLFQSGalFTDMNVFDNVAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLREPRQINGlPFDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNL 184
Cdd:PRK11831 108 PLREHTQLPA-PLLHSTVMMKLEAVGLRG-AAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520926077 185 LQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:PRK11831 186 ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-221 |
3.58e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaQKAFTGALRQQVQMVFQDPYA----SLHPLHRIR 103
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--QHYASKEVARRIGLLAQNATTpgdiTVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLREPRQINGLPFDEASLMASVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 184 LLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-221 |
4.85e-14 |
|
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: 68.84 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDW---QGEVQVLGQPLNAQKaftgaLRQQVQMVFQDPYasLHPLHRIRR 104
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQ-----FQKCVAYVRQDDI--LLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SL------REPRqinglPFDEASLMASVEQVGLP----GNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD 174
Cdd:cd03234 101 TLtytailRLPR-----KSSDAIRKKRVEDVLLRdlalTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 175 -MTVqaeiLNLLQALRR--DTGMTMILVSHDMNT-VAHLCDRALLINQGRV 221
Cdd:cd03234 176 sFTA----LNLVSTLSQlaRRNRIVILTIHQPRSdLFRLFDRILLLSSGEI 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-221 |
6.21e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQR---DWQGEVQVLGQPLNAQKA------------FTGALRQQVQMVFQdpyA 94
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMraisayvqqddlFIPTLTVREHLMFQ---A 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 95 SLHpLHRiRRSLREPRQINGLPFDEASLM-ASVEQVGLPGNIldrypHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSAL 173
Cdd:TIGR00955 125 HLR-MPR-RVTKKEKRERVDEVLQALGLRkCANTRIGVPGRV-----KGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 174 DMTVQAEILNLLQALrRDTGMTMILVSHD-MNTVAHLCDRALLINQGRV 221
Cdd:TIGR00955 198 DSFMAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-223 |
8.63e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 5 DINHLTVTF----KRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGA 80
Cdd:PRK11176 341 DIEFRNVTFtypgKEVP----ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMV------FQDPYASLHPLHRIRRSLREprQInglpfDEASLMA-SVEQVGLPGNILDRYPHQ----LSGGQRQ 149
Cdd:PRK11176 415 LRNQVALVsqnvhlFNDTIANNIAYARTEQYSRE--QI-----EEAARMAyAMDFINKMDNGLDTVIGEngvlLSGGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520926077 150 RVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGR-VER 223
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEiVER 559
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-201 |
1.12e-13 |
|
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: 66.41 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHFNALEMDgLQIKAGECFGLIGGSGSGKSTLLRVLAGLqrdW---QGEVQVLGQPlnaqkaftgalrqQVQM 87
Cdd:cd03223 6 LSLATPDGRVLLKDLS-FEIKPGDRLLITGPSGTGKSSLFRALAGL---WpwgSGRIGMPEGE-------------DLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 88 VFQDPYASlhplhriRRSLREprQINglpfdeaslmasveqvglpgnildrYP--HQLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd03223 69 LPQRPYLP-------LGTLRE--QLI-------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALrrdtGMTMILVSH 201
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-204 |
1.22e-13 |
|
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: 67.13 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 27 GLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgalRQQVQMVFQDPYASLHPLHRIRRSL 106
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-----SIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQINGlpfDEASLMAsVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQ 186
Cdd:cd03231 95 RFWHADHS---DEQVEEA-LARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*...
gi 520926077 187 ALRRDTGMTMILVSHDMN 204
Cdd:cd03231 170 GHCARGGMVVLTTHQDLG 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-221 |
2.35e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 11 VTFKRGPSHF---NALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqkaftgalRQQVQM 87
Cdd:PRK11614 6 LSFDKVSAHYgkiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---------DWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 88 VFQDPYASLHPLHRI--RRSLREPRQINGLPFDEASLMASVEQV-GLPGNILDRYPHQ---LSGGQRQRVAIVRALQLNP 161
Cdd:PRK11614 77 IMREAVAIVPEGRRVfsRMTVEENLAMGGFFAERDQFQERIKWVyELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-220 |
2.65e-13 |
|
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: 64.78 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGP--SHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVlgqplnaqkaftgal 81
Cdd:cd03221 1 IELENLSKTYGGKLllKDIS------LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 rqqvqmvfqdpyaslhplhrirrslreprqinglpfdeaslmASVEQVGlpgnildrYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:cd03221 60 ------------------------------------------GSTVKIG--------YFEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 162 KLLLLDEPTSALDM-TVQAeilnLLQALRRDTGmTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:cd03221 90 NLLLLDEPTNHLDLeSIEA----LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-208 |
2.82e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQQVQMVFQDP--YASLHPLHRIRRS 105
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD---EYHQDLLYLGHQPgiKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 LReprqINGlPFDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLL 185
Cdd:PRK13538 99 QR----LHG-PGDDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170 180
....*....|....*....|...
gi 520926077 186 QALRRDTGMTMILVSHDMNTVAH 208
Cdd:PRK13538 173 AQHAEQGGMVILTTHQDLPVASD 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-221 |
4.44e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQVLGQPLNAQKAftGALRQQVQMVFQDPyaslhplHRIRRSLR 107
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP--ESWRKHLSWVGQNP-------QLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMASVEQVGLpGNILDRYPH-----------QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWV-SEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 177 VQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PRK11174 520 SEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-223 |
4.61e-13 |
|
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: 67.92 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA--QKAftgaLRQQVQMVFQDP------------Y-- 93
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtQAS----LRAAIGIVPQDTvlfndtiayniaYgr 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 94 --------------ASLHPLhrirrslreprqINGLP--FDeaslmASVEQVGLpgnildryphQLSGGQRQRVAIVRAL 157
Cdd:COG5265 457 pdaseeeveaaaraAQIHDF------------IESLPdgYD-----TRVGERGL----------KLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 158 QLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGR-VER 223
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRiVER 573
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-223 |
4.62e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRGP---SHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftG 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlvlQNIN------LSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH--S 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQDPYAslhplhrirrsLREPRQIN---GLPFDEASLMASVEQV-------GLPGNILDRYPHQ---LSGG 146
Cdd:PRK10790 412 VLRQGVAMVQQDPVV-----------LADTFLANvtlGRDISEEQVWQALETVqlaelarSLPDGLYTPLGEQgnnLSVG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 147 QRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTgmTMILVSHDMNTVAHlCDRALLINQGR-VER 223
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQaVEQ 555
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-206 |
7.39e-13 |
|
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: 65.07 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgaLRQQvQMVFQDPYASLHPLHRIRRSLREP 109
Cdd:TIGR01189 23 LNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD----EPHE-NILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 110 RQINGlpFDEASLMASVEQVGLPGnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALR 189
Cdd:TIGR01189 98 AAIHG--GAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHL 174
|
170
....*....|....*..
gi 520926077 190 RDTGMTMILVSHDMNTV 206
Cdd:TIGR01189 175 ARGGIVLLTTHQDLGLV 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-225 |
8.19e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVqVLGQPLNaqkafTGALRQQVqmvfqdpyASLHPLHRIRRSLR 107
Cdd:COG0488 336 LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK-----IGYFDQHQ--------EELDPDKTVLDELR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EprqinGLP-FDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM-TVQAeilnLL 185
Cdd:COG0488 402 D-----GAPgGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520926077 186 QALRRDTGmTMILVSHDMNTVAHLCDRALLINQGRVERHL 225
Cdd:COG0488 473 EALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-211 |
1.07e-12 |
|
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: 65.47 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 21 NALEMDGLQI-KAGECFGLIGGSGSGKSTLLRVLAGLQR----------DWQGEVQVL-GQPLnaQKAFTGALRQQVQMV 88
Cdd:cd03236 13 NSFKLHRLPVpREGQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppDWDEILDEFrGSEL--QNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 89 FQDPYASLHPLH---RIRRSLREPRQINGLpfDEAslmasVEQVGLPgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd03236 91 VKPQYVDLIPKAvkgKVGELLKKKDERGKL--DEL-----VDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 520926077 166 LDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCD 211
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSD 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-219 |
1.12e-12 |
|
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: 66.96 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkaFTGALRQQVQMVFQDPYASLHPLHRIRRSLREP 109
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 110 RQINGLPFDEASLMA--SVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVAnwSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190
....*....|....*....|....*....|..
gi 520926077 188 LRRDtGMTMILVSHDMNTVAHLCDRALLINQG 219
Cdd:TIGR01257 2116 IIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-224 |
1.85e-12 |
|
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: 63.97 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkaftgalrqqvqmvfqdpyaSLHPLHRIRRSL-- 106
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----------------------STIPLEDLRSSLti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 --REPRQINGL------PFDEAS---LMASVEqVGLPGNildryphQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:cd03369 87 ipQDPTLFSGTirsnldPFDEYSdeeIYGALR-VSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 176 TVQAEIlnllQALRRD--TGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:cd03369 159 ATDALI----QKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEY 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-214 |
2.76e-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: 64.35 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG-----QPLNAQKAFTGALRQQVQMVFQDPYAslH 97
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKPQYIKADYEGTVRDLLSSITKDFYT--H 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 98 PLHRIrrSLREPRQINGlpfdeaslmasveqvglpgnILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDmtV 177
Cdd:cd03237 93 PYFKT--EIAKPLQIEQ--------------------ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--V 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520926077 178 QAEILnLLQALRR---DTGMTMILVSHDMNTVAHLCDRAL 214
Cdd:cd03237 149 EQRLM-ASKVIRRfaeNNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-228 |
2.76e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqKAFTGALRQQVQMVFQDpyaslhplhriRR--- 104
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI-RSPRDAIRAGIAYVPED-----------RKgeg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 -----SLRE-------PRQINGLPFDEASLMASVEQVglpgniLDRY------PHQ----LSGGQRQRVAIVRALQLNPK 162
Cdd:COG1129 341 lvldlSIREnitlaslDRLSRGGLLDRRRERALAEEY------IKRLriktpsPEQpvgnLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 163 LLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDRA 228
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-224 |
3.38e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGL-QRDW------QGEVQVLgqPLNAQ-KAFTGALRQQVQMVFQ-DPYASLHP 98
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAgniiidDEDISLL--PLHARaRRGIGYLPQEASIFRRlSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 99 LHRIRRSL-REPRQinglpfDEAS-LMASVEQVGLPGNIldryPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:PRK10895 102 VLQIRDDLsAEQRE------DRANeLMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520926077 177 VQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERH 224
Cdd:PRK10895 172 SVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAH 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-228 |
3.65e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAfTGALRQQVQMVFQDPYA-SLHPLHRIRR-- 104
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP-RDAIRAGIMLCPEDRKAeGIIPVHSVADni 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 --SLREPRQINGLPFDEASLMASVEQVGLPGNILDRYPHQ----LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQ 178
Cdd:PRK11288 353 niSARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 179 AEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDRA 228
Cdd:PRK11288 433 HEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELARE 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-219 |
5.34e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFkrGPSHfnALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLN------AQKAF 77
Cdd:PRK09700 6 ISMAGIGKSF--GPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhklAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 78 TGALRQQVQM-----VFQDPYASLHPLhrirrslrepRQINGLPFDEASLMASVEQ-----VGLPGNiLDRYPHQLSGGQ 147
Cdd:PRK09700 82 IGIIYQELSVideltVLENLYIGRHLT----------KKVCGVNIIDWREMRVRAAmmllrVGLKVD-LDEKVANLSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 148 RQRVAIVRALQLNPKLLLLDEPTSALdmtVQAEILNLLQALR--RDTGMTMILVSHDMNTVAHLCDRALLINQG 219
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-208 |
7.73e-12 |
|
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: 62.73 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAFTGALRQQVQMVfqdpYASLHPLhrIRRSLR 107
Cdd:cd03290 22 IRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA----YAAQKPW--LLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPFDEASLMASVEQVGLPGNIlDRYPH-----------QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM- 175
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 520926077 176 ----TVQAEILNLLQALRRdtgmTMILVSHDMNTVAH 208
Cdd:cd03290 175 lsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-221 |
8.11e-12 |
|
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: 64.65 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 37 GLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQkafTGALRQQVQMVFQDPYAsLHPLhRIRRSLREPRQINGLP 116
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGMCPQHNIL-FHHL-TVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 117 FDEASLM--ASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLqaLRRDTGM 194
Cdd:TIGR01257 1035 WEEAQLEmeAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGR 1111
|
170 180
....*....|....*....|....*..
gi 520926077 195 TMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:TIGR01257 1112 TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-220 |
2.01e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 27 GLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNA----QKAFTGALR--QQVQ-----------MVF 89
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghQIARMGVVRtfQHVRlfremtvienlLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QDPY------ASLHPLHRIRRSLREPrqinglpFDEASLMasVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:PRK11300 105 QHQQlktglfSGLLKTPAFRRAESEA-------LDRAATW--LERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 164 LLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-221 |
3.16e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgALRQQVQmvfqdpYAS------------ 95
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI---ATRRRVG------YMSqafslygeltvr 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 ----LHP-LHRIRRSLREPRqinglpFDEAslmasVEQVGLpGNILDRYPHQLSGGQRQR----VAIVRALQLNPKllll 166
Cdd:NF033858 358 qnleLHArLFHLPAAEIAAR------VAEM-----LERFDL-ADVADALPDSLPLGIRQRlslaVAVIHKPELLIL---- 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 167 DEPTS-----ALDMTVQaeilnLLQALRRDTGMTmILVS-HDMNTvAHLCDRALLINQGRV 221
Cdd:NF033858 422 DEPTSgvdpvARDMFWR-----LLIELSREDGVT-IFIStHFMNE-AERCDRISLMHAGRV 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-220 |
3.93e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAqKAFTGALRQQVQMVFQDpyaslhpLHR 101
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-KSSKEALENGISMVHQE-------LNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 IR-RSL-------REPRQinGLPFDEASLMASVEQVGLPGNIlDRYPHQ----LSGGQRQRVAIVRALQLNPKLLLLDEP 169
Cdd:PRK10982 85 VLqRSVmdnmwlgRYPTK--GMFVDQDKMYRDTKAIFDELDI-DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 520926077 170 TSALdmtVQAEILNLLQALR--RDTGMTMILVSHDMNTVAHLCDRALLINQGR 220
Cdd:PRK10982 162 TSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-211 |
5.79e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 21 NALEMDGLQI-KAGECFGLIGGSGSGKSTLLRVLAGLQR----DWQGEV---QVLgqplnaqKAFTGAlrqQVQMVFQDP 92
Cdd:PRK13409 86 NGFKLYGLPIpKEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPswdEVL-------KRFRGT---ELQNYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 93 YA-SLHPLHRIRRSLREPRQING------LPFDEASLMAS-VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLL 164
Cdd:PRK13409 156 YNgEIKVVHKPQYVDLIPKVFKGkvrellKKVDERGKLDEvVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520926077 165 LLDEPTSALDMTvqaEILNLLQALRRDT-GMTMILVSHDMNTVAHLCD 211
Cdd:PRK13409 235 FFDEPTSYLDIR---QRLNVARLIRELAeGKYVLVVEHDLAVLDYLAD 279
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-221 |
5.96e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKaftgalrqqvqmvfqdpyaslhPLHRIRRS-- 105
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----------------------TAQRLARGlv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 -LREPRQINGLpFDEASLMASVeqVGLPGN-------------ILDRYPHQ--------------LSGGQRQRVAIVRAL 157
Cdd:PRK15439 342 yLPEDRQSSGL-YLDAPLAWNV--CALTHNrrgfwikparenaVLERYRRAlnikfnhaeqaartLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 158 QLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-202 |
6.19e-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: 61.49 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 37 GLIGGSGSGKSTLLRVLAGLQRDWQGE--------VQVLGQ--PLNAQKAftgaLRQQVQMVFQDPYASLHPLHRIRRSL 106
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgikVGYLPQepQLDPTKT----VRENVEEGVAEIKDALDRFNEISAKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REP-RQINGLPFDEASLMASVEQVGlpGNILD----------RYP------HQLSGGQRQRVAIVRALQLNPKLLLLDEP 169
Cdd:TIGR03719 111 AEPdADFDKLAAEQAELQEIIDAAD--AWDLDsqleiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
170 180 190
....*....|....*....|....*....|....
gi 520926077 170 TSALDmtvqAE-ILNLLQALRRDTGmTMILVSHD 202
Cdd:TIGR03719 189 TNHLD----AEsVAWLERHLQEYPG-TVVAVTHD 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-218 |
6.62e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQvlgqplNAQKAFTGALRQQVQMvfqDPYASLhplhRIRRSLR 107
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQKLYL---DTTLPL----TVNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINglpfdEASLMASVEQVGlPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQA 187
Cdd:PRK09544 92 LRPGTK-----KEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQ 165
|
170 180 190
....*....|....*....|....*....|.
gi 520926077 188 LRRDTGMTMILVSHDMNTVAHLCDRALLINQ 218
Cdd:PRK09544 166 LRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-235 |
9.00e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRGPshfnALEMDGLQIKAGECFGLIGGSGSGKSTLLrvlAGLQRDW---QGEVQVLGQPLNAQK--AF 77
Cdd:PRK10789 315 DVNIRQFTYPQTDHP----ALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHFdvsEGDIRFHDIPLTKLQldSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 78 TG--ALRQQVQMVFQDPYASLHPLHRIRRSlrePRQInglpfDEASLMASVEQvglpgNILdRYPH-----------QLS 144
Cdd:PRK10789 388 RSrlAVVSQTPFLFSDTVANNIALGRPDAT---QQEI-----EHVARLASVHD-----DIL-RLPQgydtevgergvMLS 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 145 GGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRdtGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQR 530
|
250
....*....|.
gi 520926077 225 LDRAVLGELAG 235
Cdd:PRK10789 531 GNHDQLAQQSG 541
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-222 |
1.41e-10 |
|
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: 60.73 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQDPYAslhplhrIRRSLR 107
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLHDLRFKITIIPQDPVL-------FSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqINGLPFDEAS---LMASVEQVGLPGNIL---DRYPHQ-------LSGGQRQRVAIVRALQLNPKLLLLDEPTSALD 174
Cdd:TIGR00957 1378 ----MNLDPFSQYSdeeVWWALELAHLKTFVSalpDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 175 MtvqaEILNLLQALRRDT--GMTMILVSHDMNTVAHLCdRALLINQGRVE 222
Cdd:TIGR00957 1454 L----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-224 |
1.88e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 8 HLTVtFKRGPSHFNALEmdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRD--------WQGEVQVLGQPLNAQKAFTG 79
Cdd:PRK13547 6 HLHV-ARRHRAILRDLS---LRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 A-----LRQQVQMVFQ---DPYASLHPLHRIRRSLREPRQINGLPFDEASLMASVEQVGlpgnildRYPHQLSGGQRQRV 151
Cdd:PRK13547 82 ArlravLPQAAQPAFAfsaREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVG-------RDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 152 AIVRA---------LQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK13547 155 QFARVlaqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
..
gi 520926077 223 RH 224
Cdd:PRK13547 235 AH 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-202 |
2.23e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 37 GLIGGSGSGKSTLLRVLAGLQRDWQGEVQV--------LGQ--PLNAQKAftgaLRQQVQMVFQDPYASLHPLHRIRRSL 106
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPapgikvgyLPQepQLDPEKT----VRENVEEGVAEVKAALDRFNEIYAAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQinglPFDEasLMAsvEQVGLPgNILD------------------RYPH------QLSGGQRQRVAIVRALQLNPK 162
Cdd:PRK11819 113 AEPDA----DFDA--LAA--EQGELQ-EIIDaadawdldsqleiamdalRCPPwdakvtKLSGGERRRVALCRLLLEKPD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 520926077 163 LLLLDEPTSALDmtvqAE-ILNLLQALRRDTGmTMILVSHD 202
Cdd:PRK11819 184 MLLLDEPTNHLD----AEsVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-201 |
2.50e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKAftgalRQQVQMVFQDPYASLHPLHRIRRSLR 107
Cdd:PRK13540 22 FHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC-----TYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQIN--GLPFDEASLMASVeqvglpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLL 185
Cdd:PRK13540 97 YDIHFSpgAVGITELCRLFSL------EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*.
gi 520926077 186 QALRRDTGmTMILVSH 201
Cdd:PRK13540 171 QEHRAKGG-AVLLTSH 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-221 |
2.51e-10 |
|
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: 58.32 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkaftgalrqqvqmvfqdpyaSLHPLHRirrslR 107
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----------------------TKLPMHK-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPfDEAS----------LMASVEQVGLP-----------------GNILDRYPHQLSGGQRQRVAIVRALQLN 160
Cdd:cd03218 73 ARLGIGYLP-QEASifrkltveenILAVLEIRGLSkkereekleelleefhiTHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-212 |
5.14e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 32 AGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNaqkAFTGALRQQ--VQMVFQDP--YASLHPLHRIrrSLR 107
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA---RLTPAKAHQlgIYLVPQEPllFPNLSVKENI--LFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQinglPFDEASLMASVEQVGLPGNiLDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALdmtVQAEILNLLQA 187
Cdd:PRK15439 111 LPKR----QASMQKMKQLLAALGCQLD-LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSR 182
|
170 180
....*....|....*....|....*..
gi 520926077 188 LR--RDTGMTMILVSHDMNTVAHLCDR 212
Cdd:PRK15439 183 IRelLAQGVGIVFISHKLPEIRQLADR 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
143-228 |
8.10e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 143 LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
....*.
gi 520926077 223 RHLDRA 228
Cdd:PRK10762 475 GEFTRE 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-222 |
9.27e-10 |
|
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: 57.91 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGL-QRDWQGEVQVLGQPLNAqKAFTGALRQQVQMVFQDP-----YASLHPLHRIR 103
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDI-RNPAQAIRAGIAMVPEDRkrhgiVPILGVGKNIT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLREPRQINGLPFDEA---SLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:TIGR02633 362 LSVLKSFCFKMRIDAAAelqIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 520926077 181 ILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:TIGR02633 442 IYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-203 |
1.05e-09 |
|
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: 57.87 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 21 NALEMDGLQI-KAGECFGLIGGSGSGKSTLLRVLAGLQR----------DWQgevQVLgqplnaqKAFTGAlrqQVQMVF 89
Cdd:COG1245 86 NGFRLYGLPVpKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepSWD---EVL-------KRFRGT---ELQDYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 QDPYA-SLHPLHRIRRSLREPRQINGLP------FDEASLMAS-VEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:COG1245 153 KKLANgEIKVAHKPQYVDLIPKVFKGTVrellekVDERGKLDElAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 162 KLLLLDEPTSALDMTvqaEILNLLQALRR--DTGMTMILVSHDM 203
Cdd:COG1245 232 DFYFFDEPSSYLDIY---QRLNVARLIRElaEEGKYVLVVEHDL 272
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-93 |
1.23e-09 |
|
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: 57.50 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 15 RGPSHFNALEMDG--------------------LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQ 74
Cdd:COG4615 320 PAPADFQTLELRGvtyrypgedgdegftlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD 399
|
90
....*....|....*....
gi 520926077 75 KAftGALRQQVQMVFQDPY 93
Cdd:COG4615 400 NR--EAYRQLFSAVFSDFH 416
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-220 |
1.75e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 33 GECFGLIGGSGSGKSTLLRVLAGlqrDWQGEvQVLGQPLNAQKAFTGALRQQVQMVFQDPYasLHPLHRIRRSL------ 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG---RIQGN-NFTGTILANNRKPTKQILKRTGFVTQDDI--LYPHLTVRETLvfcsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQingLPFDEASLMAS--VEQVGLP--GN--ILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:PLN03211 168 RLPKS---LTKQEKILVAEsvISELGLTkcENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 520926077 181 ILNLLQALRRdTGMTMILVSHDMNT-VAHLCDRALLINQGR 220
Cdd:PLN03211 245 LVLTLGSLAQ-KGKTIVTSMHQPSSrVYQMFDSVLVLSEGR 284
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-221 |
3.36e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGL-QRDWQGEVQVLGQPL---NAQKAftgaLRQQVQMVFQD-------------- 91
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVkirNPQQA----IAQGIAMVPEDrkrdgivpvmgvgk 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 92 --PYASL------------HPLHRIRRSLREprqingLPFDEASLMASVEQvglpgnildryphqLSGGQRQRVAIVRAL 157
Cdd:PRK13549 361 niTLAALdrftggsriddaAELKTILESIQR------LKVKTASPELAIAR--------------LSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520926077 158 QLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-224 |
4.24e-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: 56.46 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 4 VDINHLTVTFKRGPShfNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDwQGEVQVLGQPLNA------QKAF 77
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSvtlqtwRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 78 tGALRQQVqMVFQ-------DPYAslhplhriRRSLREPRQINglpfDEASLMASVEQvgLPGN---ILDRYPHQLSGGQ 147
Cdd:TIGR01271 1295 -GVIPQKV-FIFSgtfrknlDPYE--------QWSDEEIWKVA----EEVGLKSVIEQ--FPDKldfVLVDGGYVLSNGH 1358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 148 RQRVAIVRALQLNPKLLLLDEPTSALD-MTVQAEILNLLQALrrdTGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDpVTLQIIRKTLKQSF---SNCTVILSEHRVEALLE-CQQFLVIEGSSVKQY 1432
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-221 |
8.05e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQKafTGALRQQVQMVFQDPYAslhplhrIRRSLRE 108
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG--LRELRRQFSMIPQDPVL-------FDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 109 prqiNGLPFDEAS---LMASVEQVGLPGNILDRYP----------HQLSGGQRQRVAIVRALQLNPKL-LLLDEPTS--- 171
Cdd:PTZ00243 1403 ----NVDPFLEASsaeVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKGSGfILMDEATAnid 1478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 172 -ALDMTVQAEILNLLQAlrrdtgMTMILVSHDMNTVAHlCDRALLINQGRV 221
Cdd:PTZ00243 1479 pALDRQIQATVMSAFSA------YTVITIAHRLHTVAQ-YDKIIVMDHGAV 1522
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-226 |
9.44e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ------PLNAQK---AFTGALRQQVQMVfqdPYASLHPL 99
Cdd:PRK09700 285 SVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKkgmAYITESRRDNGFF---PNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLR-----------EPRQINGLPFDEASLMA----SVEQvglpgNIldrypHQLSGGQRQRVAIVRALQLNPKLL 164
Cdd:PRK09700 362 MAISRSLKdggykgamglfHEVDEQRTAENQRELLAlkchSVNQ-----NI-----TELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 165 LLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLD 226
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-212 |
1.04e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL-QRDwQGEVQVLGQPLN------AQKAFTGALRQQVQMVFQDPYA 94
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRD-AGSILYLGKEVTfngpksSQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 95 SLHPLHRirrslrEPRQINGL-----PFDEAS-LMASVEqvglpgniLDRYPHQLSG----GQRQRVAIVRALQLNPKLL 164
Cdd:PRK10762 98 ENIFLGR------EFVNRFGRidwkkMYAEADkLLARLN--------LRFSSDKLVGelsiGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 520926077 165 LLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDR 212
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDD 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-175 |
2.10e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 16 GPSHFnalemdglQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPL-NAQKAFTGALRQQVQMVFQDpYA 94
Cdd:PRK13543 28 GPLDF--------HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGHLPGLKAD-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 95 SLHPLHRIRR-SLREPRQINGlpfdeaslmASVEQVGLPGNiLDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSAL 173
Cdd:PRK13543 99 TLENLHFLCGlHGRRAKQMPG---------SALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
..
gi 520926077 174 DM 175
Cdd:PRK13543 169 DL 170
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-221 |
2.90e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.72 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLNAQkaftgalrqqvqmvfqdpyaslhPLHRirrslR 107
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-----------------------PMHK-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 EPRQINGLPfDEAS----------LMASVEQVGLP-----------------GNILDRYPHQLSGGQRQRVAIVRALQLN 160
Cdd:COG1137 76 ARLGIGYLP-QEASifrkltvednILAVLELRKLSkkereerleelleefgiTHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 161 PKLLLLDEPTSALD-MTVqAEILNLLQALR-RDTGmtmILVShDMN---TVAhLCDRALLINQGRV 221
Cdd:COG1137 155 PKFILLDEPFAGVDpIAV-ADIQKIIRHLKeRGIG---VLIT-DHNvreTLG-ICDRAYIISEGKV 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-201 |
3.23e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.60 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAGLqrdWqgevqvlgqPLnaqkaFTGAL----RQQVQMVFQDPYASLhplhrirR 104
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGEL---W---------PV-----YGGRLtkpaKGKLFYVPQRPYMTL-------G 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 105 SLRE-------PRQINGLPFDEASLMASVEQVGLpGNILDR---------YPHQLSGGQRQRVAIVRALQLNPKLLLLDE 168
Cdd:TIGR00954 530 TLRDqiiypdsSEDMKRRGLSDKDLEQILDNVQL-THILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 520926077 169 PTSALDMTVQAEILNLLqalrRDTGMTMILVSH 201
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-224 |
3.33e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 34 ECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQDPYAslhplhrIRRSLReprqIN 113
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAKFGLTDLRRVLSIIPQSPVL-------FSGTVR----FN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 114 GLPFDE---ASLMASVEQVGLPgNILDRYPHQL-----------SGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQA 179
Cdd:PLN03232 1330 IDPFSEhndADLWEALERAHIK-DVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 180 eilnLLQALRRD--TGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:PLN03232 1409 ----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-201 |
3.43e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQ--GEVQVLGQPLNAQKAFTGALRQQvqmvfQDPYASLHPLHRirrs 105
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPvaGCVDVPDNQFGREASLIDAIGRK-----GDFKDAVELLNA---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 106 lreprqinglpfdeaslmasveqVGLPGNIL-DRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNL 184
Cdd:COG2401 122 -----------------------VGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170
....*....|....*..
gi 520926077 185 LQALRRDTGMTMILVSH 201
Cdd:COG2401 179 LQKLARRAGITLVVATH 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-224 |
3.82e-08 |
|
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: 52.55 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQrDWQGEVQVLGQPLNA------QKAFtGALRQQVqMVFQDPyasl 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSvplqkwRKAF-GVIPQKV-FIFSGT---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 hplhrIRRSLrEPrqiNGLPFDEaSLMASVEQVGLPgNILDRYPHQL-----------SGGQRQRVAIVRALQLNPKLLL 165
Cdd:cd03289 93 -----FRKNL-DP---YGKWSDE-EIWKVAEEVGLK-SVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 166 LDEPTSALD-MTVQAEILNLLQALrrdTGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:cd03289 162 LDEPSAHLDpITYQVIRKTLKQAF---ADCTVILSEHRIEAMLE-CQRFLVIEENKVRQY 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-204 |
3.87e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRG-PSHFNALEmdgLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQ-PLNAQKAFTGA 80
Cdd:TIGR00957 636 SITVHNATFTWARDlPPTLNGIT---FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvAYVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 81 LRQQVQMVFQDPyaslhplhrirrsLREPRQINGLpfDEASLMASVEQvgLPGNilDRYP-----HQLSGGQRQRVAIVR 155
Cdd:TIGR00957 713 DSLRENILFGKA-------------LNEKYYQQVL--EACALLPDLEI--LPSG--DRTEigekgVNLSGGQKQRVSLAR 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEIL-NLLQALRRDTGMTMILVSHDMN 204
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGIS 823
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-221 |
6.42e-08 |
|
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: 51.37 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQ--RDWQGEVQVLGQPLNA----QKAFTGalrqqVQMVFQDPYAslhplhr 101
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDlppeERARLG-----IFLAFQYPPE------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 102 irrslreprqINGLPFdeASLMASVEqVGLpgnildryphqlSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEI 181
Cdd:cd03217 89 ----------IPGVKN--ADFLRYVN-EGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 520926077 182 LNLLQALRRDtGMTMILVSHDMNTVAHL-CDRALLINQGRV 221
Cdd:cd03217 144 AEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-214 |
8.12e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAG---------------------LQRDWQGEVQVLgqplnaqkaftgaL 81
Cdd:PRK13409 355 LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGvlkpdegevdpelkisykpqyIKPDYDGTVEDL-------------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 82 RQQVQMvFQDPYaslhplhrIRRSLREPRQINglpfdeaslmasveqvglpgNILDRYPHQLSGGQRQRVAIVRALQLNP 161
Cdd:PRK13409 422 RSITDD-LGSSY--------YKSEIIKPLQLE--------------------RLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 162 KLLLLDEPTSALDmtVQaEILNLLQALRR---DTGMTMILVSHDMNTVAHLCDRAL 214
Cdd:PRK13409 473 DLYLLDEPSAHLD--VE-QRLAVAKAIRRiaeEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-221 |
1.15e-07 |
|
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: 50.34 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 1 MSAVDINHLTVTFKRGPSHFNAL-EMDGLqIKAGECFGLIGGSGSGKSTLLRVLAGLQRDW---QGEVQVLGQPLnaqKA 76
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILkDFSGV-VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY---KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 77 FTGALRQQVQMVFQDpyaSLH-PLHRIRRSLREPRQINGlpfdeaslmasveqvglpgnilDRYPHQLSGGQRQRVAIVR 155
Cdd:cd03233 77 FAEKYPGEIIYVSEE---DVHfPTLTVRETLDFALRCKG----------------------NEFVRGISGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMT-MILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-214 |
1.48e-07 |
|
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: 51.32 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEV----------QVLGQplnaqkAFTGALRQQVQMVFQDP 92
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpQYISP------DYDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 93 YASlhplHRIRRSLREPRQINglpfdeaslmasveqvglpgNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:COG1245 430 FGS----SYYKTEIIKPLGLE--------------------KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 173 LDmtVQaEILNLLQALRR---DTGMTMILVSHDMNTVAHLCDRAL 214
Cdd:COG1245 486 LD--VE-QRLAVAKAIRRfaeNRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-236 |
1.74e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 6 INHLTVtfkRGPSHFNALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPLnaqkaftgalrqqv 85
Cdd:COG3845 260 VENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-------------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 86 qmvfqdpyASLHPLHRIRRSLR---EPRQINGL--PFD--EASLMASVEQVGL-PGNILD-----------------RYP 140
Cdd:COG3845 323 --------TGLSPRERRRLGVAyipEDRLGRGLvpDMSvaENLILGRYRRPPFsRGGFLDrkairafaeelieefdvRTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 141 H------QLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRAL 214
Cdd:COG3845 395 GpdtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIA 473
|
250 260
....*....|....*....|....*..
gi 520926077 215 LINQGR----VERH-LDRAVLGELAGG 236
Cdd:COG3845 474 VMYEGRivgeVPAAeATREEIGLLMAG 500
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-233 |
2.61e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGlQRDWQ---GEVQVLGQPLNA----QKAFTGalrqqVQMVFQDP-----YAS 95
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEvtgGTVEFKGKDLLElspeDRAGEG-----IFMAFQYPveipgVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LHPLHRIRRSLREPRQINGLP-FDEASLM-ASVEQVGLPGNILDRYPHQ-LSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDrFDFQDLMeEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520926077 173 LDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHL-CDRALLINQGRVERHLDRAVLGEL 233
Cdd:PRK09580 176 LDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGDFTLVKQL 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-227 |
4.52e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 22 ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGL--QRDWQGEVqvlgqplnaqkAFTGALRQqvqmvFQDPYAS---- 95
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEI-----------LFDGEVCR-----FKDIRDSealg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 ---------LHPLHRIRRS--LREPRQINGL-PFDEASLMAS--VEQVGLPGNildryPHQLSG----GQRQRVAIVRAL 157
Cdd:NF040905 80 iviihqelaLIPYLSIAENifLGNERAKRGViDWNETNRRARelLAKVGLDES-----PDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 158 QLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLINQGRVERHLDR 227
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIETLDC 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-219 |
5.21e-07 |
|
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: 48.39 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDW--QGEVQVLGQPLNaqKAF---TGALRQQvqmvfqdpyaSLH-PLHRIR 103
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD--KNFqrsTGYVEQQ----------DVHsPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLREPRQINGLpfdeaslmaSVEqvglpgnildryphqlsggQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN 183
Cdd:cd03232 98 EALRFSALLRGL---------SVE-------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 520926077 184 LLQALrRDTGMTMILVSHDMN-TVAHLCDRALLINQG 219
Cdd:cd03232 150 FLKKL-ADSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-221 |
5.90e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAG-LQRDWQGEVQVLGqplnaqkafTGALRQQVQMVFQdpyASlhplhrIRRSL 106
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG---------TVAYVPQVSWIFN---AT------VRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 reprqINGLPFDEASLMASVEQVGL-------PGNILDRYPHQ---LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:PLN03130 700 -----LFGSPFDPERYERAIDVTALqhdldllPGGDLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 177 VQAEILN--LLQALRrdtGMTMILVSHDMNTVAHLcDRALLINQGRV 221
Cdd:PLN03130 775 VGRQVFDkcIKDELR---GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-202 |
1.24e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAG-------------------LQ----RDWQGEV-QVLGQPLNAQKAFTGALRQ 83
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarLQqdppRNVEGTVyDFVAEGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 84 QVQMVFQDPYASLhpLHRIRRsLREPRQINGLPFDEASLMASVEQVGLPGnilDRYPHQLSGGQRQRVAIVRALQLNPKL 163
Cdd:PRK11147 104 ISHLVETDPSEKN--LNELAK-LQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 164 LLLDEPTSALDMtvqaEILNLLQALRRDTGMTMILVSHD 202
Cdd:PRK11147 178 LLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-222 |
1.35e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAG-LQRDWQGEVQVLGQPLNAQKA---FTGALRQQVqmVFQDPYASlhplHRIR 103
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVPQVswiFNATVRENI--LFGSDFES----ERYW 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 104 RSLreprqinglpfDEASLMASVEQvgLPGNILDRYPHQ---LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAE 180
Cdd:PLN03232 712 RAI-----------DVTALQHDLDL--LPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 520926077 181 ILN--LLQALRrdtGMTMILVSHDMNTVAhLCDRALLINQGRVE 222
Cdd:PLN03232 779 VFDscMKDELK---GKTRVLVTNQLHFLP-LMDRIILVSEGMIK 818
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-222 |
1.67e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRDWQGEVQvlgqplnAQKAFTGALRQQVQM--------VFQDP--YASLHPLHRIRRslr 107
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVW-------AERSIAYVPQQAWIMnatvrgniLFFDEedAARLADAVRVSQ--- 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqingLPFDEASLMASVE-QVGLPGNildryphQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILN--L 184
Cdd:PTZ00243 761 -------LEADLAQLGGGLEtEIGEKGV-------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecF 826
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 185 LQALRrdtGMTMILVSHDMNTVAHlCDRALLINQGRVE 222
Cdd:PTZ00243 827 LGALA---GKTRVLATHQVHVVPR-ADYVVALGDGRVE 860
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-221 |
2.45e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRDWQGEVqvlgqplnaqkaFTGAlrqQVQM-VFQDPYA-----SLHPLhrirrsLREPRQ 111
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTV------------FRSA---KVRMaVFSQHHVdgldlSSNPL------LYMMRC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 112 INGLPfdEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM-TVQAeilnLLQALRR 190
Cdd:PLN03073 599 FPGVP--EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEA----LIQGLVL 672
|
170 180 190
....*....|....*....|....*....|.
gi 520926077 191 DTGmTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PLN03073 673 FQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-201 |
2.98e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.60 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGlqRDW----QGEVQVLGQPLNA----QKAFTGalrqqVQMVFQDP------- 92
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILElspdERARAG-----IFLAFQYPveipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 93 YASLhpLHRIRRSLREPRQinGLPFDEASLMASVEQVGLPGNILDRYPHQ-LSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:COG0396 94 VSNF--LRTALNARRGEEL--SAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190
....*....|....*....|....*....|...
gi 520926077 172 ALD---MTVQAEILNLLqalrRDTGMTMILVSH 201
Cdd:COG0396 170 GLDidaLRIVAEGVNKL----RSPDRGILIITH 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-221 |
3.10e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 143 LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQAL-RRDTGMTMIlvSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIII--SSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-234 |
4.54e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 21 NALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQvlgqplnaqKAFTGALR----QQVQMV---FQDPY 93
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ---------SQFSHITRlsfeQLQKLVsdeWQRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 94 ASLHPLHR--IRRSLREPRQiNGLPfDEASLMASVEQVGLpGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:PRK10938 88 TDMLSPGEddTGRTTAEIIQ-DEVK-DPARCEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 172 ALDMTVQAEILNLLQALRRdTGMTMILVS---HD----MNTVAHLCDRAlLINQGRVERHLDRAVLGELA 234
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQ-SGITLVLVLnrfDEipdfVQFAGVLADCT-LAETGEREEILQQALVAQLA 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-224 |
4.74e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQDPYAslhplhrIRRSLRep 109
Cdd:PLN03130 1262 ISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDLRKVLGIIPQAPVL-------FSGTVR-- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 110 rqINGLPFDE---ASLMASVEQVGLPgNILDRYPHQL-----------SGGQRQRVAIVRALQLNPKLLLLDEPTSALDM 175
Cdd:PLN03130 1331 --FNLDPFNEhndADLWESLERAHLK-DVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 520926077 176 TVQAeilnLLQALRRD--TGMTMILVSHDMNTVAHlCDRALLINQGRVERH 224
Cdd:PLN03130 1408 RTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-219 |
6.19e-06 |
|
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: 46.00 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLaglqrdwQGEVQvlgqplnaqkAFTGALRQQVQMVFQDPYASLHPlHRIRRSLr 107
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLI-------LGELE----------PSEGKIKHSGRISFSSQFSWIMP-GTIKENI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqINGLPFDEASLMASVEQVGLPGNILdRYPHQ-----------LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:cd03291 119 ----IFGVSYDEYRYKSVVKACQLEEDIT-KFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 520926077 177 VQAEILN----LLQALRrdtgmTMILVShdmNTVAHL--CDRALLINQG 219
Cdd:cd03291 194 TEKEIFEscvcKLMANK-----TRILVT---SKMEHLkkADKILILHEG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-68 |
7.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 7.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLG 68
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-201 |
8.70e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 24 EMDGLqIKAGECFGLIGGSGSGKSTLLRVLAglQRD-----WQGEVQVLGQPLnaQKAF---TGALRQQvqmvfqdpyaS 95
Cdd:TIGR00956 781 NVDGW-VKPGTLTALMGASGAGKTTLLNVLA--ERVttgviTGGDRLVNGRPL--DSSFqrsIGYVQQQ----------D 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LH-PLHRIRRSLREP---RQINGLPFDEAslMASVEQ--------------VGLPGNildryphQLSGGQRQRVAI-VRA 156
Cdd:TIGR00956 846 LHlPTSTVRESLRFSaylRQPKSVSKSEK--MEYVEEvikllemesyadavVGVPGE-------GLNVEQRKRLTIgVEL 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520926077 157 LQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSH 201
Cdd:TIGR00956 917 VAKPKLLLFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
28-201 |
1.73e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGlQRDWQ---GEVQVLGQPLNaqkAFTGALRQQ--VQMVFQDPYAS------- 95
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYKileGDILFKGESIL---DLEPEERAHlgIFLAFQYPIEIpgvsnad 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 -LHPLHRIRRSLREPRQINGLPFDEAsLMASVEQVGLPGNILDRYPHQ-LSGGQRQRVAIVRALQLNPKLLLLDEPTSAL 173
Cdd:CHL00131 104 fLRLAYNSKRKFQGLPELDPLEFLEI-INEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
170 180 190
....*....|....*....|....*....|.
gi 520926077 174 D---MTVQAEILNLLqalrRDTGMTMILVSH 201
Cdd:CHL00131 183 DidaLKIIAEGINKL----MTSENSIILITH 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-201 |
2.60e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 38 LIGGSGSGKSTLLRVLAGLQRDW--QGEVQVLGQPLNaQKAF---TGALRQQvqmvfqdpyaSLH-PLHRIRRSL----- 106
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKK-QETFariSGYCEQN----------DIHsPQVTVRESLiysaf 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 -REPRQING---LPF-DEasLMASVEQ-------VGLPGNIldryphQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALD 174
Cdd:PLN03140 980 lRLPKEVSKeekMMFvDE--VMELVELdnlkdaiVGLPGVT------GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*....
gi 520926077 175 MTVQAEIlnlLQALRR--DTGMTMILVSH 201
Cdd:PLN03140 1052 ARAAAIV---MRTVRNtvDTGRTVVCTIH 1077
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-221 |
2.78e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 3 AVDINHLTVTFKRGP--SHFNalemdgLQIKAGECFGLIGGSGSGKSTLLRVLAG-LQRDwQGEVQVlgqplnAQKAFTG 79
Cdd:PRK15064 319 ALEVENLTKGFDNGPlfKNLN------LLLEAGERLAIIGENGVGKTTLLRTLVGeLEPD-SGTVKW------SENANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 80 ALRQQVQMVFQDPYASLHPLHRIRRSLREPRQING----LPFDEASLMASVEQvglpgnildryphqLSGGQRQRVAIVR 155
Cdd:PRK15064 386 YYAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVRGtlgrLLFSQDDIKKSVKV--------------LSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 156 ALQLNPKLLLLDEPTSALDMTvQAEILNLlqALRRDTGmTMILVSHDMNTVAHLCDRALLINQGRV 221
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDME-SIESLNM--ALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-131 |
2.80e-05 |
|
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: 42.75 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 33 GECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVlgqpLNAQKAFTGALRQQVQMVFQDPYASLHPLHRIRRSLREPRQI 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
|
90 100
....*....|....*....|.
gi 520926077 113 NG--LPFDEASLMASVEQVGL 131
Cdd:smart00382 78 KPdvLILDEITSLLDAEQEAL 98
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-217 |
3.66e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 3.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520926077 139 YPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHlCDRALLIN 217
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1432
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-195 |
3.79e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 25 MDGLqIKAGECFGLIGGSGSGKSTLLRVLA----GLQRDWQGEVQVLGQPLNA-QKAFTGALRQQVQMVFQDPYASLHPL 99
Cdd:TIGR00956 80 MDGL-IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEiKKHYRGDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 100 HRIRRSLREPR-QINGLPFDE-ASLMASV--EQVGLP-------GNILDRyphQLSGGQRQRVAIVRALQLNPKLLLLDE 168
Cdd:TIGR00956 159 LDFAARCKTPQnRPDGVSREEyAKHIADVymATYGLShtrntkvGNDFVR---GVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180
....*....|....*....|....*..
gi 520926077 169 PTSALDMTVQAEILNLLQALRRDTGMT 195
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTT 262
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-232 |
4.20e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVqVLGQPLNAQKAFTGALRQQVQMVFQDP------------YA--S 95
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLKWWRSKIGVVSQDPllfsnsiknnikYSlyS 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 96 LHPLHRIRRSLRE---------------PRQINGLPFDEASLMASVEQVGLPGN------------------------IL 136
Cdd:PTZ00265 487 LKDLEALSNYYNEdgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIEMRKNyqtikdsevvdvskkvlihdfvsaLP 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 137 DRY-------PHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDTGMTMILVSHDMNTVAHL 209
Cdd:PTZ00265 567 DKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYA 646
|
250 260
....*....|....*....|...
gi 520926077 210 CDRALLINQGRVERhLDRAVLGE 232
Cdd:PTZ00265 647 NTIFVLSNRERGST-VDVDIIGE 668
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
138-221 |
5.74e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 138 RYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTVQAEILNLLQALRRDtGMTMILVSHDMNTVAHLCDRALLIN 217
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
....
gi 520926077 218 QGRV 221
Cdd:NF000106 219 RGRV 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-206 |
5.76e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 29 QIKAGECFGLIGGSGSGKSTLLRVLAG-LQRDwQGEVQVlGQPLnaqkaftgalrqqvQMVFQDPY-ASLHPLHRIRRSL 106
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGqLQAD-SGRIHC-GTKL--------------EVAYFDQHrAELDPEKTVMDNL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQ---INGLP-----------FDEASLMASVEQvglpgnildryphqLSGGQRQRVAIVRALQLNPKLLLLDEPTSA 172
Cdd:PRK11147 405 AEGKQevmVNGRPrhvlgylqdflFHPKRAMTPVKA--------------LSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 520926077 173 LDMtvqaEILNLLQALRRDTGMTMILVSHDM----NTV 206
Cdd:PRK11147 471 LDV----ETLELLEELLDSYQGTVLLVSHDRqfvdNTV 504
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-219 |
6.92e-05 |
|
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: 43.75 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQplnaqkaftgalrqqvqMVFQDPYASLHPlHRIRRSLr 107
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMP-GTIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 108 eprqINGLPFDEASLMASVEQVGLPGNIlDRYPHQ-----------LSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMT 176
Cdd:TIGR01271 508 ----IFGLSYDEYRYTSVIKACQLEEDI-ALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 520926077 177 VQAEILN--LLQALrrdTGMTMILVSHDMNtvaHL--CDRALLINQG 219
Cdd:TIGR01271 583 TEKEIFEscLCKLM---SNKTRILVTSKLE---HLkkADKILLLHEG 623
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
129-208 |
7.49e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 129 VGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLL--LDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTV 206
Cdd:cd03270 124 VGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTI 202
|
..
gi 520926077 207 AH 208
Cdd:cd03270 203 RA 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-222 |
7.80e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 28 LQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVlgqplnaQKAFTGALRQQVQMVFQDPYASlhPL-HRIRRSL 106
Cdd:PRK10636 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------AKGIKLGYFAQHQLEFLRADES--PLqHLARLAP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 107 REPRQinglpfdeaSLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDmtvqaeiLNLLQ 186
Cdd:PRK10636 404 QELEQ---------KLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQ 467
|
170 180 190
....*....|....*....|....*....|....*....
gi 520926077 187 ALRR---DTGMTMILVSHDMNTVAHLCDRALLINQGRVE 222
Cdd:PRK10636 468 ALTEaliDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-219 |
8.76e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 128 QVGLPGNILDRYPHQLSGGQRQRVAIVR--ALQLNPKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNT 205
Cdd:PRK00635 462 DLGLPYLTPERALATLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQM 540
|
90
....*....|....
gi 520926077 206 VAhLCDRALLINQG 219
Cdd:PRK00635 541 IS-LADRIIDIGPG 553
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-186 |
1.57e-04 |
|
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: 41.82 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 19 HFNALemdglqIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGqpLNAQKAFTGALRQQVQMVFQDP--YASl 96
Cdd:cd03288 39 HVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDPilFSG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 97 hplhRIRRSLREPRQINGLPFDEASLMASVEQV--GLPGN---ILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTS 171
Cdd:cd03288 110 ----SIRFNLDPECKCTDDRLWEALEIAQLKNMvkSLPGGldaVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170
....*....|....*
gi 520926077 172 ALDMTVQaeilNLLQ 186
Cdd:cd03288 186 SIDMATE----NILQ 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-226 |
3.63e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 13 FKRGPSHFN-ALEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQVLGQPlnAQKAFTGALRQQVQMVfqd 91
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--ALIAISSGLNGQLTGI--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 92 pyaslhplhrirrslrEPRQINGLpfdeasLMA-SVEQVG--LPGNI----LDRYPHQ----LSGGQRQRVAIVRALQLN 160
Cdd:PRK13545 104 ----------------ENIELKGL------MMGlTKEKIKeiIPEIIefadIGKFIYQpvktYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520926077 161 PKLLLLDEPTSALDMTVQAEILNLLQALrRDTGMTMILVSHDMNTVAHLCDRALLINQGRVERHLD 226
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-212 |
4.06e-04 |
|
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: 39.86 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 23 LEMDGLQIKAGECFGLIGGSGSGKSTLLRVLAGLQRDWQGEVQvlgqplnaqkaftgalrqqvqmvfqdpyaslhpLHRI 102
Cdd:cd03222 15 LLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE---------------------------------WDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 103 RRSLRePRQINglpfdeaslmasveqvglpgnildryphqLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDMTvqaEIL 182
Cdd:cd03222 62 TPVYK-PQYID-----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE---QRL 108
|
170 180 190
....*....|....*....|....*....|...
gi 520926077 183 NLLQALRR---DTGMTMILVSHDMNTVAHLCDR 212
Cdd:cd03222 109 NAARAIRRlseEGKKTALVVEHDLAVLDYLSDR 141
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-218 |
5.67e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 30 IKAGECFGLIGGSGSGKSTLLRVLAG-LQRD---------WQ-----GEVQVLGQP-----LNAQKAFTgALRQQVQMVF 89
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNeISADggsytfpgnWQlawvnQETPALPQPaleyvIDGDREYR-QLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 90 Q----DPYASLH-PLHRIR----RSlREPRQINGLPFDEASLMASVEQvglpgnildryphqLSGGQRQRVAIVRALQLN 160
Cdd:PRK10636 103 ErndgHAIATIHgKLDAIDawtiRS-RAASLLHGLGFSNEQLERPVSD--------------FSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 520926077 161 PKLLLLDEPTSALDMTVqaeILNLLQALRRDTGmTMILVSHDMNTVAHLCDRALLINQ 218
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-202 |
6.11e-04 |
|
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: 39.23 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 21 NALEMDGLQIKAGECFGLIGGSGSGKSTLlrVLAGLqrdwqgevqvlgqplnaqkaftgalrqqvqmvfqdpYASLhplh 100
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL------------------------------------YASG---- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 101 rirrslrEPRQINGLPFDEASLMASVEQ------VGLPGNILDRYPHQLSGGQRQRVAIVR--ALQLNPKLLLLDEPTSA 172
Cdd:cd03238 47 -------KARLISFLPKFSRNKLIFIDQlqflidVGLGYLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|
gi 520926077 173 LDMTVQAEILNLLQALrRDTGMTMILVSHD 202
Cdd:cd03238 120 LHQQDINQLLEVIKGL-IDLGNTVILIEHN 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-208 |
1.94e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 129 VGLPGNILDRYPHQLSGGQRQRVAIVR--ALQLNPKLLLLDEPTSALDmtvQAEILNLLQALR--RDTGMTMILVSHDMN 204
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLH---QRDNRRLINTLKrlRDLGNTLIVVEHDED 551
|
....
gi 520926077 205 TVAH 208
Cdd:TIGR00630 552 TIRA 555
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
135-209 |
3.35e-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: 37.59 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 135 ILDRYPHQLSGGQRQ------RVAIVRALQLNPKLLLLDEPTSALDM-TVQAEILNLLQALRRDTGMTMILVSHDMNTVA 207
Cdd:cd03240 108 PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVD 187
|
..
gi 520926077 208 HL 209
Cdd:cd03240 188 AA 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-202 |
3.58e-03 |
|
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: 37.99 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 37 GLIGGSGSGKSTLLRVLAGLQRDWQGEVQVlgqplnaqkaftGalrQQVQMVFQDPY-ASLHPLHRIRRSLREPRQINGL 115
Cdd:TIGR03719 352 GVIGPNGAGKSTLFRMITGQEQPDSGTIEI------------G---ETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520926077 116 PFDEASLMASVEQVGLPGNILDRYPHQLSGGQRQRVAIVRALQLNPKLLLLDEPTSALDM-TVQAeilnLLQALRRDTGM 194
Cdd:TIGR03719 417 GKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA----LEEALLNFAGC 492
|
....*...
gi 520926077 195 TMIlVSHD 202
Cdd:TIGR03719 493 AVV-ISHD 499
|
|
| |
