|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-222 |
2.71e-63 |
|
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: 197.33 E-value: 2.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRL 90
Cdd:COG1124 2 LEVRNLSVSygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG--RPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPASTLNPKMTALDAVERAARVsvRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRP 170
Cdd:COG1124 80 RVQMVFQDPYASLHPRHTVDRILAEPLRI--HGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-222 |
1.18e-62 |
|
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: 203.21 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCV----NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWP 85
Cdd:COG1123 258 EPLLEVRNLSKRypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 86 RKNRLMMQIVPQDPASTLNPKMTALDAVERAARV-SVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIAR 164
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-222 |
1.64e-62 |
|
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: 194.65 E-value: 1.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLS---CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-VTREAKRTWPRKN 88
Cdd:cd03257 1 LLEVKNLSvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQDPASTLNPKMTALDAVERAARV--SVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARAL 166
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 167 AVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-222 |
4.36e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 178.31 E-value: 4.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLS---CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT----REAKRT 83
Cdd:COG1136 2 SPLLELRNLTksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 84 WPRKNRLmmQIVPQDPasTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIA 163
Cdd:COG1136 82 RLRRRHI--GFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 164 RALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLqSYCSTVI 222
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVI 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-222 |
7.10e-56 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 177.30 E-value: 7.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLS---CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT----REAKRTWPR 86
Cdd:cd03255 1 IELKNLSktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 KNRlmMQIVPQDPasTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARAL 166
Cdd:cd03255 81 RRH--IGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 167 AVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLqSYCSTVI 222
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRII 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-222 |
6.58e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 170.62 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-----TREAKRTWPR 86
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 knRLMMqiVPQDPAstLNPKMTALDAV--ERAARVSVRGRRDAR------RAAIDLLDKVGIDKQLAQRkPSGLSGGQRQ 158
Cdd:COG3638 81 --RIGM--IFQQFN--LVPRLSVLTNVlaGRLGRTSTWRSLLGLfppedrERALEALERVGLADKAYQR-ADQLSGGQQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRII 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-222 |
7.23e-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: 7.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRknRLMMQ 93
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL--RRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDP-----AST------LNPKMTALDAVERAARVsvrgrrdarraaIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAI 162
Cdd:COG1122 79 LVFQNPddqlfAPTveedvaFGPENLGLPREEIRERV------------EEALELVGLEH-LADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 163 ARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-222 |
2.16e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.80 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRknrl 90
Cdd:COG1121 4 MPAIELENLT-VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG--KPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 mmqI--VPQDPASTLNPKMTALDAVE--RAARVSVRGRRDARRAAI--DLLDKVGIDKqLAQRKPSGLSGGQRQRVAIAR 164
Cdd:COG1121 77 ---IgyVPQRAEVDWDFPITVRDVVLmgRYGRRGLFRRPSRADREAvdEALERVGLED-LADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-222 |
7.13e-49 |
|
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: 159.17 E-value: 7.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSC-VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMQ 93
Cdd:cd03225 1 ELKNLSFsYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--KDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDPASTL-----------NPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKqLAQRKPSGLSGGQRQRVAI 162
Cdd:cd03225 79 LVFQNPDDQFfgptveeevafGLENLGLPEEEIEERVE------------EALELVGLEG-LRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 163 ARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVI 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-210 |
1.50e-48 |
|
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: 161.76 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSC---VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL---NHAESGEI-----ECAGVTREAK 81
Cdd:COG0444 1 LLEVRNLKVyfpTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEIlfdgeDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 82 RTWpRKNRlmMQIVPQDPASTLNPKMTALDAVERAARV-SVRGRRDARRAAIDLLDKVGID--KQLAQRKPSGLSGGQRQ 158
Cdd:COG0444 81 RKI-RGRE--IQMIFQDPMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDY--QAatKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVtiQA--QILNLLKDLQRElGLAILFITHD 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-210 |
9.83e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 157.08 E-value: 9.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQIVPQDPAstLNPKMTALD 111
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGMVFQQFN--LFPHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 ----------------AVERAarvsvrgrrdarraaIDLLDKVGI-DKqlAQRKPSGLSGGQRQRVAIARALAVRPKLLL 174
Cdd:COG1126 97 nvtlapikvkkmskaeAEERA---------------MELLERVGLaDK--ADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHE 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-210 |
1.94e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 159.13 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWpRKNRLMMQIVPQDPASTLNPKMTA 109
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqdITGLSGREL-RPLRRRMQMVFQDPYASLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDAV-------------ERAARVsvrgrrdarraaIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:COG4608 115 GDIIaeplrihglaskaERRERV------------AELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 2791281350 177 EITSALDY--QAatKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG4608 183 EPVSALDVsiQA--QVLNLLEDLQDElGLTYLFISHD 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-224 |
2.89e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.97 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKR--TWPRKNRLm 91
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppEWRRQVAY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 mqiVPQDPAstLnPKMTALDAVERAARVSvrGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPK 171
Cdd:COG4619 79 ---VPQEPA--L-WGGTVRDNLPFPFQLR--ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQEL-NSEGMGIVLVSHDDELLQSYCSTVIPI 224
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-210 |
6.98e-47 |
|
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: 162.16 E-value: 6.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLFQ----------GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAEsGEIECAG-----V 76
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLFRrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGqdldgL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 77 TREAKRTWprknRLMMQIVPQDPASTLNPKMT--------------ALDAVERAARVsvrgrrdarraaIDLLDKVGIDK 142
Cdd:COG4172 353 SRRALRPL----RRRMQVVFQDPFGSLSPRMTvgqiiaeglrvhgpGLSAAERRARV------------AEALEEVGLDP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 143 QLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDyqaatkvMSV-------LQELNSE-GMGIVLVSHD 210
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-------VSVqaqildlLRDLQREhGLAYLFISHD 485
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-210 |
1.49e-45 |
|
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: 150.76 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQIVPQDpaSTLNPKMTAL 110
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMVFQQ--FNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAAR-VSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATK 189
Cdd:cd03262 95 ENITLAPIkVKGMSKAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180
....*....|....*....|.
gi 2791281350 190 VMSVLQELNSEGMGIVLVSHD 210
Cdd:cd03262 174 VLDVMKDLAEEGMTMVVVTHE 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-222 |
2.04e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 151.73 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPRKNR-LM 91
Cdd:COG1120 1 MLEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG---RDLASLSRRELaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDPASTLNpkMTALDAVE--RAARVSVRGRRDARRAAI--DLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALA 167
Cdd:COG1120 77 IAYVPQEPPAPFG--LTVRELVAlgRYPHLGLFGRPSAEDREAveEALERTGLEH-LADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-222 |
6.63e-45 |
|
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: 156.60 E-value: 6.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCV-NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL---NHAESGEIECAGVTREAKRTWPR 86
Cdd:COG1123 2 TPLLEVRDLSVRyPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 KNRLMMqiVPQDPASTLNPkMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARAL 166
Cdd:COG1123 82 GRRIGM--VFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 167 AVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVV 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-214 |
8.01e-45 |
|
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: 148.78 E-value: 8.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLm 91
Cdd:COG4133 1 MMLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 mqIVPQDPAstLNPKMTALDAVERAARVSvrGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPK 171
Cdd:COG4133 79 --YLGHADG--LKPELTVRENLRFWAALY--GLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-222 |
1.18e-44 |
|
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: 149.26 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNRLMM 92
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPAstLNPKMTALDAV--ERAARVSVRGRRDARRAAID------LLDKVGIDKQLAQRKpSGLSGGQRQRVAIAR 164
Cdd:cd03256 81 GMIFQQFN--LIERLSVLENVlsGRLGRRSTWRSLFGLFPKEEkqralaALERVGLLDKAYQRA-DQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-212 |
1.84e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtwPRKN 88
Cdd:COG1116 6 PALELRGVSKRfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMmqiVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:COG1116 82 RGV---VFQEPA--LLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAG-FEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQEL-NSEGMGIVLVSHD-DE 212
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDvDE 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-222 |
5.10e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 145.79 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFqGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQ 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLN-DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDPAstLNPKMTALDAVERaarvsvrgrrdarraaidlldkvgidkqlaqrkpsGLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03229 80 MVFQDFA--LFPHLTVLENIAL-----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVV 172
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-222 |
1.09e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTReakRTWPRKNRLMMQIVPQDPAstLNPKMTALD 111
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV---ARDPAEVRRRIGYVPQEPA--LYPDLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 AVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVM 191
Cdd:COG1131 93 NLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 192 SVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1131 172 ELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
27-210 |
1.96e-42 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 143.69 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQIVPQDpaSTLNPK 106
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQ--FYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 107 MTALDAVERAA-RVSVRGRRDARRAAIDLLDKVGidkqLAQRK---PSGLSGGQRQRVAIARALAVRPKLLLCDEITSAL 182
Cdd:PRK09493 92 LTALENVMFGPlRVRGASKEEAEKQARELLAKVG----LAERAhhyPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 2791281350 183 DYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-217 |
2.33e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWP---RK 87
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 nrlmMQIVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALA 167
Cdd:COG2884 81 ----IGVVFQDFR--LLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSY 217
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRM 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-212 |
3.87e-42 |
|
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: 142.23 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreAKRTWPRKNRL 90
Cdd:cd03293 1 LEVRNVSKTyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMqivPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRP 170
Cdd:cd03293 77 YV---FQQDA--LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQEL-NSEGMGIVLVSHD-DE 212
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDiDE 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-222 |
8.32e-42 |
|
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: 141.13 E-value: 8.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTreakrtwPRKNRLMMQI 94
Cdd:cd03235 1 EVEDLTVSYGGHPVL-EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-------LEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQ----DP----------ASTLNPKMTALDAVERAARVSVrgrrdarraaIDLLDKVGIDKqLAQRKPSGLSGGQRQRV 160
Cdd:cd03235 73 VPQrrsiDRdfpisvrdvvLMGLYGHKGLFRRLSKADKAKV----------DEALERVGLSE-LADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 161 AIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
27-212 |
6.05e-41 |
|
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: 138.81 E-value: 6.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAkrtwPRKNRLMMqiVPQDPAstLN 104
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdVTGVP----PERRNIGM--VFQDYA--LF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDY 184
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180
....*....|....*....|....*....
gi 2791281350 185 QAATKVMSVLQEL-NSEGMGIVLVSHDDE 212
Cdd:cd03259 164 KLREELREELKELqRELGITTIYVTHDQE 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
28-212 |
6.34e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTwPRKNRlmMQIVPQDPAstLNPKM 107
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-PRERR--VGFVFQHYA--LFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAV------------ERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:COG1118 91 TVAENIafglrvrppskaEIRARVE------------ELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSEgMGI--VLVSHDDE 212
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDE-LGGttVFVTHDQE 195
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-210 |
6.56e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.54 E-value: 6.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAkrtwPRKN 88
Cdd:COG3842 3 MPALELENVSKRYGDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdVTGLP----PEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMqiVPQDPAstLNPKMTALDAV------------ERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQ 156
Cdd:COG3842 78 NVGM--VFQDYA--LFPHLTVAENVafglrmrgvpkaEIRARVA------------ELLELVGLE-GLADRYPHQLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHD 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-221 |
7.83e-41 |
|
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: 139.25 E-value: 7.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRTWPRK---------NR 89
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltlLSGKELRKARRrigmifqhfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 LMMQIVPQDPASTLnpKMTALDAVERAARVSvrgrrdarraaiDLLDKVGI-DKqlAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:cd03258 94 LSSRTVFENVALPL--EIAGVPKAEIEERVL------------ELLELVGLeDK--ADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTV 221
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRV 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-229 |
9.85e-41 |
|
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: 139.36 E-value: 9.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-----VTREAKRTWPRK 87
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditkLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NRLMMQivpqdpASTLNPKMTALDAV--ERAARVSVRGRRDAR------RAAIDLLDKVGIDKQLAQRKpSGLSGGQRQR 159
Cdd:TIGR02315 81 IGMIFQ------HYNLIERLTVLENVlhGRLGYKPTWRSLLGRfseedkERALSALERVGLADKAYQRA-DQLSGGQQQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 160 VAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVIPIGTAAV 229
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-222 |
2.21e-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: 136.41 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPRKNR-LMMQ 93
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG---KDLASLSPKELaRKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQdpastlnpkmtaldaveraarvsvrgrrdarraaidLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03214 77 YVPQ------------------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVI 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-215 |
5.01e-40 |
|
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: 137.18 E-value: 5.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLS-CV--NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-----TREAKR 82
Cdd:COG4181 6 APIIELRGLTkTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfalDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 83 TWPRKNrlmMQIVPQdpASTLNPKMTAL-------------DAVERAARvsvrgrrdarraaidLLDKVGidkqLAQR-- 147
Cdd:COG4181 86 RLRARH---VGFVFQ--SFQLLPTLTALenvmlplelagrrDARARARA---------------LLERVG----LGHRld 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 148 -KPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQ 215
Cdd:COG4181 142 hYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-210 |
5.96e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.83 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT---------REAK 81
Cdd:COG1135 2 IELENLSKTfptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalserelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 82 RtwprknRLMMqiVPQDpASTLNPKmTALDAV------------ERAARVSvrgrrdarraaiDLLDKVGI-DKqlAQRK 148
Cdd:COG1135 82 R------KIGM--IFQH-FNLLSSR-TVAENValpleiagvpkaEIRKRVA------------ELLELVGLsDK--ADAY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 149 PSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-222 |
2.09e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.74 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-----TREAKRTWPRKnrlmMQIVPQDPAST 102
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklNRAQRKAFRRD----IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPK-------------MTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVR 169
Cdd:PRK10419 102 VNPRktvreiireplrhLLSLDKAERLARAS------------EMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVM 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-210 |
4.74e-39 |
|
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: 134.72 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRTWPRK 87
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditgLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NrlmMQIVPQDPA--STLN-------P--KMTALDAVERAARVsvrgrrdarraaIDLLDKVGIdKQLAQRKPSGLSGGQ 156
Cdd:COG1127 83 R---IGMLFQGGAlfDSLTvfenvafPlrEHTDLSEAEIRELV------------LEKLELVGL-PGAADKMPSELSGGM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
32-222 |
5.34e-39 |
|
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: 132.52 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreaKRTWPRKNRLMMQI--VPQDPAstLNPKMTA 109
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-----KDIKKEPEEVKRRIgyLPEEPS--LYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDAVEraarvsvrgrrdarraaidlldkvgidkqlaqrkpsgLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATK 189
Cdd:cd03230 91 RENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 190 VMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEEAERLCDRVA 166
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-222 |
8.75e-39 |
|
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: 131.60 E-value: 8.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLmmQI 94
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI--GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQdpastlnpkmtaldaveraarvsvrgrrdarraaidlldkvgidkqlaqrkpsgLSGGQRQRVAIARALAVRPKLLL 174
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVI 151
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-210 |
4.04e-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: 132.30 E-value: 4.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE-----SGEIECAGVTREAKRTWPRKN 88
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQDPastlNP-KMTALDAVERAARVS-VRGRRDARRAAIDLLDKVGIDKQLAQR-KPSGLSGGQRQRVAIARA 165
Cdd:cd03260 80 RRRVGMVFQKP----NPfPGSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2791281350 166 LAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgMGIVLVSHD 210
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHN 199
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-222 |
1.36e-36 |
|
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: 129.15 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNRLMMQIVPQDPASTL 103
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdLYQLDRKQRRAFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTA-------------LDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRP 170
Cdd:TIGR02769 102 NPRMTVrqiigeplrhltsLDESEQKARIA------------ELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVA 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-210 |
4.14e-36 |
|
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: 127.23 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNRLMMQIVPQDPA--STLN 104
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdISGLSEAELYRLRRRMGMLFQSGAlfDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 -------P--KMTALDAVERAARVsvrgrrdarraaIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:cd03261 94 vfenvafPlrEHTRLSEEEIREIV------------LEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-230 |
7.91e-36 |
|
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: 125.45 E-value: 7.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreaKRTWPRKNRLMMQI 94
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQDPASTLnpkmtALDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLL 174
Cdd:cd03226 76 VMQDVDYQL-----FTDSVREELLLGLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPIGTAAVG 230
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-222 |
5.10e-35 |
|
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: 124.58 E-value: 5.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPRKNRLMM 92
Cdd:COG4555 1 MIEVENLSKKYGKVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG---EDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKL 172
Cdd:COG4555 77 GVLPDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2791281350 173 LLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-180 |
6.98e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.60 E-value: 6.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKNrlmMQIVPQDPasTLNPKMT 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKE---IGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 109 ALDAVERAARVSVRGRRDARRAAIDLLDKVGI---DKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-210 |
7.33e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 126.36 E-value: 7.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWpRKNRLMMQIVPQDPASTLNPKMTA 109
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdLLGMKDDEW-RAVRSDIQMIFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 --------------LDAVERAARVSVrgrrdarraaidLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK15079 118 geiiaeplrtyhpkLSRQEVKDRVKA------------MMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-222 |
1.73e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.67 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLF----------QGLSFAVQRGTMVGVKGPSGSGKST----LLRCLiglnhAESGEIECAGv 76
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILkrtvdhnvvvKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDG- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 77 trEAKRTWPRKN----RLMMQIVPQDPASTLNPKMTALDAVERAARV--SVRGRRDARRAAIDLLDKVGIDKQLAQRKPS 150
Cdd:PRK15134 347 --QPLHNLNRRQllpvRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 151 GLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVI 497
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-215 |
2.34e-34 |
|
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: 129.57 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSC-VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlm 91
Cdd:COG2274 474 IELENVSFrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdLRQIDPASLRRQ--- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDP---ASTL-------NPKMTaLDAVERAARVSvrgrrdarraaiDLLDKV-----GIDKQLAQRKpSGLSGGQ 156
Cdd:COG2274 551 IGVVLQDVflfSGTIrenitlgDPDAT-DEEIIEAARLA------------GLHDFIealpmGYDTVVGEGG-SNLSGGQ 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELLQ 215
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR 674
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-210 |
2.90e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAkrtwPRKNRLM 91
Cdd:COG3839 4 LELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdVTDLP----PKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MqiVPQDPAstLNPKMTA------------LDAVERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQRQR 159
Cdd:COG3839 79 M--VFQSYA--LYPHMTVyeniafplklrkVPKAEIDRRVR------------EAAELLGLE-DLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 160 VAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHD 193
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-214 |
5.83e-34 |
|
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: 127.57 E-value: 5.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKNr 89
Cdd:COG4988 334 PPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lmMQIVPQDP---ASTL-------NPKMTAlDAVERAARVSvrgrrdarraaiDLLDKV-----GIDKQLAQRKpSGLSG 154
Cdd:COG4988 413 --IAWVPQNPylfAGTIrenlrlgRPDASD-EELEAALEAA------------GLDEFVaalpdGLDTPLGEGG-RGLSG 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 155 GQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELL 214
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL 535
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-212 |
1.51e-33 |
|
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: 120.52 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLmmQIVPQDPAstLNPKMTALD 111
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQERNV--GFVFQHYA--LFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 AVERAARV----SVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAA 187
Cdd:cd03296 94 NVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180
....*....|....*....|....*..
gi 2791281350 188 TKVMSVLQELNSEgMGI--VLVSHDDE 212
Cdd:cd03296 173 KELRRWLRRLHDE-LHVttVFVTHDQE 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-228 |
1.93e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 122.77 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNRLMMQIVPQDPASTLNPKM--- 107
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKkvg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 ----------TALDAVERAARVsvrgrrdarraaIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDE 177
Cdd:PRK11308 113 qileepllinTSLSAAERREKA------------LAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 178 ITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD--------DELLQSYCSTVIPIGTAA 228
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDlsvvehiaDEVMVMYLGRCVEKGTKE 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
47-215 |
2.20e-33 |
|
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: 122.90 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 47 GPSGSGKSTLLRCLIGLNHAESGEIECAGVT--REAKRTW--PRKNRLMMqiVPQDPAstLNPKMTA----LDAVERAAR 118
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqDSARGIFlpPHRRRIGY--VFQEAR--LFPHLSVrgnlLYGRKRAPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 vsvRGRRDARRAAIDLLdkvGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN 198
Cdd:COG4148 108 ---AERRISFDEVVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLR 180
|
170
....*....|....*....
gi 2791281350 199 SE-GMGIVLVSHD-DELLQ 215
Cdd:COG4148 181 DElDIPILYVSHSlDEVAR 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-225 |
3.70e-33 |
|
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: 119.05 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPrKNRLMMQIVPQDpaSTLN 104
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdVSDLRGRAIP-YLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGidkqLAQRK---PSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRVPAALELVG----LSHKHralPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 182 LDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPIG 225
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-215 |
6.39e-33 |
|
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: 117.10 E-value: 6.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQDP-- 99
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdLRDLDLESLRKN---IAYVPQDPfl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 -ASTL--NpkmtaldaveraarvsvrgrrdarraaidlldkvgIdkqlaqrkpsgLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:cd03228 88 fSGTIreN-----------------------------------I-----------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 177 EITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELLQ 215
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR 159
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-216 |
9.99e-33 |
|
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: 119.07 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLS--CVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWP-RKNr 89
Cdd:TIGR04520 1 IEVENVSfsYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLWEiRKK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lmMQIVPQDP-----ASTLN------PKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLaQRKPSGLSGGQRQ 158
Cdd:TIGR04520 79 --VGMVFQNPdnqfvGATVEddvafgLENLGVPREEMRKRVD------------EALKLVGMEDFR-DREPHLLSGGQKQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD-DELLQS 216
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDmEEAVLA 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-221 |
1.15e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 26 RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT---------REAKRtwprK--------N 88
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalsekelRKARR----QigmifqhfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQDPASTLnpKMTALDAVERAARVSvrgrrdarraaiDLLDKVGI-DKqlAQRKPSGLSGGQRQRVAIARALA 167
Cdd:PRK11153 93 LLSSRTVFDNVALPL--ELAGTPKAEIKARVT------------ELLELVGLsDK--ADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTV 221
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRV 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-210 |
5.50e-32 |
|
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: 116.67 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNErvtlFQ--GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI--ECAGVTreakrTWPRKNR 89
Cdd:cd03299 1 LKVENLSKDWKE----FKlkNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllNGKDIT-----NLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lMMQIVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVR 169
Cdd:cd03299 72 -DISYVPQNYA--LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHD 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-222 |
9.26e-32 |
|
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: 115.47 E-value: 9.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 43 VGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRTWPRKNR--LMMQivpqdpASTLNPKMTALDAVERA 116
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKigLVFQ------QYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 117 ARVSVRGRRDARRAaiDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQE 196
Cdd:cd03297 100 LKRKRNREDRISVD--ELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180
....*....|....*....|....*..
gi 2791281350 197 LNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03297 177 IKKNlNIPVIFVTHDLSEAEYLADRIV 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-210 |
1.14e-31 |
|
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: 120.94 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSC---VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKS----TLLRCLIGLNHAESGEI-----ECAGVTR 78
Cdd:COG4172 4 MPLLSVEDLSVafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlfdgqDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 79 EAKRTWpRKNRLMMqiVPQDPASTLNPKMT-------------ALDAVERAARVsvrgrrdarraaIDLLDKVGID--KQ 143
Cdd:COG4172 84 RELRRI-RGNRIAM--IFQEPMTSLNPLHTigkqiaevlrlhrGLSGAAARARA------------LELLERVGIPdpER 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 144 LAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDY--QAatKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG4172 149 RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvQA--QILDLLKDLQRElGMALLLITHD 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-228 |
5.04e-31 |
|
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: 113.68 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLS------CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI--ECAG----VTR 78
Cdd:COG4778 2 TTLLEVENLSktftlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvRHDGgwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 79 EAKRTWPRKNRLMMQIVPQdpasTLN--PKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQ 156
Cdd:COG4778 82 ASPREILALRRRTIGYVSQ----FLRviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPIGTAA 228
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-212 |
8.91e-31 |
|
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: 113.10 E-value: 8.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMqiVPQDPAstLNPKMTAL 110
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--KDITNLPPHKRPVNT--VFQNYA--LFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:cd03300 91 ENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
|
170 180
....*....|....*....|...
gi 2791281350 191 MSVLQELNSE-GMGIVLVSHDDE 212
Cdd:cd03300 170 QLELKRLQKElGITFVFVTHDQE 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-207 |
1.19e-30 |
|
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: 112.53 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWpRKNRLMMQ 93
Cdd:cd03224 1 LEVENLN-AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDPAstLNPKMTALDAVERAARVsvrGRRDARRAAID-LLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKL 172
Cdd:cd03224 79 YVPEGRR--IFPELTVEENLLLGAYA---RRRAKRKARLErVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2791281350 173 LLCDEITSALDYQAATKVMSVLQELNSEGMGIVLV 207
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLV 188
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-216 |
4.45e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCV--NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKN 88
Cdd:PRK13635 3 EEIIRVEHISFRypDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMqiVPQDP-----ASTL---------NPKMTALDAVERAArvsvrgrrdarraaiDLLDKVGIdKQLAQRKPSGLSG 154
Cdd:PRK13635 82 QVGM--VFQNPdnqfvGATVqddvafgleNIGVPREEMVERVD---------------QALRQVGM-EDFLNREPHRLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 155 GQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVL-VSHD-DELLQS 216
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDlDEAAQA 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-210 |
5.46e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 111.85 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLF--------QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKR 82
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFrrqqfeavKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 83 TWPRKNRLMMqiVPQDPASTLNPKM-------------TALDAVERAARVsvrgrrdarraaIDLLDKVGIDKQLAQRKP 149
Cdd:COG4167 82 YKYRCKHIRM--IFQDPNTSLNPRLnigqileeplrlnTDLTAEEREERI------------FATLRLVGLLPEHANFYP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 150 SGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNsEGMGI--VLVSHD 210
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQ-EKLGIsyIYVSQH 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-210 |
7.16e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPR-KNRLMM 92
Cdd:COG4559 2 LEAENLSVRLGGR-TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 qivPQdpASTLNPKMTALDAVE--RAARVSVRGRRDARRAAIdlLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALA--- 167
Cdd:COG4559 81 ---PQ--HSSLAFPFTVEEVVAlgRAPHGSSAAQDRQIVREA--LALVGLA-HLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2791281350 168 ----VRPKLLLCDEITSALD--YQAAtkVMSVLQELNSEGMGIVLVSHD 210
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDlaHQHA--VLRLARQLARRGGGVVAVLHD 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
29-222 |
1.35e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECA-----------GVTREAKRTWPRKNRLMMQIVPQ 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 98 DpaSTLNPKMTALDAV-ERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PRK10619 100 H--FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2791281350 177 EITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-210 |
1.47e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.61 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQI------VPQDpaS 101
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLrqhvgfVFQN--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TLNPKMTALDAV-ERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK11264 95 NLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 181 ALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-212 |
2.15e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.48 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 26 RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTwpRKnrlmMQIVPQDPAstL 103
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHARD--RK----VGFVFQHYA--L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDAV----------ERAARVSVRGRRDArraaidLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:PRK10851 86 FRHMTVFDNIafgltvlprrERPNAAAIKAKVTQ------LLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDE 212
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQE 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-222 |
2.37e-29 |
|
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: 109.45 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTReakrtWP--RKNRLMM----QIVpqdpasT 102
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGedITG-----LPphEIARLGIgrtfQIP------R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALDAVERAARVSVRGRRDARRAAI----------DLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKL 172
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSGLLLARARReereareraeELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2791281350 173 LLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-209 |
3.00e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQDP---ASTL-- 103
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdIRDLTLESLRRQ---IGVVPQDTflfSGTIre 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 -----NPKMTaLDAVERAARVSvrgrrdARRAAIDLLDKvGIDKQLAQRkpsG--LSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:COG1132 433 nirygRPDAT-DEEVEEAAKAA------QAHEFIEALPD-GYDTVVGER---GvnLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 177 EITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:COG1132 502 EATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-213 |
3.12e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.13 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNE---RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT----REAKRT 83
Cdd:PRK11629 3 KILLQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 84 WPRKNRL--MMQIvpqdpaSTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVA 161
Cdd:PRK11629 83 ELRNQKLgfIYQF------HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHR-ANHRPSELSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 162 IARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHDDEL 213
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQL 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-222 |
9.24e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQgLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTRE-AKRTWPRKNRLMM 92
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 Q---IVPQDpaSTLNPKMTALD-AVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:PRK11124 82 RnvgMVFQQ--YNLWPHLTVQQnLIEAPCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVV 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-214 |
1.57e-28 |
|
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: 112.55 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 2 PGAGAGAGASPVLRVSNLSCV-NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtreA 80
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRyPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV---D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 81 KRTWPRKN-RLMMQIVPQDP---ASTL--NPKMTALDAVERAARvsvrgrrdarraaiDLLDKVGIDKqLAQRKPSGL-- 152
Cdd:COG4987 399 LRDLDEDDlRRRIAVVPQRPhlfDTTLreNLRLARPDATDEELW--------------AALERVGLGD-WLAALPDGLdt 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 153 ---------SGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELL 214
Cdd:COG4987 464 wlgeggrrlSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL 533
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-222 |
2.63e-28 |
|
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: 106.30 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtreAKRTWPRKNRLMMQIVPQDPAst 102
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEARRRLGFVSDSTG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSAL 182
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 183 DYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVV 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-214 |
4.66e-28 |
|
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: 110.84 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKnr 89
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lmmQI--VPQDP---ASTL--NPKMTALDA----VERAARvsvrgrrdarraAIDLLDKV-----GIDKQLAQRkPSGLS 153
Cdd:TIGR02857 397 ---QIawVPQHPflfAGTIaeNIRLARPDAsdaeIREALE------------RAGLDEFVaalpqGLDTPIGEG-GAGLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 154 GGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELL 214
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA 520
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-221 |
5.64e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMM 92
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPASTL-----------NPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKqLAQRKPSGLSGGQRQRVA 161
Cdd:PRK13639 81 GIVFQNPDDQLfaptveedvafGPLNLGLSKEEVEKRVK------------EALKAVGMEG-FENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 162 IARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTV 221
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKV 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-214 |
6.12e-28 |
|
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: 106.57 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-----VTREAKRTWpRKNRLMMqiVPQDPAstLNPKMT 108
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaaMSRKELREL-RRKKISM--VFQSFA--LLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALDAVERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAAT 188
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180
....*....|....*....|....*...
gi 2791281350 189 KVMSVLQELNSE-GMGIVLVSHD-DELL 214
Cdd:cd03294 198 EMQDELLRLQAElQKTIVFITHDlDEAL 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-212 |
9.49e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE---SGEIECAGVTREAKRTWPRKnrl 90
Cdd:COG4136 2 LSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 mMQIVPQDPasTLNPKMT-------AL-DAVERAARvsvrgrrdaRRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAI 162
Cdd:COG4136 78 -IGILFQDD--LLFPHLSvgenlafALpPTIGRAQR---------RARVEQALEEAGLAG-FADRDPATLSGGQRARVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 163 ARALAVRPKLLLCDEITSALDYQAATKVMS-VLQELNSEGMGIVLVSHDDE 212
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-215 |
2.60e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL-NHAeSGEIECagvtreakrtwPRKNRLMM 92
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYG-SGRIAR-----------PAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 qiVPQDP---ASTLnpkMTAL------DAVERAArvsvrgrrdarraAIDLLDKVGIDK---QLAQRKP--SGLSGGQRQ 158
Cdd:COG4178 431 --LPQRPylpLGTL---REALlypataEAFSDAE-------------LREALEAVGLGHlaeRLDEEADwdQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQElNSEGMGIVLVSHDDELLQ 215
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAA 548
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-216 |
5.26e-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: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV--NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtreAKRTWPRKN-RL 90
Cdd:cd03246 1 LEVENVSFRypGAEPPVL-RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA---DISQWDPNElGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDpastlnpkmtaldaveraarvsvrgrrdarraaIDLLDKVGIDKQLaqrkpsglSGGQRQRVAIARALAVRP 170
Cdd:cd03246 77 HVGYLPQD---------------------------------DELFSGSIAENIL--------SGGQRQRLGLARALYGNP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQS 216
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-212 |
1.01e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLFqglsfavqrgtmvgvkGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREakrtwPRKNR 89
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLL----------------GPSGCGKTTVLRLIAGFETPDSGRIMLDGqdITHV-----PAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lMMQIVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVR 169
Cdd:PRK09452 87 -HVNTVFQSYA--LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDE 212
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQE 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-210 |
1.05e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.53 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQG-----LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRtwP-----RKNRL 90
Cdd:COG3840 5 DDLTYRYGdfplrFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltaLPPAER--PvsmlfQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQI-VPQDPASTLNPKMTaLDAVERAArvsvrgrrdarraAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALaVR 169
Cdd:COG3840 83 FPHLtVAQNIGLGLRPGLK-LTAEQRAQ-------------VEQALERVGLAG-LLDRLPGQLSGGQRQRVALARCL-VR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 170 PK-LLLCDEITSALDyQAATKVM-SVLQELNSE-GMGIVLVSHD 210
Cdd:COG3840 147 KRpILLLDEPFSALD-PALRQEMlDLVDELCRErGLTVLMVTHD 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-209 |
1.20e-26 |
|
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: 101.47 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSC-----VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEIECAGVTREaKRTWp 85
Cdd:cd03213 3 TLSFRNLTVtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD-KRSF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 86 rknRLMMQIVPQDpaSTLNPKMTALDAVERAARVSvrgrrdarraaidlldkvgidkqlaqrkpsGLSGGQRQRVAIARA 165
Cdd:cd03213 81 ---RKIIGYVPQD--DILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 166 LAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-222 |
2.66e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQgLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG----VTREAKRTWPRKNR 89
Cdd:COG4161 3 IQLKNINCFYGSHQALFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 LMMQIVPQDpaSTLNPKMTALD-AVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:COG4161 82 QKVGMVFQQ--YNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDK-ADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-212 |
2.78e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 2 PGAGAGAGASPVLRVSNLScvnnervTLFQG------LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG 75
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLT-------KSFDGqhavddVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 76 VTREAKRTWPRKNRLMMQ--------IVPQDPASTLnpKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIdKQLAQR 147
Cdd:PRK11607 81 VDLSHVPPYQRPINMMFQsyalfphmTVEQNIAFGL--KQDKLPKAEIASRVN------------EMLGLVHM-QEFAKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 148 KPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV-MSVLQELNSEGMGIVLVSHDDE 212
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQE 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-212 |
3.04e-26 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 101.29 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREakrtwPRKNRLMMQIVPQDPasTLNPKMTA 109
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdVVRE-----PREVRRRIGIVFQDL--SVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDAVERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATK 189
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180
....*....|....*....|....
gi 2791281350 190 VMSVLQELNSE-GMGIVLVSHDDE 212
Cdd:cd03265 170 VWEYIEKLKEEfGMTILLTTHYME 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-210 |
3.54e-26 |
|
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: 101.04 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV--NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPRKNRLM 91
Cdd:cd03263 1 LQIRNLTKTykKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDpaSTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPK 171
Cdd:cd03263 77 LGYCPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHD 210
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHS 191
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-212 |
7.70e-26 |
|
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: 102.57 E-value: 7.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 47 GPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQ--------IVPQDPASTLnpKMTALDAVERAAR 118
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQsyalfphmTVEENVAFGL--KMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 VSvrgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN 198
Cdd:TIGR01187 81 VL------------EALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170
....*....|....*
gi 2791281350 199 SE-GMGIVLVSHDDE 212
Cdd:TIGR01187 148 EQlGITFVFVTHDQE 162
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-213 |
9.33e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.24 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 26 RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-----VTREAKRTWPRKNrlmMQIVPQdpA 100
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqMDEEARAKLRAKH---VGFVFQ--S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 101 STLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLaQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK10584 97 FMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|....
gi 2791281350 181 ALDYQAATKVMSVLQELNSE-GMGIVLVSHDDEL 213
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHDLQL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-215 |
1.01e-25 |
|
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: 99.59 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIVPQDP--- 99
Cdd:cd03245 14 NQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT--DIRQLDPADLRRNIGYVPQDVtlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ASTL--NPKMTALDA----VERAARVSVRGrrdarraaiDLLDK--VGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPK 171
Cdd:cd03245 91 YGTLrdNITLGAPLAdderILRAAELAGVT---------DFVNKhpNGLDLQIGERG-RGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELLQ 215
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLD 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
28-225 |
1.02e-25 |
|
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: 99.21 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIvpqdPASTLNPKM 107
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALI----EAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAVERAARVsvrgrRDARRAAID-LLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:cd03268 88 TARENLRLLARL-----LGIRKKRIDeVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 187 ATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPIG 225
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-212 |
1.25e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtwPRKN 88
Cdd:COG4525 2 SMLTVRHVSVRypgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG----PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RlmmQIVPQDPAstLNPKMTALDAV------------ERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQ 156
Cdd:COG4525 78 R---GVVFQKDA--LLPWLNVLDNVafglrlrgvpkaERRARAE------------ELLALVGLA-DFARRRIWQLSGGM 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDyqAATKvmSVLQEL-----NSEGMGIVLVSHDDE 212
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALD--ALTR--EQMQELlldvwQRTGKGVFLITHSVE 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-214 |
1.68e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtwprknrlmmqIVPQDPASTLN 104
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-------------YVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDAVE--------------RAARVSVrgrrdarraaIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRP 170
Cdd:NF040873 70 LPLTVRDLVAmgrwarrglwrrltRDDRAAV----------DDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-216 |
2.03e-25 |
|
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: 103.67 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV-NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTReakRTWPRkNRLMM 92
Cdd:COG4618 331 LSVENLTVVpPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL---SQWDR-EELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QI--VPQDPAstLNP--------KMTALD--AVERAARvsvrgrrdarraaidlldKVGIDkQLAQRKPSG--------- 151
Cdd:COG4618 407 HIgyLPQDVE--LFDgtiaeniaRFGDADpeKVVAAAK------------------LAGVH-EMILRLPDGydtrigegg 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 152 --LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQS 216
Cdd:COG4618 466 arLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA 532
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-222 |
2.08e-25 |
|
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: 98.80 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGtMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTwPRKNRLMMQIVPQDPasTLNPKMTALD 111
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQ-PQKLRRRIGYLPQEF--GVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 AVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVM 191
Cdd:cd03264 92 FLDYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFR 170
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 192 SVLQELnSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03264 171 NLLSEL-GEDRIVILSTHIVEDVESLCNQVA 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-215 |
3.02e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.50 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNnervtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRK-NRL 90
Cdd:cd03215 3 PVLEVRGLSVKG-----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG--KPVTRRSPRDaIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPAST-LNPKMTaldaveraarvsvrgrrdarraaidLLDKVGIdkqlaqrkPSGLSGGQRQRVAIARALAVR 169
Cdd:cd03215 76 GIAYVPEDRKREgLVLDLS-------------------------VAENIAL--------SSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSElDELLG 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-222 |
3.78e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAK--RTWPRKnr 89
Cdd:PRK09536 2 PMIDVSDLS-VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaRAASRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lmMQIVPQDPASTLN------------PKMTALDAVERAARVSVRGRrdarraaidlLDKVGIDkQLAQRKPSGLSGGQR 157
Cdd:PRK09536 79 --VASVPQDTSLSFEfdvrqvvemgrtPHRSRFDTWTETDRAAVERA----------MERTGVA-QFADRPVTSLSGGER 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELV 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-210 |
3.78e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.34 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAEsGEIECAG-VTREAKRTWPRK--- 87
Cdd:PRK14258 6 PAIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrVEFFNQNIYERRvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NRLMMQIVPQDPASTLNPkMTALDAVERAAR-------VSVRGRRDARRAAIDLLDKVgidKQLAQRKPSGLSGGQRQRV 160
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKivgwrpkLEIDDIVESALKDADLWDEI---KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 161 AIARALAVRPKLLLCDEITSALDYQAATKVMSVLQ--ELNSEgMGIVLVSHD 210
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSE-LTMVIVSHN 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-211 |
3.78e-25 |
|
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: 97.81 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMq 93
Cdd:TIGR01189 1 LAARNLACSRGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 ivpqDPASTLNPKMTALD------AVERAARVSVRgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALA 167
Cdd:TIGR01189 79 ----GHLPGLKPELSALEnlhfwaAIHGGAQRTIE----------DALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDD 211
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-207 |
4.38e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.52 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLFqGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWpRKNRL 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH-RIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPAstLNPKMTALDAVERAARVSVRGRRDArraaiDLLDKV-GIDKQLAQRK--PSG-LSGGQRQRVAIARAL 166
Cdd:COG0410 79 GIGYVPEGRR--IFPSLTVEENLLLGAYARRDRAEVR-----ADLERVyELFPRLKERRrqRAGtLSGGEQQMLAIGRAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2791281350 167 AVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLV 207
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-222 |
4.61e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTR-------------------------EAKR 82
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigylpqeppldddltvldtvldgdaELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 83 TWPRKNRLMMQIVPQDP----ASTLNPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQ 158
Cdd:COG0488 92 LEAELEELEAKLAEPDEdlerLAELQEEFEALGGWEAEARAE------------EILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDyqaatkVMSV--LQE-LNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLD------LESIewLEEfLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-224 |
5.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRtWPRKnrlMMQIVPQDP-----ASTL- 103
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGreVNAENEK-WVRS---KVGLVFQDPddqvfSSTVw 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 -----NPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:PRK13647 99 ddvafGPVNMGLDKDEVERRVE------------EALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2791281350 179 TSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPI 224
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVL 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-214 |
5.84e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 97.72 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGlnhAESGEIEcAGVTREAKRTWPRKNRLMMQIVPQDPAstlnpkm 107
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPV-AGCVDVPDNQFGREASLIDAIGRKGDF------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 taLDAVEraarvsvrgrrdarraaidLLDKVGI-DKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:COG2401 113 --KDAVE-------------------LLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*....
gi 2791281350 187 ATKVMSVLQELNSE-GMGIVLVSHDDELL 214
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATHHYDVI 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-210 |
8.77e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPR----K 87
Cdd:PRK13548 1 AMLEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG---RPLADWSPaelaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NRLMMqivPQdpASTLNPKMTALDAVE--RAARVSVRGRRDARRAaiDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARA 165
Cdd:PRK13548 77 RRAVL---PQ--HSSLSFPFTVEEVVAmgRAPHGLSRAEDDALVA--AALAQVDLA-HLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 166 LA------VRPKLLLCDEITSALDYQAATKVMSVLQEL-NSEGMGIVLVSHD 210
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHD 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
27-210 |
1.37e-24 |
|
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: 96.55 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTReakrtWPRKNR-LMMqiVPQDPAstL 103
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdVTD-----LPPKDRdIAM--VFQNYA--L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALD 183
Cdd:cd03301 84 YPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 184 ----YQAATKVMSVLQELnseGMGIVLVSHD 210
Cdd:cd03301 163 aklrVQMRAELKRLQQRL---GTTTIYVTHD 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-209 |
1.52e-24 |
|
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: 97.23 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIVPQDP---ASTL 103
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNLRWLRSQIGLVSQEPvlfDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 --NPKMTALDA----VERAARVSvrgrrDARRAAIDLLDkvGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLCDE 177
Cdd:cd03249 94 aeNIRYGKPDAtdeeVEEAAKKA-----NIHDFIMSLPD--GYDTLVGERG-SQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190
....*....|....*....|....*....|..
gi 2791281350 178 ITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA-MKGRTTIVIAH 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
43-214 |
1.67e-24 |
|
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: 99.42 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 43 VGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT----REAKRTWPRKNRLmmQIVPQDP--------ASTLNPKMTAL 110
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsRKGIFLPPEKRRI--GYVFQEArlfphlsvRGNLRYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARvsvrgrrdaRRAAIDLLdkvGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:TIGR02142 104 RPSERRIS---------FERVIELL---GIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180
....*....|....*....|....*.
gi 2791281350 191 MSVLQELNSE-GMGIVLVSHD-DELL 214
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSlQEVL 196
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-209 |
1.82e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.41 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLFqGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN------HAEsGEIECAGVTREAKRTWP 85
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALK-DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgaRVE-GEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 86 ---RKnRLMMqiVPQDPastlNP-------------------KMTALDA-VERAarvsvrgrrdarraaidlLDKVGI-- 140
Cdd:COG1117 88 velRR-RVGM--VFQKP----NPfpksiydnvayglrlhgikSKSELDEiVEES------------------LRKAALwd 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 141 ---DKqLaQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgMGIVLVSH 209
Cdd:COG1117 143 evkDR-L-KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTH 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-211 |
2.00e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRtwPRKNRLMM 92
Cdd:PRK13538 1 MLEARNLACERDERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR--DEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIvpqDPASTLNPKMTALDAVERAARVSvrgRRDARRAAIDLLDKVGidkqLAQRK--PSG-LSGGQRQRVAIARALAVR 169
Cdd:PRK13538 78 YL---GHQPGIKTELTALENLRFYQRLH---GPGDDEALWEALAQVG----LAGFEdvPVRqLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 170 PKLLLCDEITSALDYQAatkvMSVLQELNSE-----GMgIVLVSHDD 211
Cdd:PRK13538 148 APLWILDEPFTAIDKQG----VARLEALLAQhaeqgGM-VILTTHQD 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-212 |
2.34e-24 |
|
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: 96.60 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMQ 93
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--EDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDPAstLNPKMTALDAV------------ERAARVSvrgrrdarraaiDLLDKVGID-KQLAQRKPSGLSGGQRQRV 160
Cdd:cd03295 79 YVIQQIG--LFPHMTVEENIalvpkllkwpkeKIRERAD------------ELLALVGLDpAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 161 AIARALAVRPKLLLCDEITSALDyqAATKvmSVLQE----LNSE-GMGIVLVSHD-DE 212
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALD--PITR--DQLQEefkrLQQElGKTIVFVTHDiDE 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-215 |
4.34e-24 |
|
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: 95.69 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTReakrtWP--RKNR 89
Cdd:cd03218 1 LRAENLSKRYGKRKVV-NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqdITK-----LPmhKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 LMMQIVPQDPasTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVR 169
Cdd:cd03218 75 LGIGYLPQEA--SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLS 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-212 |
1.27e-23 |
|
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: 94.77 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNH-AESGEIECAGVTREAKRTWPRKNR 89
Cdd:COG1119 1 DPLLELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lmMQIVPQDPASTLNPKMTALDAV------------------ERAARvsvrgrrdarraaiDLLDKVGIDkQLAQRKPSG 151
Cdd:COG1119 80 --IGLVSPALQLRFPRDETVLDVVlsgffdsiglyreptdeqRERAR--------------ELLELLGLA-HLADRPFGT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 152 LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEG-MGIVLVSHDDE 212
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVE 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
26-222 |
1.89e-23 |
|
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: 93.50 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 26 RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTwprknrlmMQIVPQDPAstL 103
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAARNR--------IGYLPEERG--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALD 183
Cdd:cd03269 82 YPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 184 YQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-215 |
2.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.67 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLS-CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKR-TWPRKN 88
Cdd:PRK13632 5 SVMIKVENVSfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 rlmMQIVPQDP-------------ASTLNPKMtaLDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLaQRKPSGLSGG 155
Cdd:PRK13632 85 ---IGIIFQNPdnqfigatveddiAFGLENKK--VPPKKMKDIID------------DLAKKVGMEDYL-DKEPQNLSGG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 156 QRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVL-VSHD-DELLQ 215
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDmDEAIL 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-224 |
2.24e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL---NHAESGEIECAG--VTREAKRTWP-R 86
Cdd:PRK09984 4 IIRVEKLAKTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtVQREGRLARDiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 KNRLMMQIVPQDpaSTLNPKMTALDAVERAARVSVRG--------RRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQ 158
Cdd:PRK09984 83 KSRANTGYIFQQ--FNLVNRLSVLENVLIGALGSTPFwrtcfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHDDELLQSYCSTVIPI 224
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-209 |
2.40e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTRE-AKRTWPRK--------NRLMMQIVPQDPAS 101
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRRqvgvvlqeNVLFNRSIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TlNPKMTaLDAVERAARVSvrgrrdarrAAIDLLDKV--GIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:cd03252 99 A-DPGMS-MERVIEAAKLA---------GAHDFISELpeGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 180 SALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:cd03252 167 SALDYESEHAIMRNMHDI-CAGRTVIIIAH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-222 |
2.58e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECaGVTreakrtwprknrlm 91
Cdd:COG0488 314 KVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET-------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQI--VPQDPAsTLNPKMTALDAVERAARvsvrgrRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVR 169
Cdd:COG0488 378 VKIgyFDQHQE-ELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 170 PKLLLCDEITSALDyqaatkvMSVLQELNS-----EGmGIVLVSHDDELLQSYCSTVI 222
Cdd:COG0488 451 PNVLLLDEPTNHLD-------IETLEALEEalddfPG-TVLLVSHDRYFLDRVATRIL 500
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-215 |
3.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.77 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNER----VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNR 89
Cdd:PRK13651 3 IKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 LMMQIVPQDPASTLNPKMTAL------------------------------------DAVERAArvsvrgrrdarraaiD 133
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIrrrvgvvfqfaeyqlfeqtiekdiifgpvsmgvskeEAKKRAA---------------K 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 134 LLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DE 212
Cdd:PRK13651 148 YIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDN 227
|
...
gi 2791281350 213 LLQ 215
Cdd:PRK13651 228 VLE 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-227 |
4.77e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.79 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLnHAESGEIEcaGVTREAKR---TWPRK--NRL---MMQIVPQD 98
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIG--GSATFNGReilNLPEKelNKLraeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 99 PASTLNP----------------KMTALDAVERAARvsvrgrrdarraaidLLDKVgidKQLAQRK-----PSGLSGGQR 157
Cdd:PRK09473 106 PMTSLNPymrvgeqlmevlmlhkGMSKAEAFEESVR---------------MLDAV---KMPEARKrmkmyPHEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD--------DELLQSYCSTVIPIGTA 227
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDlgvvagicDKVLVMYAGRTMEYGNA 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-226 |
8.70e-23 |
|
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: 92.40 E-value: 8.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtreakRTWPRKNRLMMQI------------ 94
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-----VPWKRRKKFLRRIgvvfgqktqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 -VPQDPASTLNPKMTALDAVERAARVSvrgrrdarrAAIDLLDKVGIDKQLAQRkpsgLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03267 109 dLPVIDSFYLLAAIYDLPPARFKKRLD---------ELSELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVIPIGT 226
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-215 |
8.75e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV------TREAKRtwprknrLMMQIVPQDPAstLN 104
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsPRDAQA-------AGIAIIHQELN--LV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALD-----------------AVERAARvsvrgrrdarraaiDLLDKVGIDKQLAqRKPSGLSGGQRQRVAIARALA 167
Cdd:COG1129 92 PNLSVAEniflgreprrgglidwrAMRRRAR--------------ELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFE 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-209 |
9.44e-23 |
|
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: 92.29 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKnrlMMQIVPQDpaSTL---- 103
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdIREVTLDSLRR---AIGVVPQD--TVLfndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 ---NPKMTALDA----VERAARVSvrgrrdarraaiDLLDKV-----GIDKQLAQRkpsG--LSGGQRQRVAIARALAVR 169
Cdd:cd03253 91 igyNIRYGRPDAtdeeVIEAAKAA------------QIHDKImrfpdGYDTIVGER---GlkLSGGEKQRVAIARAILKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-215 |
1.18e-22 |
|
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: 90.29 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECagvtreakrtwPRKNRLMMq 93
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 iVPQDP---ASTLnpkmtaLDAVeraarvsvrgrrdarraaIDLLDKVgidkqlaqrkpsgLSGGQRQRVAIARALAVRP 170
Cdd:cd03223 69 -LPQRPylpLGTL------REQL------------------IYPWDDV-------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQElnsEGMGIVLVSHDDELLQ 215
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGHRPSLWK 152
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-214 |
1.42e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.09 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLScvnneRVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPR---KN 88
Cdd:COG1129 255 VVLEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG--KPVRIRSPRdaiRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMqiVPQDPAST-LNPKM--------TALDAVERAARVSVRGRRDARRAAIDLLD-KVGIDKQLAqrkpSGLSGGQRQ 158
Cdd:COG1129 328 GIAY--VPEDRKGEgLVLDLsirenitlASLDRLSRGGLLDRRRERALAEEYIKRLRiKTPSPEQPV----GNLSGGNQQ 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELL 214
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELL 458
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-210 |
1.67e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNL-------SCVNNeRVT----LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV---T 77
Cdd:PRK10261 312 PILQVRNLvtrfplrSGLLN-RVTrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 78 REAKRTWP-RKNrlmMQIVPQDPASTLNPKMTALDAVERAARVSVRGRRDARRAAID-LLDKVGIDKQLAQRKPSGLSGG 155
Cdd:PRK10261 391 LSPGKLQAlRRD---IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAwLLERVGLLPEHAWRYPHEFSGG 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 156 QRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHD 523
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-222 |
1.72e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQDPASTLNPKmTAL 110
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLKKLRKKVSLVFQFPEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190
....*....|....*....|....*....|..
gi 2791281350 191 MSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13641 185 MQLFKDYQKAGHTVILVTHNMDDVAEYADDVL 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-216 |
1.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMM---------- 92
Cdd:PRK13650 17 DQEKYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMvfqnpdnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 -QIVPQDPASTLNPKmtALDAVERAARVSvrgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPK 171
Cdd:PRK13650 96 gATVEDDVAFGLENK--GIPHEEMKERVN------------EALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD-DELLQS 216
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDlDEVALS 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-211 |
2.46e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFqGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQDPAST 102
Cdd:PRK13649 19 EGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlITSTSKNKDIKQIRKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKmTALDAV--------------ERAARvsvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:PRK13649 98 LFEE-TVLKDVafgpqnfgvsqeeaEALAR--------------EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH--DD 211
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlmDD 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-207 |
2.75e-22 |
|
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: 91.05 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKnRLMMQ 93
Cdd:TIGR03410 1 LEVSNLNVYYGQSHIL-RGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA-RAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQ--DPASTLNPK---MTALDAVERAARvsvrgrrdarraAI--DLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARAL 166
Cdd:TIGR03410 79 YVPQgrEIFPRLTVEenlLTGLAALPRRSR------------KIpdEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2791281350 167 AVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLV 207
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLV 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-229 |
4.11e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtwPRKNRLM 91
Cdd:PRK13539 1 MMLEGEDLACVRGGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD----PDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDPastLNPKMTALDAVERAARVsvrgRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPK 171
Cdd:PRK13539 76 HYLGHRNA---MKPALTVAENLEFWAAF----LGGEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQE-LNSEGMgIVLVSHDDelLQSYCSTVIPIGTAAV 229
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAhLAQGGI-VIAATHIP--LGLPGARELDLGPFAA 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
25-210 |
4.31e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQdpAST 102
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdVATLDADALAQLRREHFGFIFQ--RYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRkPSGLSGGQRQRVAIARALAVRPKLLLCDEITSAL 182
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180
....*....|....*....|....*...
gi 2791281350 183 DYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-212 |
6.15e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNER----VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPR-- 86
Cdd:PRK13631 21 ILRVKNLYCVFDEKqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHEli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 --------KN----RLMMQIVPQDPASTL--------------NPKMTALDAVERAARvsvrgrrdarraaidLLDKVGI 140
Cdd:PRK13631 101 tnpyskkiKNfkelRRRVSMVFQFPEYQLfkdtiekdimfgpvALGVKKSEAKKLAKF---------------YLNKMGL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 141 DKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDE 212
Cdd:PRK13631 166 DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-218 |
6.86e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLM 91
Cdd:PRK11231 3 LRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQI--VPQD------------PASTLNPKMTALD--AVERAarvsvrgrrdarraaidlLDKVGIDkQLAQRKPSGLSGG 155
Cdd:PRK11231 82 PQHhlTPEGitvrelvaygrsPWLSLWGRLSAEDnaRVNQA------------------MEQTRIN-HLADRRLTDLSGG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 156 QRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYC 218
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYC 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-210 |
8.18e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE-----SGEIECAGVT----R 78
Cdd:PRK15134 3 QPLLAIENLSVAfrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESllhaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 79 EAKRTWPRKNRLMMqiVPQDPASTLNPkmtaLDAVER---------------AARVSVrgrrdarraaIDLLDKVGIdKQ 143
Cdd:PRK15134 83 EQTLRGVRGNKIAM--IFQEPMVSLNP----LHTLEKqlyevlslhrgmrreAARGEI----------LNCLDRVGI-RQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 144 LAQR---KPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK15134 146 AAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHN 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
31-214 |
8.45e-22 |
|
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: 89.83 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGeiecaGVTREAKR-TWPRKNRLmmqIVPQDPAstLNPKMTA 109
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG-----GVILEGKQiTEPGPDRM---VVFQNYS--LLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDAVERAARVSVRGRRDARRAAI--DLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDyqAA 187
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIveEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD--AL 148
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 188 TKvmSVLQE-----LNSEGMGIVLVSHD-DELL 214
Cdd:TIGR01184 149 TR--GNLQEelmqiWEEHRVTVLMVTHDvDEAL 179
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-209 |
1.08e-21 |
|
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: 87.48 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRK-NRLMMQIVPQdpastlnpkmtal 110
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--KEVSFASPRDaRRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 daveraarvsvrgrrdarraaidlldkvgidkqlaqrkpsgLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170
....*....|....*....
gi 2791281350 191 MSVLQELNSEGMGIVLVSH 209
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISH 140
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-210 |
1.18e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.99 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTlFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECA---GVTRE-AKRTWPRK 87
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdGQLRDlYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NRLMMQ---IVPQDPASTLNPKMTALDAV-ERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIA 163
Cdd:PRK11701 84 RRLLRTewgFVHQHPRDGLRMQVSAGGNIgERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 164 RALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHD 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-209 |
1.73e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.93 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTReakrtWP--RK 87
Cdd:COG1137 2 MTLEAENLVKSYGKRTVV-KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedITH-----LPmhKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 88 NRLMMQIVPQDP------------ASTLnpKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKqLAQRKPSGLSGG 155
Cdd:COG1137 76 ARLGIGYLPQEAsifrkltvedniLAVL--ELRKLSKKEREERLE------------ELLEEFGITH-LRKSKAYSLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 156 QRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-222 |
1.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNN-----ERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKN 88
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQDPASTL-----------NPKMTALDAVERAARVsvrgrrdarraaIDLLDKVGIDKQ-LAQRKPSGLSGGQ 156
Cdd:PRK13637 82 RKKVGLVFQYPEYQLfeetiekdiafGPINLGLSEEEIENRV------------KRAMNIVGLDYEdYKDKSPFELSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRII 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-210 |
3.44e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL---NHAESGEIECAGVTREAKRTWPRKNRLmmQIVPQDPASTLNPKMTA 109
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREKV--GIVFQNPDNQFVGATVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LD--------AVERAARVSVRGrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:PRK13640 104 DDvafglenrAVPRPEMIKIVR---------DVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 182 LDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKnNLTVISITHD 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-209 |
3.65e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGL----SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRtwP-----RKNRLMMQI- 94
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhttTPPSRR--PvsmlfQENNLFSHLt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQDPASTLNPKMTaLDAVERAARVsvrgrrdarraaiDLLDKVGIDKQLaQRKPSGLSGGQRQRVAIARALAVRPKLLL 174
Cdd:PRK10771 88 VAQNIGLGLNPGLK-LNAAQREKLH-------------AIARQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSH 209
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSH 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-216 |
4.92e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNR-----------LMMQIVP 96
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREVPFLRRqigmifqdhhlLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 97 QDPASTLNPKMTALDAVERaaRVSVRgrrdarraaidlLDKVGI-DKqlAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRR--RVSAA------------LDKVGLlDK--AKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQS 216
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISR 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
6.36e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.54 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQgLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQDPAST 102
Cdd:PRK13634 19 ERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvITAGKKNKKLKPLRKKVGIVFQFPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 L--------------NPKMTALDAVERAArvsvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:PRK13634 98 LfeetvekdicfgpmNFGVSEEDAKQKAR---------------EMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIV 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-209 |
1.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQDPASTLNPKmTAL 110
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170
....*....|....*....
gi 2791281350 191 MSVLQELNSEGMGIVLVSH 209
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTH 202
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-216 |
1.26e-20 |
|
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: 89.71 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCV--NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtreAKRTWPRkNRL 90
Cdd:TIGR01842 316 HLSVENVTIVppGGKKPTL-RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA---DLKQWDR-ETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQI--VPQDP---ASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKvGIDKQLAQRKpSGLSGGQRQRVAIARA 165
Cdd:TIGR01842 391 GKHIgyLPQDVelfPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPD-GYDTVIGPGG-ATLSGGQRQRIALARA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 166 LAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQS 216
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC 519
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-210 |
1.61e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIeCAGVT--REAKRtwprKNRLMMQivpqdpASTLNP 105
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAplAEARE----DTRLMFQ------DARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAV---------ERAARVsvrgrrdarraaidlLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PRK11247 95 WKKVIDNVglglkgqwrDAALQA---------------LAAVGLADR-ANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 177 EITSALDyqAATKVMsvLQEL-----NSEGMGIVLVSHD 210
Cdd:PRK11247 159 EPLGALD--ALTRIE--MQDLieslwQQHGFTVLLVTHD 193
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
32-183 |
1.63e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.49 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-----VTREAKRTwprknrlMMQIVPQDPA---STL 103
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdVTQASLRA-------AIGIVPQDTVlfnDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 -------NPKMTAlDAVERAARVSvrgrrdARRAAIDLLDKvGIDKQLAQR--KpsgLSGGQRQRVAIARALAVRPKLLL 174
Cdd:COG5265 449 ayniaygRPDASE-EEVEAAARAA------QIHDFIESLPD-GYDTRVGERglK---LSGGEKQRVAIARTLLKNPPILI 517
|
....*....
gi 2791281350 175 CDEITSALD 183
Cdd:COG5265 518 FDEATSALD 526
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
31-209 |
1.65e-20 |
|
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: 89.42 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQ----------DP 99
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdLAIADPAWLRRQ---MGVVLQenvlfsrsirDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ASTLNPKMTaLDAVERAARVSvrgrrdARRAAIDLLdKVGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:TIGR01846 551 IALCNPGAP-FEHVIHAAKLA------GAHDFISEL-PQGYNTEVGE-KGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 180 SALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:TIGR01846 622 SALDYESEALIMRNMREI-CRGRTVIIIAH 650
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-204 |
1.95e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.77 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLF--------QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTW 84
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 PRKNRLMMqiVPQDPASTLNPKM-------------TALDAVERAARVsvrgrrdarraaIDLLDKVGIDKQLAQRKPSG 151
Cdd:PRK15112 84 YRSQRIRM--IFQDPSTSLNPRQrisqildfplrlnTDLEPEQREKQI------------IETLRQVGLLPDHASYYPHM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 152 LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNsEGMGI 204
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQ-EKQGI 201
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-209 |
2.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNRLMM-----------QIVPQDPA 100
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDEENLWDIRNKAGMvfqnpdnqivaTIVEEDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 101 stLNPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK13633 109 --FGPENLGIPPEEIRERVD------------ESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 181 ALDYQAATKVMSVLQELNSE-GMGIVLVSH 209
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-222 |
3.46e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.15 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRL 90
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG--EDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPA--------STLNPKMTALDAVERAArvsvrgrrdarraAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAI 162
Cdd:PRK10247 82 QVSYCAQTPTlfgdtvydNLIFPWQIRNQQPDPAI-------------FLDDLERFALPDTILTKNIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 163 ARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD-DELlqSYCSTVI 222
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDkDEI--NHADKVI 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-210 |
3.65e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQG---LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGL------NHAESGEIEcagvTREAKRT 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAvdrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEKLEFN----GQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 84 WPRKNRLM----MQIVPQDPASTLNPKMTALDAVERAARVSVR-GRRDARRAAIDLLDKVGIDKQLAQRK--PSGLSGGQ 156
Cdd:PRK11022 79 SEKERRNLvgaeVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRLDvyPHQLSGGM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 157 RQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHD 210
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHD 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-211 |
4.17e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.47 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMQ 93
Cdd:cd03231 1 LEADELTCERDGR-ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--GPLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQDPAStlnpkmTALDAVEraaRVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03231 78 LGHAPGIK------TTLSVLE---NLRFWHADHSDEQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDD 211
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-210 |
4.29e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCV---NNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREakrtwpRKNR 89
Cdd:PRK10261 12 VLAVENLNIAfmqEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR------RRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 LM------------------MQIVPQDPASTLNPKMTALDAVERAARVSVRGRRDARRAAID-LLDKVGI--DKQLAQRK 148
Cdd:PRK10261 86 QVielseqsaaqmrhvrgadMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKrMLDQVRIpeAQTILSRY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 149 PSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHD 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-222 |
5.84e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRtwprknrlmmQI--VPQDPAstLNPKM 107
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDRR----------RIgyLPEERG--LYPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAV----------ERAARVSVRgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDE 177
Cdd:COG4152 87 KVGEQLvylarlkglsKAEAKRRAD----------EWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2791281350 178 ITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIV 200
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-209 |
8.35e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.24 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 20 SCVNNERVT--LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNH---AESGEIECAGVtreakrtwPRKNRLMMQI 94
Cdd:cd03234 11 LKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ--------PRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 ---VPQDpaSTLNPKMTALDAVERAA----RVSVRGRRDARRAAIDLLDKVGiDKQLAQRKPSGLSGGQRQRVAIARALA 167
Cdd:cd03234 83 vayVRQD--DILLPGLTVRETLTYTAilrlPRKSSDAIRKKRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-209 |
8.76e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE-----SGEIECAGVTREAKRTWP 85
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 86 RKNRLMMQIVPQDPastlNP-KMTALDAVERAARVSVRGRRDARRAAID-------LLDKVgidKQLAQRKPSGLSGGQR 157
Cdd:PRK14239 82 VDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEkslkgasIWDEV---KDRLHDSALGLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgMGIVLVSH 209
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTR 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-224 |
9.18e-20 |
|
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: 82.11 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcagvtreakrtwpRKNRLMMQ 93
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------WGSTVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 IVPQdpastlnpkmtaldaveraarvsvrgrrdarraaidlldkvgidkqlaqrkpsgLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSegmGIVLVSHDDELLQSYCSTVIPI 224
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIEL 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-222 |
9.92e-20 |
|
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: 84.12 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 20 SCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreakrtwprknrlmmQIVPQ-D 98
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----------------RVSSLlG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 99 PASTLNPKMTALDAVERAARV---SVRGRRDARRAAIDL--LDKVgIDKQLaqrkpSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:cd03220 91 LGGGFNPELTGRENIYLNGRLlglSRKEIDEKIDEIIEFseLGDF-IDLPV-----KTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRAL 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-209 |
1.39e-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: 83.81 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 23 NNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKnrlMMQIVPQDP-- 99
Cdd:cd03254 13 DEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSLRS---MIGVVLQDTfl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 -ASTL--NPKMTALDAveRAARVSVRGRRDARRAAIDLLDKvGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:cd03254 89 fSGTImeNIRLGRPNA--TDEEVIEAAKEAGAHDFIMKLPN-GYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 177 EITSALDYQAATKVMSVLQELNsEGMGIVLVSH 209
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLM-KGRTSIIIAH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-215 |
1.46e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLM 91
Cdd:COG3845 256 VVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG--EDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 -MQIVPQDPAST-LNPKMTALD---------------------AVERAARvsvrgrrdarraaiDLLDKVGIDKQLAQRK 148
Cdd:COG3845 334 gVAYIPEDRLGRgLVPDMSVAEnlilgryrrppfsrggfldrkAIRAFAE--------------ELIEEFDVRTPGPDTP 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 149 PSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILA 467
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-212 |
1.62e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtwPRKNRlmmQIVPQDPAstLNPKMTAL 110
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG----PGAER---GVVFQNEG--LLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDY----QA 186
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftreQM 167
|
170 180
....*....|....*....|....*.
gi 2791281350 187 ATKVMSVLQElnsEGMGIVLVSHDDE 212
Cdd:PRK11248 168 QTLLLKLWQE---TGKQVLLITHDIE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-218 |
1.68e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTWPRKNRLMMQIVPQdpASTLNPKM 107
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRARHARQRVGVVPQ--FDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAA 187
Cdd:PRK13537 96 TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 188 TKVMSVLQELNSEGMGIVLVSHDDELLQSYC 218
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHFMEEAERLC 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-209 |
2.37e-19 |
|
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: 82.54 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQ--------IVPQDPASTLN 104
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQennlfahlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 P--KMTALD--AVERAARvsvrgrrdarraaidlldKVGIDKQLAqRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:cd03298 97 PglKLTAEDrqAIEVALA------------------RVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 181 ALDYQAATKVMSVLQELNSE-GMGIVLVSH 209
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAEtKMTVLMVTH 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-209 |
3.38e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE---SGEIECAGVTREAKrtwprKNRLM 91
Cdd:TIGR00955 26 RLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK-----EMRAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDpaSTLNPKMTALDA---------------VERAARVSvrgrrdarraaiDLLDKVGIDK------QLAQRKpS 150
Cdd:TIGR00955 101 SAYVQQD--DLFIPTLTVREHlmfqahlrmprrvtkKEKRERVD------------EVLQALGLRKcantriGVPGRV-K 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 151 GLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-183 |
3.62e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKrtwprKNRLMMqIVPQDPAstLNP 105
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSI-----QQRDIC-MVFQSYA--LFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 ------------KMTALDAVERAARVSvrgrrdarrAAIDLLDKVGI-DKQLAQrkpsgLSGGQRQRVAIARALAVRPKL 172
Cdd:PRK11432 92 hmslgenvgyglKMLGVPKEERKQRVK---------EALELVDLAGFeDRYVDQ-----ISGGQQQRVALARALILKPKV 157
|
170
....*....|.
gi 2791281350 173 LLCDEITSALD 183
Cdd:PRK11432 158 LLFDEPLSNLD 168
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-209 |
3.63e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRC---LIGLNHAE--SGEIECAGVTREAKRTWPRKNRLMMQIVPQDPASTlnP 105
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPF--P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAVERAARVS--VRGRRDARRAAIDLLDKVGIDKQLAQR---KPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK14267 99 HLTIYDNVAIGVKLNglVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180
....*....|....*....|....*....
gi 2791281350 181 ALDYQAATKVMSVLQELNSEgMGIVLVSH 209
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
29-209 |
4.30e-19 |
|
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: 85.38 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtWPRK---NRLMMqiVPQDP---AST 102
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE---IPREvlaNSVAM--VDQDIflfEGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALD------AVERAARvsvrgrrdarraaiD--LLDKV-----GIDKQLAQrKPSGLSGGQRQRVAIARALAVR 169
Cdd:TIGR03796 569 VRDNLTLWDptipdaDLVRACK--------------DaaIHDVItsrpgGYDAELAE-GGANLSGGQRQRLEIARALVRN 633
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 170 PKLLLCDEITSALDyqAATKVMsVLQELNSEGMGIVLVSH 209
Cdd:TIGR03796 634 PSILILDEATSALD--PETEKI-IDDNLRRRGCTCIIVAH 670
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-212 |
7.70e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT----REAKRTWPRKN 88
Cdd:PRK14246 10 VFNISRLYLYINDKAIL-KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQDPASTlnPKMTALDAVERAARV-SVRGRRDARRAAIDLLDKVGIDKQLAQR---KPSGLSGGQRQRVAIAR 164
Cdd:PRK14246 89 RKEVGMVFQQPNPF--PHLSIYDNIAYPLKShGIKEKREIKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgMGIVLVSHDDE 212
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-222 |
8.09e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 25 ERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreaKRTWPrknrLmmqivpqDPASTLN 104
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RVSAL----L-------ELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDAVERAARvsvrgrrdarraaidLLdkvGIDK-QLAQRKP-----SGL-----------SGGQRQRVAIARALA 167
Cdd:COG1134 101 PELTGRENIYLNGR---------------LL---GLSRkEIDEKFDeivefAELgdfidqpvktySSGMRARLAFAVATA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-216 |
1.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNL--SCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRL 90
Cdd:PRK13642 4 ILEVENLvfKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMqiVPQDPASTLNPKMTALDAV-----ERAARVSVRGRRDARRAAIDLLDkvgidkqLAQRKPSGLSGGQRQRVAIARA 165
Cdd:PRK13642 84 GM--VFQNPDNQFVGATVEDDVAfgmenQGIPREEMIKRVDEALLAVNMLD-------FKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 166 LAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD-DELLQS 216
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDlDEAASS 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-209 |
1.49e-18 |
|
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: 80.68 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQ--------IVPQDP 99
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQennlfahlTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ASTLNPKMTaLDAVERAARVSVRGrrdarraaidlldKVGIDKQLAqRKPSGLSGGQRQRVAIARALaVRPK-LLLCDEI 178
Cdd:TIGR01277 92 GLGLHPGLK-LNAEQQEKVVDAAQ-------------QVGIADYLD-RLPEQLSGGQRQRVALARCL-VRPNpILLLDEP 155
|
170 180 190
....*....|....*....|....*....|..
gi 2791281350 179 TSALDYQAATKVMSVLQELNSE-GMGIVLVSH 209
Cdd:TIGR01277 156 FSALDPLLREEMLALVKQLCSErQRTLLMVTH 187
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
30-198 |
1.54e-18 |
|
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: 83.85 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI-----ECAGVTREAKRtwpRKnrlmMQIVPQD----PA 100
Cdd:TIGR03797 469 LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqDLAGLDVQAVR---RQ----LGVVLQNgrlmSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 101 STLN----PKMTALDAVERAARVsvrgrrdarraaidlldkVGIDKQLaQRKPSG-----------LSGGQRQRVAIARA 165
Cdd:TIGR03797 542 SIFEniagGAPLTLDEAWEAARM------------------AGLAEDI-RAMPMGmhtvisegggtLSGGQRQRLLIARA 602
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 166 LAVRPKLLLCDEITSALDYQAATKVMSVLQELN 198
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLK 635
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-196 |
1.58e-18 |
|
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: 80.62 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIVPQDP-------ASTLN 104
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV--DISKIGLHDLRSRISIIPQDPvlfsgtiRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDA-VERA-ARVSVRGRRDARRAAIDLLDKVGidkqlaqrkPSGLSGGQRQRVAIARALAVRPKLLLCDEITSAL 182
Cdd:cd03244 100 PFGEYSDEeLWQAlERVGLKEFVESLPGGLDTVVEEG---------GENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170
....*....|....
gi 2791281350 183 DYQAATKVMSVLQE 196
Cdd:cd03244 171 DPETDALIQKTIRE 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-197 |
1.91e-18 |
|
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: 80.74 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKnrlMMQIVPQDP---ASTL----- 103
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdVRDYTLASLRR---QIGLVSQDVflfNDTVaenia 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 --NPKMTAlDAVERAARVSvrgrrdARRAAIDLLDKvGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:cd03251 98 ygRPGATR-EEVEEAARAA------NAHEFIMELPE-GYDTVIGERG-VKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170
....*....|....*.
gi 2791281350 182 LDYQAATKVMSVLQEL 197
Cdd:cd03251 169 LDTESERLVQAALERL 184
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-216 |
2.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI--ECAGVTREAKRTWpRK----------NRLMMQIVPQDPA 100
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfyNNQAITDDNFEKL-RKhigivfqnpdNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 101 STLNPKMTALDAVERaaRVSvrgrrdARRAAIDLLDKvgidkqlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK13648 107 FGLENHAVPYDEMHR--RVS------EALKQVDMLER-------ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2791281350 181 ALDYQAATKVMSVLQELNSE-GMGIVLVSHD-DELLQS 216
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEhNITIISITHDlSEAMEA 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-209 |
2.37e-18 |
|
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: 83.23 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTwpRKNRLMMQIVPQDPA---STL--NPK 106
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL--ASLRRQVALVSQDVVlfnDTIanNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 107 MTALDAVERAaRVSVRGRRDARRAAIDLLDKvGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:TIGR02203 428 YGRTEQADRA-EIERALAAAYAQDFVDKLPL-GLDTPIGE-NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180
....*....|....*....|...
gi 2791281350 187 ATKVMSVLQELNSEGMGIVlVSH 209
Cdd:TIGR02203 505 ERLVQAALERLMQGRTTLV-IAH 526
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-209 |
6.33e-18 |
|
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: 78.61 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIVPQDPastlnpkmTALD 111
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--DISTIPLEDLRSSLTIIPQDP--------TLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 AVERAarvsvrgrrdarraAIDLLDKVGiDKQL--AQRKPSG---LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:cd03369 96 GTIRS--------------NLDPFDEYS-DEEIygALRVSEGglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180
....*....|....*....|...
gi 2791281350 187 ATKVMSVLQELNSeGMGIVLVSH 209
Cdd:cd03369 161 DALIQKTIREEFT-NSTILTIAH 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-215 |
8.38e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPrKNRLMM 92
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ-GIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPAS-----------TLNPKMTALDAVERAARVSVRgrrdarraaidlLDKVGIDKqLAQRKPSGLSGGQRQRVA 161
Cdd:PRK13644 80 GIVFQNPETqfvgrtveedlAFGPENLCLPPIEIRKRVDRA------------LAEIGLEK-YRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 162 IARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQ 215
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH 200
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-191 |
9.88e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCV-----NNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTR--EAKRTw 84
Cdd:COG1101 2 LELKNLSKTfnpgtVNEK-RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdVTKlpEYKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 prknrLMMQIVPQDPASTLNPKMT-----ALdAVERAARVSVRGRRDARRAAI--DLLDKV--GIDKQLAQrkPSG-LSG 154
Cdd:COG1101 80 -----KYIGRVFQDPMMGTAPSMTieenlAL-AYRRGKRRGLRRGLTKKRRELfrELLATLglGLENRLDT--KVGlLSG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2791281350 155 GQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVM 191
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVL 188
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-218 |
1.23e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKrtwPRKNRLMMQIVPQdpASTLNPKMTALD 111
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR---ARLARARIGVVPQ--FDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 112 AVERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVM 191
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180
....*....|....*....|....*..
gi 2791281350 192 SVLQELNSEGMGIVLVSHDDELLQSYC 218
Cdd:PRK13536 213 ERLRSLLARGKTILLTTHFMEEAERLC 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-210 |
1.46e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTreakrTWPRKNRLMMQI--V------------P 96
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRKEFARRIgvVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 97 QDpASTLNPKMTALDAVERAARVSvrgrrdarrAAIDLLDkvgIDKQLAQ--RKpsgLSGGQRQRVAIARALAVRPKLLL 174
Cdd:COG4586 114 ID-SFRLLKAIYRIPDAEYKKRLD---------ELVELLD---LGELLDTpvRQ---LSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHD 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-215 |
2.89e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV----TREAKRTWPRKNRLMMqiVPQDPAstLNPKMTA 109
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakISDAELREVRRKKIAM--VFQSFA--LMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDAVERAARVSVRGRRDARRAAIDLLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATK 189
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180
....*....|....*....|....*...
gi 2791281350 190 VMSVLQELNSEGM-GIVLVSHD-DELLQ 215
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDlDEAMR 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-216 |
4.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRL 90
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQ---------IVPQDPAstLNPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQRQRVA 161
Cdd:PRK13652 83 VFQnpddqifspTVEQDIA--FGPINLGLDEETVAHRVS------------SALHMLGLE-ELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 162 IARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQS 216
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPE 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-210 |
4.45e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN------HAEsGEIECAGVTREAKRTWPR 86
Cdd:PRK14243 10 VLRTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVE-GKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 KNRLMMQIVPQDP-------------ASTLNPKMTALDA-VERAARVSVrgrrdarraaidLLDKVGiDKQlaqrKPSG- 151
Cdd:PRK14243 88 EVRRRIGMVFQKPnpfpksiydniayGARINGYKGDMDElVERSLRQAA------------LWDEVK-DKL----KQSGl 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 152 -LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHD 210
Cdd:PRK14243 151 sLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHN 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-222 |
4.68e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIVPQDPASTL------- 103
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitITHKTKDKYIRPVRKRIGMVFQFPESQLfedtver 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 -------NPKMTALDAVERAarvsvrgrrdarraaIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PRK13646 106 eiifgpkNFKMNLDEVKNYA---------------HRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 177 EITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVI 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-222 |
4.72e-17 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 76.35 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVT----LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreakrtwprknr 89
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lMMQIVPQDP-------------ASTLNPKMtaLDAVERAArvsvrgrrdARRAAIDLLDKvGIDKQLAQRkpsG--LSG 154
Cdd:cd03250 67 -SIAYVSQEPwiqngtirenilfGKPFDEER--YEKVIKAC---------ALEPDLEILPD-GDLTEIGEK---GinLSG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 155 GQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVM-SVLQELNSEGMGIVLVSHDDELLqSYCSTVI 222
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLL-PHADQIV 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-222 |
5.43e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQIVPQDP------AST- 102
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPdnqlfsASVy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 -------LNPKMTALDAVERAARVsvrgrrdarraaidlLDKVGIDkQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK13636 102 qdvsfgaVNLKLPEDEVRKRVDNA---------------LKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVF 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-209 |
6.29e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLS-----CVNNERVtlfqglSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPR 86
Cdd:COG3845 4 PALELRGITkrfggVVANDDV------SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--KPVRIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 87 K-NRL---MmqiVPQDPasTLNPKMTALD----AVERAARVsvrgrrdarraaidLLDKVGIDKQLAQ------------ 146
Cdd:COG3845 76 DaIALgigM---VHQHF--MLVPNLTVAEnivlGLEPTKGG--------------RLDRKAARARIRElserygldvdpd 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 147 RKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:COG3845 137 AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-183 |
1.11e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.58 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAkrtwPRKNRLMMqiVPQDPAstLNPKMT 108
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELE----PADRDIAM--VFQNYA--LYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALD------------------AVERAARVsvrgrrdarraaidlldkVGIDkQLAQRKPSGLSGGQRQRVAIARALaVR- 169
Cdd:PRK11650 93 VREnmayglkirgmpkaeieeRVAEAARI------------------LELE-PLLDRKPRELSGGQRQRVAMGRAI-VRe 152
|
170
....*....|....
gi 2791281350 170 PKLLLCDEITSALD 183
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-209 |
1.54e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRC---LIGLNHAE--SGEIECAGvtREAKRTWPRKNRLMMQIVPQDPAS 101
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDG--QDIFKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TlnPKMTALDAVERAARVS--VRGRRDARRAAIDLLDKVGIDKQLAQR--KPSG-LSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PRK14247 94 I--PNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLWDEVKDRldAPAGkLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 177 EITSALDYQAATKVMSVLQELNSEgMGIVLVSH 209
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
37-190 |
4.06e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreaKR---TWPRKNRLMMqiVPQDPAstLNPKMTALDAV 113
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-----KRmndVPPAERGVGM--VFQSYA--LYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 114 ERAARVSVRgrrdarraaidllDKVGIDK---------QLA---QRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:PRK11000 97 SFGLKLAGA-------------KKEEINQrvnqvaevlQLAhllDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
....*....
gi 2791281350 182 LDyqAATKV 190
Cdd:PRK11000 164 LD--AALRV 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-218 |
4.68e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREA--KRTWPRKNRLMMQIVPQDPASTLN- 104
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPAAEGMTVRe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 -------PKMTALDAVERAARVSVRgrrdarraaiDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDE 177
Cdd:PRK10575 105 lvaigryPWHGALGRFGAADREKVE----------EAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2791281350 178 ITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYC 218
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYC 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-209 |
5.97e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQDP----AS 101
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVpLVQYDHHYLHRQ---VALVGQEPvlfsGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDkvGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGE-KGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*....
gi 2791281350 182 LDYQaatkVMSVLQELNS-EGMGIVLVSH 209
Cdd:TIGR00958 648 LDAE----CEQLLQESRSrASRTVLLIAH 672
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-209 |
5.98e-16 |
|
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: 73.05 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 22 VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEIECAGvtREAKRTWPRKNRLMMQivpQDp 99
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING--RPLDKNFQRSTGYVEQ---QD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 asTLNPKMTALDAVERAArvsvrgrrdarraaidlldkvgidkqlaqrKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:cd03232 89 --VHSPNLTVREALRFSA------------------------------LLRGLSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 180 SALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-210 |
7.96e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLsCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKStlLRCLIGLNHAESGEIECAG-VTREAKRTWPRKNR-L 90
Cdd:PRK10418 4 QIELRNI-ALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGrVLLDGKPVAPCALRgR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPASTLNPKMT-ALDAVERAARVSVRGRRDARraaIDLLDKVGID--KQLAQRKPSGLSGGQRQRVAIARALA 167
Cdd:PRK10418 80 KIATIMQNPRSAFNPLHTmHTHARETCLALGKPADDATL---TAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHD 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-217 |
1.02e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.27 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIG-LNHaeSGEIECAGVT-RE-AKRTWpRKnrlmmQIV-----PQDPASTL- 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPY--QGSLKINGIElRElDPESW-RK-----HLSwvgqnPQLPHGTLr 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 ------NPKMT--ALDAVERAARVSvrgrrdarrAAIDLLDKvGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK11174 441 dnvllgNPDASdeQLQQALENAWVS---------EFLPLLPQ-GLDTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2791281350 176 DEITSALDYQAATKVMSVLQElNSEGMGIVLVSHDDELLQSY 217
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW 550
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-215 |
1.59e-15 |
|
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: 74.84 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEI--------ECAGVTREAK-- 81
Cdd:TIGR03269 1 IEVKNLT-KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIiyhvalceKCGYVERPSKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 82 -------------------------RTWPRKNRLMMQivpqdPASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLD 136
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQ-----RTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 137 KVgidkQLAQRK---PSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQEL-NSEGMGIVLVSHDDE 212
Cdd:TIGR03269 155 MV----QLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPE 230
|
...
gi 2791281350 213 LLQ 215
Cdd:TIGR03269 231 VIE 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-214 |
5.24e-15 |
|
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: 70.63 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEIECAGvtreakrtwprknrlm 91
Cdd:cd03217 1 LEIKDLHVSVGGKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 mqivpQDpastlnpkMTALDAVERAAR--------------VSVrgrrdarraaIDLLDKVGIdkqlaqrkpsGLSGGQR 157
Cdd:cd03217 64 -----ED--------ITDLPPEERARLgiflafqyppeipgVKN----------ADFLRYVNE----------GFSGGEK 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:cd03217 111 KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLL 167
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-226 |
5.40e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRtwprKNr 89
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQpTRQALQ----KN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 90 lMMQIVPQDPASTLNPKMTALDAVE----------RAARVSVRGRRDARRAAIDLLDkvgidkqLAQRKPSGLSGGQRQR 159
Cdd:PRK15056 79 -LVAYVPQSEEVDWSFPVLVEDVVMmgryghmgwlRRAKKRDRQIVTAALARVDMVE-------FRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 160 VAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCS-TVIPIGT 226
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDyTVMVKGT 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-210 |
6.01e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 16 VSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREA-KRTWPRKNRLMMQI 94
Cdd:PRK11831 10 MRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDL-LDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:PRK11831 89 LFQSGA--LFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD 203
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
44-221 |
6.95e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 44 GVKGPSGSGKSTLLRCLIGLN------HAES---GEIECAGVTREAKRTWPRKNrlmMQIVPQDPASTLNPKMTALDAVE 114
Cdd:COG4170 37 GLVGESGSGKSLIAKAICGITkdnwhvTADRfrwNGIDLLKLSPRERRKIIGRE---IAMIFQEPSSCLDPSAKIGDQLI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 115 ------------------RAARVsvrgrrdarraaIDLLDKVGI--DKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLL 174
Cdd:COG4170 114 eaipswtfkgkwwqrfkwRKKRA------------IELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHDDELLQSYCSTV 221
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTI 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-214 |
1.34e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.81 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLMMQIVPQDPASTLNpkMT 108
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIF--YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALDA----VERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQrkpsGLSGGQRQRVAIARALAVRPKLLLCDEITSALDY 184
Cdd:PRK13638 94 DIDSdiafSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQ----CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 185 QAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-218 |
2.55e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKnrlmmQIVPQDPASTLNPKMT 108
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK-----QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALDAVERAARVSVRGRRDARRAAIDLLDKVgIDKqlaqrkPSGL-SGGQRQRVAIARALAVRPKLLLCDEITSALDYQAA 187
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSLEHL-IDY------PCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2791281350 188 TKVMSVLQELNSEGMGIVLVSHDDELL-----QSYC 218
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHQDLPLnkadyEEYH 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
33-197 |
3.86e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKN--------RLMMQIVPQDPASTL 103
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlRDYTLASLRNQvalvsqnvHLFNDTIANNIAYAR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDaVERAARVSvrgrrdarrAAIDLLDKV--GIDKQLAQRKPSgLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:PRK11176 442 TEQYSREQ-IEEAARMA---------YAMDFINKMdnGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170
....*....|....*.
gi 2791281350 182 LDYQAATKVMSVLQEL 197
Cdd:PRK11176 511 LDTESERAIQAALDEL 526
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
47-215 |
4.89e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 47 GPSGSGKSTLLRCLIGLNHAESGEIECAGVT--REAKRTW--PRKNRlmMQIVPQDpaSTLNPKMTaldaVERAARVSVR 122
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfDAEKGIClpPEKRR--IGYVFQD--ARLFPHYK----VRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 123 GRRDARRAAI-DLLdkvGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE- 200
Cdd:PRK11144 103 KSMVAQFDKIvALL---GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREi 178
|
170
....*....|....*.
gi 2791281350 201 GMGIVLVSHD-DELLQ 215
Cdd:PRK11144 179 NIPILYVSHSlDEILR 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-209 |
5.36e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 30 FQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAkrtWPRKN-RLMMQIVPQDP---ASTL-- 103
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD---YSEAAlRQAISVVSQRVhlfSATLrd 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDAVERAarvsvrgrrdarraAIDLLDKVGIDKQLAQRKP------SG---LSGGQRQRVAIARALAVRPKLLL 174
Cdd:PRK11160 433 NLLLAAPNASDEA--------------LIEVLQQVGLEKLLEDDKGlnawlgEGgrqLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190
....*....|....*....|....*....|....*
gi 2791281350 175 CDEITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEH-AQNKTVLMITH 532
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
8.04e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.70 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 2 PGAGAGAGASPVLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAK 81
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 82 RTWPRKNRLmmQIVPQDP---ASTL--NPKMTALDAVERAARvsvrgrrdarraaiDLLDKVGIdKQLAQRKPSGL---- 152
Cdd:TIGR02868 403 DQDEVRRRV--SVCAQDAhlfDTTVreNLRLARPDATDEELW--------------AALERVGL-ADWLRALPDGLdtvl 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 153 -------SGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHD 210
Cdd:TIGR02868 466 geggarlSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-209 |
8.81e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTwprKNRLM--MQIVPQDpaSTLNPKMT 108
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAALAagVAIIYQE--LHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALDAV---ERAARVSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ 185
Cdd:PRK11288 96 VAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDID-PDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180
....*....|....*....|....
gi 2791281350 186 AATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSH 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-224 |
9.50e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN-HAE-SGEIECAGVTREAK--RTWPRKNrlmMQIVPQDpaST 102
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYpHGTwDGEIYWSGSPLKASniRDTERAG---IVIIHQE--LT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALDAVERAARVSVRGRRDARRAAI----DLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:TIGR02633 89 LVPELSVAENIFLGNEITLPGGRMAYNAMYlrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2791281350 179 TSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPI 224
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-210 |
9.74e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAvqRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEiecagvtreakrTWPRKNrLMMQIVPQDPAstLNPKMTALDA 112
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------------ARPQPG-IKVGYLPQEPQ--LDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARVSVRGRR-----------------------DARRAAIDLLDKVGIDKQL-----AQRKPSG------LSGGQRQ 158
Cdd:TIGR03719 89 VEEGVAEIKDALDrfneisakyaepdadfdklaaeqAELQEIIDAADAWDLDSQLeiamdALRCPPWdadvtkLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDyqaATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-209 |
9.99e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 67.88 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKnrlmMQIVPQDP---ASTLNP 105
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpISQYEHKYLHSK----VSLVGQEPvlfARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAVERAARVSVRGRRDARRAAIDLLDKvGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ 185
Cdd:cd03248 107 NIAYGLQSCSFECVKEAAQKAHAHSFISELAS-GYDTEVGE-KGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|....
gi 2791281350 186 AATKVMSVLQELNsEGMGIVLVSH 209
Cdd:cd03248 185 SEQQVQQALYDWP-ERRTVLVIAH 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-218 |
1.16e-13 |
|
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: 69.45 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLS----CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIeCAGVTRE----AKRT 83
Cdd:TIGR03269 278 PIIKVRNVSkryiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-NVRVGDEwvdmTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 84 WPRKNRL--MMQIVPQDpaSTLNPKMTALDAVERAARVSVRGRRDARRAAIdLLDKVGIDKQLAQ----RKPSGLSGGQR 157
Cdd:TIGR03269 357 PDGRGRAkrYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVI-TLKMVGFDEEKAEeildKYPDELSEGER 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALD----YQAATKVMSVLQELNSEgmgIVLVSHDDELLQSYC 218
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQT---FIIVSHDMDFVLDVC 495
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-197 |
2.42e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.45 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQDP----------- 99
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdIRTVTRASLRRN---IAVVFQDAglfnrsiedni 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ----ASTLNPKMtaLDAVERAArvsvrgrrdarraAIDLLDK--VGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:PRK13657 430 rvgrPDATDEEM--RAAAERAQ-------------AHDFIERkpDGYDTVVGERG-RQLSGGERQRLAIARALLKDPPIL 493
|
170 180
....*....|....*....|....
gi 2791281350 174 LCDEITSALDYQAATKVMSVLQEL 197
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDEL 517
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-210 |
3.44e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN-----HAESGEIECAGVTREAKR---TWPRKNRLMMQIVPQDP 99
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIFNYRdvlEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVgidKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAV---KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 180 SALDYQAATKVMSVLQELnSEGMGIVLVSHD 210
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSL-ADRLTVIIVTHN 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-210 |
3.56e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERvTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcagVTREAKRTWPRKNRLMM 92
Cdd:PRK10895 3 TLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QI--VPQDPA-----STLNPKMTALD------AVERAARVSvrgrrdarraaiDLLDKVGIDkQLAQRKPSGLSGGQRQR 159
Cdd:PRK10895 79 GIgyLPQEASifrrlSVYDNLMAVLQirddlsAEQREDRAN------------ELMEEFHIE-HLRDSMGQSLSGGERRR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 160 VAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-226 |
4.17e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEC------AGVTR--EAKRTwpRKN----------RLMMQIV 95
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKikEVKRL--RKEiglvfqfpeyQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 96 PQDPAstLNPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK13645 109 EKDIA--FGPVNLGENKQEAYKKVP------------ELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 176 DEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD--------DELLQSYCSTVIPIGT 226
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNmdqvlriaDEVIVMHEGKVISIGS 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-210 |
4.91e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcagvtreakrtwpRKNRL 90
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------------RNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQ----DPASTLNPK--MTALDAVERAARVSVrgrrdarraaidlLDKVGIdKQLAQRKPSGLSGGQRQRVAIAR 164
Cdd:PRK09544 68 RIGYVPQklylDTTLPLTVNrfLRLRPGTKKEDILPA-------------LKRVQA-GHLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-208 |
5.10e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSC--VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNH-AESGEIECAGvtREAKRTWPRKN- 88
Cdd:PRK13549 259 ILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG--KPVKIRNPQQAi 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 RLMMQIVPQD-------PASTLNPKMTaLDAVERAARVSVrgrrdarraaIDLLDKVG-IDKQLAQRK---PS------G 151
Cdd:PRK13549 337 AQGIAMVPEDrkrdgivPVMGVGKNIT-LAALDRFTGGSR----------IDDAAELKtILESIQRLKvktASpelaiaR 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 152 LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVS 208
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVIS 462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-210 |
5.56e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSC--VNNervtlfqgLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTreakrtwprknrlm 91
Cdd:PRK10762 258 LKVDNLSGpgVND--------VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE-------------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 mqIVPQDPASTL------------------------NPKMTALDAVERAA-RVSVRGRRDARRAAIDLLDKvgidKQLAQ 146
Cdd:PRK10762 316 --VVTRSPQDGLangivyisedrkrdglvlgmsvkeNMSLTALRYFSRAGgSLKHADEQQAVSDFIRLFNI----KTPSM 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 147 RKPSG-LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK10762 390 EQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-210 |
7.17e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.87 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 15 RVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKnrlmM 92
Cdd:COG4604 3 EIKNVSKRYGGKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldVATTPSRELAKR----L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPASTLN------------P----KMTALD--AVERAarvsvrgrrdarraaIDLLDKVGI-DKQLAQrkpsgLS 153
Cdd:COG4604 78 AILRQENHINSRltvrelvafgrfPyskgRLTAEDreIIDEA---------------IAYLDLEDLaDRYLDE-----LS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 154 GGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHD 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-210 |
9.53e-13 |
|
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: 66.88 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIE--------CAGVTREAKRtw 84
Cdd:TIGR03719 322 VIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigetvklaYVDQSRDALD-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 PRKNrlmmqiVPQDPASTLNpkMTALDAVERAARVSVRGrrdarraaidlLDKVGIDKqlaQRKPSGLSGGQRQRVAIAR 164
Cdd:TIGR03719 399 PNKT------VWEEISGGLD--IIKLGKREIPSRAYVGR-----------FNFKGSDQ---QKKVGQLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2791281350 165 ALAVRPKLLLCDEITSALDyqaaTKVMSVLQE--LNSEGMGIVlVSHD 210
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD----VETLRALEEalLNFAGCAVV-ISHD 499
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-210 |
1.15e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG--VTREAKRTWPRKNRLMMQIV---------- 95
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVARRIGLLAQNAttpgditvqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 96 -------PQDPASTLNPKMTAlDAVERAARVSvrgrrdarraaidlldkvGIdKQLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:PRK10253 101 lvargryPHQPLFTRWRKEDE-EAVTKAMQAT------------------GI-THLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHD 210
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHD 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-209 |
1.21e-12 |
|
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: 63.87 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLS-CVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKnrlMM 92
Cdd:cd03247 1 LSINNVSfSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSS---LI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDP---ASTlnpkmtaldaveraarvsvrgrrdarraaidLLDKVGIDkqlaqrkpsgLSGGQRQRVAIARALAVR 169
Cdd:cd03247 78 SVLNQRPylfDTT-------------------------------LRNNLGRR----------FSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITH 155
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-210 |
1.33e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVtLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcAGVTreakrtwprknrlmM 92
Cdd:PRK11819 324 VIEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGET--------------V 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QI--VPQDPAStLNPKMTALDAVEraarvsvrgrrdarraaiDLLD--KVGiDKQLA--------------QRKPSG-LS 153
Cdd:PRK11819 388 KLayVDQSRDA-LDPNKTVWEEIS------------------GGLDiiKVG-NREIPsrayvgrfnfkggdQQKKVGvLS 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 154 GGQRQRVAIARALAVRPKLLLCDEITSALDyqaaTKVMSVLQE--LNSEGMGIVlVSHD 210
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEalLEFPGCAVV-ISHD 501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-208 |
1.41e-12 |
|
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: 66.39 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSC--VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE-SGEI----------ECAGVTRE 79
Cdd:TIGR02633 257 ILEARNLTCwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVfingkpvdirNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 80 AKRTWPrKNRLMMQIVPqDPASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQrkpSGLSGGQRQR 159
Cdd:TIGR02633 337 GIAMVP-EDRKRHGIVP-ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI---GRLSGGNQQK 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2791281350 160 VAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVS 208
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-210 |
1.59e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNhAESGEIECAGvtrEAKRTWP------RKNRLMMQIVPqdPAS----- 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG---QPLEAWSaaelarHRAYLSQQQTP--PFAmpvfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 --TLN-PKMTALDAVERAARvsvrgrrdarraaiDLLDKVGIDKQLAqRKPSGLSGGQRQRVAIARA-LAVRP------K 171
Cdd:PRK03695 89 ylTLHqPDKTRTEAVASALN--------------EVAEALGLDDKLG-RSVNQLSGGEWQRVRLAAVvLQVWPdinpagQ 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-209 |
3.00e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN-HAE-SGEIECAGVTREAK--RTWPRKNrlmMQIVPQDpaST 102
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYpHGTyEGEIIFEGEELQASniRDTERAG---IAIIHQE--LA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 LNPKMTALDAV---ERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:PRK13549 93 LVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT-PVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 180 SALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-209 |
5.47e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAES--GEIecagVTREAKRTWPRKNRlmMQIVPQDpaSTLNP 105
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTI----LANNRKPTKQILKR--TGFVTQD--DILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAVERAARVSVRGRRDARRAAI---DLLDKVGIDK----QLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSLTKQEKILvaeSVISELGLTKcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 179 TSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-210 |
6.24e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 26 RVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI----------ECAGVTREAKRTWPRKNRLMMQIV 95
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditdwQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 96 PQDpastlNPKMTALDA-----VERAARVsvrgrrdarraaIDLLDKvgIDKQLAQRKPSgLSGGQRQRVAIARALAVRP 170
Cdd:PRK11614 97 VEE-----NLAMGGFFAerdqfQERIKWV------------YELFPR--LHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-210 |
8.30e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAEsGEIECAGvtrEAKRTWP------RKNRLMMQivpQDPASTL- 103
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNG---RPLSDWSaaelarHRAYLSQQ---QSPPFAMp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 --------NPKMTALDAVERAARvsvrgrrdarraaiDLLDKVGIDKQLAqRKPSGLSGGQRQRVAIARA-LAVRP---- 170
Cdd:COG4138 86 vfqylalhQPAGASSEAVEQLLA--------------QLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVlLQVWPtinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2791281350 171 --KLLLCDEITSALD--YQAATKvmSVLQELNSEGMGIVLVSHD 210
Cdd:COG4138 151 egQLLLLDEPMNSLDvaQQAALD--RLLRELCQQGITVVMSSHD 192
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-225 |
8.76e-12 |
|
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: 61.57 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNnervtlFQGLSFAVQRGTMVGVKGPSGSGKSTLlrCLIGLnhAESGEIECAGVTREAKRTwprknrlmmq 93
Cdd:cd03238 1 LTVSGANVHN------LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL--YASGKARLISFLPKFSRN---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 ivpqdpastlnpKMTALDAVERaarvsvrgrrdarraaidlLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPK-- 171
Cdd:cd03238 61 ------------KLIFIDQLQF-------------------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgt 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 172 LLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQsYCSTVIPIG 225
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLS-SADWIIDFG 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-222 |
8.88e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNERVtlfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLM 91
Cdd:PRK09700 264 TVFEVRNVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIVPQDPASTLNPKMTaldaVERAARVSVRGRRDARRAAIDLLDKVgIDKQLA--QRKP------------SGLSGGQR 157
Cdd:PRK09700 341 AYITESRRDNGFFPNFS----IAQNMAISRSLKDGGYKGAMGLFHEV-DEQRTAenQRELlalkchsvnqniTELSGGNQ 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 158 QRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-209 |
1.33e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.61 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLnhaesgeiecaGVTREAKRTWPRKNRLMM 92
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-----------WPVYGGRLTKPAKGKLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 qiVPQDPASTLNP-------KMTALDAVERAARVSVRGRRDARRAAIDLLDK-VGIDkqLAQRKPSGLSGGQRQRVAIAR 164
Cdd:TIGR00954 520 --VPQRPYMTLGTlrdqiiyPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReGGWS--AVQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 165 ALAVRPKLLLCDEITSALDYQAATKVMSVLQElnsegMGIVL--VSH 209
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCRE-----FGITLfsVSH 637
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-209 |
2.60e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNRLmmQIVPQDP-------ASTL 103
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL--AVVSQTPflfsdtvANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 ---NPKMTALDaVERAARV-SVRGrrdarraaiDLLD-KVGIDKQLAQRkpsG--LSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PRK10789 410 algRPDATQQE-IEHVARLaSVHD---------DILRlPQGYDTEVGER---GvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190
....*....|....*....|....*....|...
gi 2791281350 177 EITSALDYQAATKVMSVLQELnSEGMGIVLVSH 209
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-215 |
3.14e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNnervtlFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTwprKNRLM 91
Cdd:PRK15439 267 PVLTVEDLTGEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 92 MQIV--PQD-PASTLNpkmtaLDAVERAARVSVRGRRD----ARRAAIDLLDK----VGIDKQLAQRKPSGLSGGQRQRV 160
Cdd:PRK15439 338 RGLVylPEDrQSSGLY-----LDAPLAWNVCALTHNRRgfwiKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKV 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 161 AIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQ 468
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-213 |
3.17e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLS-------CVNnervtlfqGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtrEAKRTW 84
Cdd:PRK11300 4 PLLSVSGLMmrfggllAVN--------NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG---QHIEGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 PRKNRLMMQIVPQDPASTLNPKMTAL------------------------------DAVERAARvsvrgrrdarraaidL 134
Cdd:PRK11300 73 PGHQIARMGVVRTFQHVRLFREMTVIenllvaqhqqlktglfsgllktpafrraesEALDRAAT---------------W 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 135 LDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDEL 213
Cdd:PRK11300 138 LERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKL 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-221 |
5.02e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLN---------HAESGEIECAGVTREAKRTWPRKNrlmMQIVPQDPASTL 103
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvtadRMRFDDIDLLRLSPRERRKLVGHN---VSMIFQEPQSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKmtaldavERAARVSVRGRRD-------------ARRAAIDLLDKVGID--KQLAQRKPSGLSGGQRQRVAIARALAV 168
Cdd:PRK15093 103 DPS-------ERVGRQLMQNIPGwtykgrwwqrfgwRKRRAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2791281350 169 RPKLLLCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSHDDELLQSYCSTV 221
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-197 |
6.07e-11 |
|
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: 59.58 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCL---IGLNHAESGEIECAGVT-REAKRTWPRknrlmmQI--VPQDPAS 101
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPyKEFAEKYPG------EIiyVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 tlNPKMTALDAVERAARVsvrgrrdarraaidlldkvgidkqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:cd03233 95 --FPTLTVRETLDFALRC------------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|....*.
gi 2791281350 182 LDYQAATKVMSVLQEL 197
Cdd:cd03233 149 LDSSTALEILKCIRTM 164
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-196 |
8.40e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtrEAKRTWPRKNRLMMQIVPQDPA-------S 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--DVAKFGLTDLRRVLSIIPQSPVlfsgtvrF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TLNPKMTALDA-----VERAARVSVRGRrdarraaidllDKVGIDKQLAQRKPSgLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PLN03232 1329 NIDPFSEHNDAdlweaLERAHIKDVIDR-----------NPFGLDAEVSEGGEN-FSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180
....*....|....*....|
gi 2791281350 177 EITSALDYQAATKVMSVLQE 196
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIRE 1416
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-195 |
9.53e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTreAKRTWPRKNRLMMQIVPQDPASTLNPKMTALDA 112
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN--IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARVSVRGRRDARraaiDLLDKV-----GIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAA 187
Cdd:TIGR00957 1383 FSQYSDEEVWWALELA----HLKTFVsalpdKLDHECAE-GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
....*...
gi 2791281350 188 TKVMSVLQ 195
Cdd:TIGR00957 1458 NLIQSTIR 1465
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-183 |
1.35e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 40 GTMVGVKGPSGSGKSTLLRCLIGLNHAESGEiecagvtreakrTWPRKNrLMMQIVPQDPAstLNPKMTALDAVERAAR- 118
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE------------ARPAPG-IKVGYLPQEPQ--LDPEKTVRENVEEGVAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 ----------VSVRGRRDARRA------------AIDLLDKVGIDKQL-----AQRKPSG------LSGGQRQRVAIARA 165
Cdd:PRK11819 98 vkaaldrfneIYAAYAEPDADFdalaaeqgelqeIIDAADAWDLDSQLeiamdALRCPPWdakvtkLSGGERRRVALCRL 177
|
170
....*....|....*...
gi 2791281350 166 LAVRPKLLLCDEITSALD 183
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLD 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-229 |
1.58e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQR------GTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWpRKNRL---MMQIVPQDPASTLN 104
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEF-RGSELqnyFTKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMtaLDAVERAARVSVrgrrdarraaIDLLDKVG--------ID----KQLAQRKPSGLSGGQRQRVAIARALAVRPKL 172
Cdd:cd03236 93 PQY--VDLIPKAVKGKV----------GELLKKKDergkldelVDqlelRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 173 LLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLqSYCSTVIPI--GTAAV 229
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVL-DYLSDYIHClyGEPGA 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-214 |
1.68e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIG---LNHAESGEIECAGVTREAkrTWPRKNRLMMQivpQD---PASTLNPKMTAL 110
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDS--SFQRSIGYVQQ---QDlhlPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLL-CDEITSALDYQAATK 189
Cdd:TIGR00956 861 AYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
170 180 190
....*....|....*....|....*....|....
gi 2791281350 190 VMSVLQELNSEGMGIVLVSHD---------DELL 214
Cdd:TIGR00956 941 ICKLMRKLADHGQAILCTIHQpsailfeefDRLL 974
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-210 |
1.73e-10 |
|
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: 58.96 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 39 RGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKrtwprknrlmmqivPQdpasTLNPKMTAldAVERAAR 118
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK--------------PQ----YIKADYEG--TVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 VSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSgLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ---AATKVMSVLQ 195
Cdd:cd03237 84 SITKDFYTHPYFKTEIAKPLQIEQILDREVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASKVIRRFA 162
|
170
....*....|....*
gi 2791281350 196 ELNSEGMgiVLVSHD 210
Cdd:cd03237 163 ENNEKTA--FVVEHD 175
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-214 |
1.81e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEiecagVTREAKrtwprknrLMMQIVPQDPASTLNPKM 107
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT-----VFRSAK--------VRMAVFSQHHVDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TAL--------DAVERAARVSvrgrrdarraaidlLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:PLN03073 590 NPLlymmrcfpGVPEQKLRAH--------------LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190
....*....|....*....|....*....|....*
gi 2791281350 180 SALDYQAatkVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:PLN03073 656 NHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLI 687
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-209 |
2.81e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVtREAKRTWPRKNRLMMQIVPQDPasTLNPK 106
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-PCARLTPAKAHQLGIYLVPQEP--LLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 107 MTALDAVeraaRVSVRGRRDARRAAIDLLDKVGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:PRK15439 101 LSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDS-SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180
....*....|....*....|...
gi 2791281350 187 ATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISH 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-209 |
8.11e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.96 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 17 SNLSCVNNervtlfqgLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV--TREAKRTWPRKNRLMMQI 94
Cdd:cd03290 12 SGLATLSN--------INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 95 VPQDP---ASTLNPKMTaLDAVERAARVSVRGRRDARRAAIDLLdKVGIDKQLAQRKPSgLSGGQRQRVAIARALAVRPK 171
Cdd:cd03290 84 AAQKPwllNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLL-PFGDQTEIGERGIN-LSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2791281350 172 LLLCDEITSALDYQAATKVMS--VLQELNSEGMGIVLVSH 209
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-209 |
1.17e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLM-MQIVPQDpastLN--PKMT 108
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG--KEVTFNGPKSSQEAgIGIIHQE----LNliPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 AldaverAARVSVRGRRDARRAAID----------LLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:PRK10762 96 I------AENIFLGREFVNRFGRIDwkkmyaeadkLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190
....*....|....*....|....*....|.
gi 2791281350 179 TSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PRK10762 169 TDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-224 |
1.18e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcagvtreakrtWPRKNRLmmQIVPQDPASTLNPKM 107
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----------WSENANI--GYYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDaveraarvsvrgrrdarraAIDLLDKVGIDKQL--------------AQRKPSGLSGGQRQRVAIARALAVRPKLL 173
Cdd:PRK15064 400 TLFD-------------------WMSQWRQEGDDEQAvrgtlgrllfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 174 LCDEITSALDyqaatkvMSVLQELNS-----EGMgIVLVSHDDELLQSYCSTVIPI 224
Cdd:PRK15064 461 VMDEPTNHMD-------MESIESLNMalekyEGT-LIFVSHDREFVSSLATRIIEI 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-226 |
1.40e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREaKRTWPRKNRLMMQIVPQ-----DPAS 101
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-KLDHKLAAQLGIGIIYQelsviDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 102 TLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLaQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSA 181
Cdd:PRK09700 97 VLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2791281350 182 LDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSYCS--TVIPIGT 226
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDryTVMKDGS 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-209 |
1.61e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNErVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-VTREAKRTwprknrL 90
Cdd:PRK13543 10 PLLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGkTATRGDRS------R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPAstLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRkpsgLSGGQRQRVAIARALAVRP 170
Cdd:PRK13543 83 FMAYLGHLPG--LKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 171 KLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-209 |
6.53e-09 |
|
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: 55.72 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-VTREAKRTWPRKNRLMMQIVPQDPastLNPKMTAl 110
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsVAYVPQQAWIQNDSLRENILFGKA---LNEKYYQ- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 111 DAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKV 190
Cdd:TIGR00957 732 QVLEACALLP------------DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180
....*....|....*....|...
gi 2791281350 191 MSvlQELNSEGM----GIVLVSH 209
Cdd:TIGR00957 800 FE--HVIGPEGVlknkTRILVTH 820
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-192 |
7.28e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 31 QGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMQIVPQDP-------ASTL 103
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG--REIGAYGLRELRRQFSMIPQDPvlfdgtvRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDAVERAArvsvrgrrdarRAAIDLLDKV-----GIDKQLaQRKPSGLSGGQRQRVAIARALAVR-PKLLLCDE 177
Cdd:PTZ00243 1405 DPFLEASSAEVWAA-----------LELVGLRERVaseseGIDSRV-LEGGSNYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
170
....*....|....*....
gi 2791281350 178 ITS----ALDYQAATKVMS 192
Cdd:PTZ00243 1473 ATAnidpALDRQIQATVMS 1491
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-210 |
9.20e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAgvtreakrtwprkNRLMMQIVPQDPAsTLNPKM 107
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------------TKLEVAYFDQHRA-ELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAV-ERAARVSVRgrrdarraaidlldkvGIDKQL-------------AQRKPSGLSGGQRQRVAIARaLAVRP-KL 172
Cdd:PRK11147 399 TVMDNLaEGKQEVMVN----------------GRPRHVlgylqdflfhpkrAMTPVKALSGGERNRLLLAR-LFLKPsNL 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 173 LLCDEITSALDYQAatkvMSVLQELNSEGMGIVL-VSHD 210
Cdd:PRK11147 462 LILDEPTNDLDVET----LELLEELLDSYQGTVLlVSHD 496
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
40-224 |
9.62e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 40 GTMVGVKGPSGSGKSTLLRCLIGLNHAESGEI------ECAGVTRE--------------AKRTWpRKNRLMMQIVPQ-- 97
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwQLAWVNQEtpalpqpaleyvidGDREY-RQLEAQLHDANErn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 98 --DPASTLNPKMTALDAVERAARVSvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLC 175
Cdd:PRK10636 106 dgHAIATIHGKLDAIDAWTIRSRAA------------SLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2791281350 176 DEITSALDYQAatkVMSVLQELNSEGMGIVLVSHDDELLQSYCSTVIPI 224
Cdd:PRK10636 174 DEPTNHLDLDA---VIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-210 |
1.22e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 36 AVQRGTMVGVKGPSGSGKSTLLRCLIGL------NHAESGEIEcaGVTREAKRTW-------PRKNRLMMQIVPQdpast 102
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgDYEEEPSWD--EVLKRFRGTElqnyfkkLYNGEIKVVHKPQ----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 lnpkmtaldAVERAARV---SVrgrrdarraaIDLLDKV---GIDKQLAQ---------RKPSGLSGGQRQRVAIARALA 167
Cdd:PRK13409 168 ---------YVDLIPKVfkgKV----------RELLKKVderGKLDEVVErlglenildRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2791281350 168 VRPKLLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHD 210
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHD 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-183 |
1.36e-08 |
|
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: 54.53 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAEsGEIECAGVTREAK--RTWprknRLMMQIVPQDPASTLNP 105
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVtlQTW----RKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAVERAARVSVRGrrdarraaidLLDKVGIdKQLAQRKPSG-----------LSGGQRQRVAIARALAVRPKLLL 174
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEIWK----------VAEEVGL-KSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILL 1376
|
....*....
gi 2791281350 175 CDEITSALD 183
Cdd:TIGR01271 1377 LDEPSAHLD 1385
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
133-210 |
1.55e-08 |
|
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: 54.41 E-value: 1.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 133 DLLDKVGIDKQLaQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:COG1245 195 ELAEKLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-216 |
1.58e-08 |
|
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: 51.99 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 39 RGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcagvtreakrtwprknrlmmqivpqdpasTLNPKMTALDAVERAAR 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------------YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 VSVRgrrdarraaidlldkvgidkqlaqRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALD------YQAATKVMS 192
Cdd:smart00382 52 IIVG------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqealLLLLEELRL 107
|
170 180
....*....|....*....|....
gi 2791281350 193 VLQELNSEGMGIVLVSHDDELLQS 216
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-183 |
2.07e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.07e-08
10 20 30
....*....|....*....|....*....|..
gi 2791281350 152 LSGGQRQRVAIARALAVRPKLLLCDEITSALD 183
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-214 |
2.29e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNL-SCVNNerVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIG-----------------LNHAESGE-- 70
Cdd:CHL00131 5 KPILEIKNLhASVNE--NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesILDLEPEEra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 71 -----------IECAGVTREA-KRTWPRKNRLMMQIVPQDPAS---TLNPKmtaldaveraarvsvrgrrdarraaidlL 135
Cdd:CHL00131 83 hlgiflafqypIEIPGVSNADfLRLAYNSKRKFQGLPELDPLEfleIINEK----------------------------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 136 DKVGIDKQLAQRKPS-GLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:CHL00131 135 KLVGMDPSFLSRNVNeGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-183 |
2.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 32 GLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGV-TREAKRTWPRKNrlmMQIVPQDPA-------STL 103
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCdISKFGLMDLRKV---LGIIPQAPVlfsgtvrFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 104 NPKMTALDA-----VERAARVSVRGRrdarraaidllDKVGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:PLN03130 1334 DPFNEHNDAdlwesLERAHLKDVIRR-----------NSLGLDAEVSE-AGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
....*
gi 2791281350 179 TSALD 183
Cdd:PLN03130 1402 TAAVD 1406
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
33-222 |
2.35e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtreakrtwprkNRLMMQIvpqdpASTLNPKMTALDA 112
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAI-----SSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQRKPSgLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMS 192
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKT-YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 193 VLQELNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-219 |
2.76e-08 |
|
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: 53.86 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTWPRKNrlmMQIVPQDPAstLNPKMTALDA 112
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQN---MGYCPQFDA--IDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARVSVRGRRDARRAAIDLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMS 192
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180
....*....|....*....|....*..
gi 2791281350 193 VLQELNSEGMGIVLVSHDDELLQSYCS 219
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHSMEECEALCT 2138
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-210 |
2.82e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRtwPRKN-RLMMQIVPQDPASTlnpKMTALDA 112
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS--PRDAiRAGIMLCPEDRKAE---GIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARVSVRGRRDARRAAIDllDKVGID------KQLAQRKPSG------LSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:PRK11288 348 VADNINISARRHHLRAGCLIN--NRWEAEnadrfiRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 181 ALDYQAATKVMSVLQELNSEGMGIVLVSHD 210
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-209 |
4.50e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 150 SGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELN-SEGMGIVLVSH 209
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAH 638
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-221 |
4.69e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGlNHAESGEIECAGVTRE--------AKRTW 84
Cdd:PRK13547 1 MLTADHLHVARRHRAIL-RDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPRGARVTGDvtlngeplAAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 PRKNRLmMQIVPQ--DPASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAI 162
Cdd:PRK13547 79 PRLARL-RAVLPQaaQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 163 ARALA---------VRPKLLLCDEITSALDYQAATKVMSVLQELNSE-GMGIVLVSHDDELLQSYCSTV 221
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRI 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-207 |
7.35e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 34 SFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECaGVTREAK-----------RTWPRKNRLMMQIVPQDPAST 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQS-QFSHITRlsfeqlqklvsDEWQRNNTDMLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 103 lnpkmTA---LDAVERAARVSvrgrrdarraaiDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEIT 179
Cdd:PRK10938 102 -----TAeiiQDEVKDPARCE------------QLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180
....*....|....*....|....*...
gi 2791281350 180 SALDYQAATKVMSVLQELNSEGMGIVLV 207
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
48-228 |
1.09e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 48 PSGSGKSTLLRCL-IGLnhaesGEIECAGvtreakrTWPRKNRLMMQIVPQDP----ASTLNPKMTALDAVERA--ARVS 120
Cdd:PRK00635 391 PKGTSATSCPRCQgTGL-----GDYANAA-------TWHGKTFAEFQQMSLQElfifLSQLPSKSLSIEEVLQGlkSRLS 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 121 VRgrrdarraaIDLldkvGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPK--LLLCDEITSALDYQAATKVMSVLQELN 198
Cdd:PRK00635 459 IL---------IDL----GLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLR 525
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 199 SEGMGIVLVSHDDELLqSYCSTVIPIGTAA 228
Cdd:PRK00635 526 DQGNTVLLVEHDEQMI-SLADRIIDIGPGA 554
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-215 |
1.24e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRTwprKNRLM--MQIVPQDpastLNP--KMTALDA 112
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSS---KEALEngISMVHQE----LNLvlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 V------ERAARVSVRGRRDARRAAIDLLDkVGIDkqlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQA 186
Cdd:PRK10982 94 MwlgrypTKGMFVDQDKMYRDTKAIFDELD-IDID---PRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 187 ATKVMSVLQELNSEGMGIVLVSHD-DELLQ 215
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKmEEIFQ 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-214 |
1.49e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 22 VNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEIECAGVTREaKRTWPRKNRLMMQIVPQDP 99
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKK-QETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 ASTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGI-DKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEI 178
Cdd:PLN03140 967 QVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLkDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2791281350 179 TSALDYQAATKVMSVLQELNSEGMGIVLVSHD---------DELL 214
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsidifeafDELL 1091
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-210 |
1.72e-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: 50.94 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcAGVTREAKrtwprknrlmmqivPQdpasTLNPKMTALdaVERA 116
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYK--------------PQ----YISPDYDGT--VEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 117 ARVSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ---AATKVMSV 193
Cdd:COG1245 422 LRSANTDDFGSSYYKTEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRR 500
|
170
....*....|....*..
gi 2791281350 194 LQElnSEGMGIVLVSHD 210
Cdd:COG1245 501 FAE--NRGKTAMVVDHD 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-216 |
1.86e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 11 SPVLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIecaGVTREAKRTWPRKNRL 90
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIIL-DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIKLGYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDP---ASTLNPKMTaldavERAARvsvrgrrdarraaiDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALA 167
Cdd:PRK10636 386 EFLRADESPlqhLARLAPQEL-----EQKLR--------------DYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 168 VRPKLLLCDEITSALDY---QAATKVMsvlqeLNSEGmGIVLVSHDDELLQS 216
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLdmrQALTEAL-----IDFEG-ALVVVSHDRHLLRS 492
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-210 |
2.78e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG---VTR-------------------------EA 80
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdliVARlqqdpprnvegtvydfvaegieeqaEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 81 KRTWPRKNRLMMQivpqDPASTLNPKMTALDAV-------ERAARVSvrgrrdarraaiDLLDKVGIDkqlAQRKPSGLS 153
Cdd:PRK11147 98 LKRYHDISHLVET----DPSEKNLNELAKLQEQldhhnlwQLENRIN------------EVLAQLGLD---PDAALSSLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 154 GGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSegmGIVLVSHD 210
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHD 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-214 |
3.46e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVtlfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTReakrtwprKNRLMM 92
Cdd:PRK10982 250 ILEVRNLTSLRQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI--------NNHNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 QIVPQDPA-STLNPKMTALDAVERAARVSVRGRRDARRAAIDLLD--KVGIDKQ-----LAQRKPS------GLSGGQRQ 158
Cdd:PRK10982 319 EAINHGFAlVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDnsRMKSDTQwvidsMRVKTPGhrtqigSLSGGNQQ 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 159 RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHD-DELL 214
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELL 455
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-191 |
3.53e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIecagvtreakrtWPRKNrlmMQIVPQDP---ASTLNP 105
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------------WAERS---IAYVPQQAwimNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 106 KMTALDAvERAARVSVRGRRDARRAAIDLLDKvGIDKQLAQrKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ 185
Cdd:PTZ00243 740 NILFFDE-EDAARLADAVRVSQLEADLAQLGG-GLETEIGE-KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
....*.
gi 2791281350 186 AATKVM 191
Cdd:PTZ00243 817 VGERVV 822
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-208 |
3.66e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 40 GTMVGVKGPSGSGKSTLLRCLIGLNH----AESGEIECAGVTREakrtwprknrlmmQIVPQDPASTLN--------PKM 107
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPE-------------EIKKHYRGDVVYnaetdvhfPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAVERAA-------RVSVRGRRDARRAAIDL------LD-----KVGIDKQlaqrkpSGLSGGQRQRVAIARALAVR 169
Cdd:TIGR00956 154 TVGETLDFAArcktpqnRPDGVSREEYAKHIADVymatygLShtrntKVGNDFV------RGVSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 2791281350 170 PKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVS 208
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-211 |
5.29e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKRtwPRKNRLMMQIVPQDP---ASTLNPKMTA 109
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLFSAVFTDFhlfDQLLGPEGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 110 LDaverAARVsvrgrrDARRAAIDLLDKVGI-DKQLAQRKpsgLSGGQRQRVAIARALAVRPKLLLCDEITSALD----- 183
Cdd:PRK10522 420 AN----PALV------EKWLERLKMAHKLELeDGRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDphfrr 486
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 184 --YQaatKVMSVLQELnseGMGIVLVSHDD 211
Cdd:PRK10522 487 efYQ---VLLPLLQEM---GKTIFAISHDD 510
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
14-213 |
8.55e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.03 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNLSCVNNERVTLFQGLSFAvqrgTMVGVKGPSGSGKSTLLRcliGLNHAESGEiecagVTREAKRTWPRKNRlmmq 93
Cdd:cd03279 6 LELKNFGPFREEQVIDFTGLDNN----GLFLICGPTGAGKSTILD---AITYALYGK-----TPRYGRQENLRSVF---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 94 ivpqdpastlnpkmtalDAVERAARVSVRGRRDARRAAIDllDKVGIDKQ-------LAQ--------RKPSGLSGGQRQ 158
Cdd:cd03279 70 -----------------APGEDTAEVSFTFQLGGKKYRVE--RSRGLDYDqftrivlLPQgefdrflaRPVSTLSGGETF 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 159 RVAIARALA----------VRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDEL 213
Cdd:cd03279 131 LASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEEL 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-209 |
9.84e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 27 VTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAES--GEIECAGVTREAKrTWPRKNRLMMQIVPQDPAstLN 104
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFK-DIRDSEALGIVIIHQELA--LI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 105 PKMTALDAV----ERAARvSVRGRRDARRAAIDLLDKVGIDKQlAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITS 180
Cdd:NF040905 91 PYLSIAENIflgnERAKR-GVIDWNETNRRARELLAKVGLDES-PDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180
....*....|....*....|....*....
gi 2791281350 181 ALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-222 |
2.42e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 143 QLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgmgIVLVSHDDELLQSYCSTVI 222
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKT---FIVVSHAREFLNTVVTDIL 412
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-210 |
2.67e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIEcAGVTREAKrtwprknrlmmqivPQ----DPASTlnpkmtalda 112
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PELKISYK--------------PQyikpDYDGT---------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 113 VERAARvSVRGRRDARRAAIDLLDKVGIDKqLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQ---AATK 189
Cdd:PRK13409 417 VEDLLR-SITDDLGSSYYKSEIIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAK 494
|
170 180
....*....|....*....|.
gi 2791281350 190 VMSVLQELNSEGMgIVlVSHD 210
Cdd:PRK13409 495 AIRRIAEEREATA-LV-VDHD 513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-209 |
4.43e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIG-LNHAESGEIECAGVtreakrtwprknrlmMQIVPQDP---ASTLNPKMT 108
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS---------------VAYVPQVSwifNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 ALDAVErAARVSVRGRRDARRAAIDLLdkVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAAT 188
Cdd:PLN03232 701 FGSDFE-SERYWRAIDVTALQHDLDLL--PGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180
....*....|....*....|.
gi 2791281350 189 KVMSVLQELNSEGMGIVLVSH 209
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTN 798
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-211 |
6.29e-06 |
|
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: 46.33 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 33 LSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVT-REAKRTWPRKN------------RLMMQIVPQDP 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvTADNREAYRQLfsavfsdfhlfdRLLGLDGEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 100 AstlnpKMTALdaVERaarvsvrgrrdarraaIDLLDKVGI-DKQLAQRKpsgLSGGQRQRVAIARALAV-RPKLLLcDE 177
Cdd:COG4615 431 A-----RAREL--LER----------------LELDHKVSVeDGRFSTTD---LSQGQRKRLALLVALLEdRPILVF-DE 483
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2791281350 178 ITSALD-------YQAatkvmsVLQELNSEGMGIVLVSHDD 211
Cdd:COG4615 484 WAADQDpefrrvfYTE------LLPELKARGKTVIAISHDD 518
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-216 |
9.29e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 9.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 150 SGLSGGQRQRVAIARALAVRPK---LLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQS 216
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ 1767
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-214 |
9.52e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLScVNNERVTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAE--SGEIECagvtreakrtwprKNRL 90
Cdd:PRK09580 1 MLSIKDLH-VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEF-------------KGKD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 MMQIVPQDPA-----------------STLNPKMTALDAVeRAAR----VSVRGRRDARRAAIDLLDkvgIDKQLAQRKP 149
Cdd:PRK09580 67 LLELSPEDRAgegifmafqypveipgvSNQFFLQTALNAV-RSYRgqepLDRFDFQDLMEEKIALLK---MPEDLLTRSV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 150 S-GLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:PRK09580 143 NvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRIL 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-183 |
1.01e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 13 VLRVSNLSCVNNERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG----VTREAKRTWPRkn 88
Cdd:NF033858 1 VARLEGVSHRYGKTVAL-DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmaDARHRRAVCPR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 89 rlmmqI--VPQDPASTLNPKMT------------ALDAVERAARVSvrgrrdarraaiDLLDKVGIDKqLAQRkPSG-LS 153
Cdd:NF033858 78 -----IayMPQGLGKNLYPTLSvfenldffgrlfGQDAAERRRRID------------ELLRATGLAP-FADR-PAGkLS 138
|
170 180 190
....*....|....*....|....*....|
gi 2791281350 154 GGQRQRVAIARALAVRPKLLLCDEITSALD 183
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-183 |
1.06e-05 |
|
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: 45.23 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 12 PVLRVSNLSCVNNervTLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-VTREAKRTWprknrl 90
Cdd:cd03291 38 NNLFFSNLCLVGA---PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFSW------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 91 mmqIVPqdpaSTLNPKMTALDAVERAARVSVRGRRDARRAAIDLLDKvgiDKQLAQRKPSGLSGGQRQRVAIARALAVRP 170
Cdd:cd03291 109 ---IMP----GTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEK---DNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170
....*....|...
gi 2791281350 171 KLLLCDEITSALD 183
Cdd:cd03291 179 DLYLLDSPFGYLD 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
37-222 |
1.28e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 37 VQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGVTREAKrtwprknrlmmqivPQdpastlnpkmtaldavera 116
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK--------------PQ------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 117 arvsvrgrrdarraAIDLldkvgidkqlaqrkpsglSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQE 196
Cdd:cd03222 69 --------------YIDL------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*.
gi 2791281350 197 LNSEGMGIVLVSHDDELLQSYCSTVI 222
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
43-196 |
1.31e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 43 VGVKGPSGSGKSTLLRCLIGLNHAESGEIECAGvtREAKRTWPRKNRLMMQIVPQDP---ASTLNPKMT----------- 108
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG--RPLSSLSHSVLRQGVAMVQQDPvvlADTFLANVTlgrdiseeqvw 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 109 -ALDAVERAARVSvrgrrdarraaiDLLDkvGIDKQLAQRKpSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDY--- 184
Cdd:PRK10790 448 qALETVQLAELAR------------SLPD--GLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANIDSgte 512
|
170
....*....|..
gi 2791281350 185 QAATKVMSVLQE 196
Cdd:PRK10790 513 QAIQQALAAVRE 524
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
40-225 |
2.70e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 40 GTMVGVKGPSGSGKSTLL-----RCLIGLNHAEsgEIECAGVTREAK----------------RTwPRKNrlmmqivpqd 98
Cdd:cd03271 21 GVLTCVTGVSGSGKSSLIndtlyPALARRLHLK--KEQPGNHDRIEGlehidkvividqspigRT-PRSN---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 99 PAS------------------------TLNPK-----------MTALDAVERAARVSvrgrrdARRAAIDLLDKVGIDK- 142
Cdd:cd03271 88 PATytgvfdeirelfcevckgkrynreTLEVRykgksiadvldMTVEEALEFFENIP------KIARKLQTLCDVGLGYi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 143 QLAQRKPSgLSGGQRQRVAIARALAVR---PKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELLQSyCS 219
Cdd:cd03271 162 KLGQPATT-LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC-AD 239
|
....*.
gi 2791281350 220 TVIPIG 225
Cdd:cd03271 240 WIIDLG 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
135-212 |
2.98e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 2.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 135 LDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVL-VSHDDE 212
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAE 463
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
39-217 |
3.55e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 39 RGTMVGVKGPSGSGKSTLLRCLiglnhaesgeieCAGVTREAKRTWPRKNRLMMQIVPQdpastlnpkmtaldavERAAR 118
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI------------GLALGGAQSATRRRSGVKAGCIVAA----------------VSAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 119 VSVRgrrdarraaidlldkvgidkqlaqrkpSGLSGGQRQRVAIARALA-----VRPkLLLCDEITSALDYQAATKVMSV 193
Cdd:cd03227 72 IFTR---------------------------LQLSGGEKELSALALILAlaslkPRP-LYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|....
gi 2791281350 194 LQELNSEGMGIVLVSHDDELLQSY 217
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPELAELA 147
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-213 |
4.51e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 149 PSGLSGGQRQ------RVAIARALAV-------RPKLLLcDEITSALDYQAATKVMSVLQELNSEGMG-IVLVSHDDEL 213
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEgiegdapLPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEqIVVVSHDDEL 856
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-209 |
6.37e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 132 IDLLDKVGIDK-QLAQRKPSgLSGGQRQRVAIARALAVR---PKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLV 207
Cdd:TIGR00630 810 LQTLCDVGLGYiRLGQPATT-LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVI 888
|
..
gi 2791281350 208 SH 209
Cdd:TIGR00630 889 EH 890
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-191 |
6.59e-05 |
|
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: 42.92 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 28 TLFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAEsGEIECAGVTREAKRTwpRKNRLMMQIVPQDPASTLNPKM 107
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPL--QKWRKAFGVIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 108 TALDAVERAARVSVrgrrdarraaIDLLDKVGIdKQLAQRKPSG-----------LSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:cd03289 95 KNLDPYGKWSDEEI----------WKVAEEVGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170
....*....|....*...
gi 2791281350 177 EITSALD---YQAATKVM 191
Cdd:cd03289 164 EPSAHLDpitYQVIRKTL 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-183 |
1.24e-04 |
|
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: 42.59 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 29 LFQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIGLNHAESGEIECAG-VTREAKRTWprknrlmmqIVPqdpaSTLNPKM 107
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTSW---------IMP----GTIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2791281350 108 TALDAVERAARVSVRGRRDARRAAIDLLDKvgiDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALD 183
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEK---DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
132-228 |
1.25e-04 |
|
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: 41.86 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 132 IDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARAL--AVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
90
....*....|....*....
gi 2791281350 210 DDELLQSyCSTVIPIGTAA 228
Cdd:cd03270 198 DEDTIRA-ADHVIDIGPGA 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-190 |
2.10e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 24 NERVTLfQGLSFAVQRGTMVGVKGPSGSGKSTLLRCLIG-LNHAESGEIECAG-VTREAKRTW-----PRKNRLMmqivp 96
Cdd:PLN03130 628 AERPTL-SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGtVAYVPQVSWifnatVRDNILF----- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 97 qdpASTLNPkmtalDAVERAARVSvrgrrdARRAAIDLLDkvGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCD 176
Cdd:PLN03130 702 ---GSPFDP-----ERYERAIDVT------ALQHDLDLLP--GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170
....*....|....
gi 2791281350 177 EITSALDYQAATKV 190
Cdd:PLN03130 766 DPLSALDAHVGRQV 779
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
149-214 |
3.13e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 3.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2791281350 149 PSGLSGGQRQ---RVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSHDDELL 214
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-208 |
3.49e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 3.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 152 LSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVS 208
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVIS 461
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
14-216 |
4.21e-04 |
|
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: 39.90 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNL-SCVNNERVTLFQGLSFAVqrgtmvgvkGPSGSGKSTLLRCLiglNHAESGEIecagvtreakrtwPRKNRLmm 92
Cdd:cd03240 4 LSIRNIrSFHERSEIEFFSPLTLIV---------GQNGAGKTTIIEAL---KYALTGEL-------------PPNSKG-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 93 qivpqdpaSTLNPKMTAldAVERAARVSVRGRRDARRA-----AIDLLDKVGIDKQ-----LAQRKPSGLSGGQRQ---- 158
Cdd:cd03240 57 --------GAHDPKLIR--EGEVRAQVKLAFENANGKKytitrSLAILENVIFCHQgesnwPLLDMRGRCSGGEKVlasl 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2791281350 159 --RVAIARALAVRPKLLLCDEITSALD-YQAATKVMSVLQELNSEG-MGIVLVSHDDELLQS 216
Cdd:cd03240 127 iiRLALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKnFQLIVITHDEELVDA 188
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
142-197 |
8.33e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.55 E-value: 8.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2791281350 142 KQLAQRKPSGLSGGQRQRVAIARALAVR-----PKLLLcDEITSALDYQAATKVMSVLQEL 197
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQkcdpaPFYLF-DEIDAALDAQYRTAVANMIKEL 208
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
133-219 |
8.60e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 133 DLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEgmgIVLVSHDDE 212
Cdd:PRK15064 137 ELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNST---MIIISHDRH 213
|
....*..
gi 2791281350 213 LLQSYCS 219
Cdd:PRK15064 214 FLNSVCT 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
133-209 |
1.17e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2791281350 133 DLLDKVGIdKQLAQRKPSGLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:NF000106 127 ELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
152-215 |
1.30e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2791281350 152 LSGGQRQRVAIARALA---VRPK-LLLCDEITSALDYQAATKVMSVLQELnSEGMGIVLVSHDDELLQ 215
Cdd:pfam02463 1078 LSGGEKTLVALALIFAiqkYKPApFYLLDEIDAALDDQNVSRVANLLKEL-SKNAQFIVISLREEMLE 1144
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
151-215 |
2.16e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2791281350 151 GLSGGQRQRVAIARALAVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVShddeLLQ 215
Cdd:PLN03140 336 GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMS----LLQ 396
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-225 |
2.26e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 132 IDLLDKVGIDKQLAQRKPSGLSGGQRQRVAIARAL---AVRPKLLLCDEITSALDYQAATKVMSVLQELNSEGMGIVLVS 208
Cdd:PRK00635 790 IHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
90
....*....|....*..
gi 2791281350 209 HDDELLQSyCSTVIPIG 225
Cdd:PRK00635 870 HNMHVVKV-ADYVLELG 885
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-210 |
2.28e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 14 LRVSNL-SCVNNERVTLFQGLsFAVQrgtmvgvkGPSGSGKSTLLRCL---IGLNHAESGEIECAGVTREAKRTW----- 84
Cdd:COG0419 5 LRLENFrSYRDTETIDFDDGL-NLIV--------GPNGAGKSTILEAIryaLYGKARSRSKLRSDLINVGSEEASvelef 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 85 ---PRKNRL---------MMQIVPQDPASTLNpKMTALDAVERAARVSVRGRRDARRAAIDLLDKVGIDKQLAQR----- 147
Cdd:COG0419 76 ehgGKRYRIerrqgefaeFLEAKPSERKEALK-RLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgld 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2791281350 148 KPSGLSGGQRQRVAIARALAvrpklLLCDeiTSALDYQAATKVMSVLQELnsegmgiVLVSHD 210
Cdd:COG0419 155 PIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
47-82 |
3.02e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.05 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2791281350 47 GPSGSGKSTLLRCLIGLNHAESGEIEcaGVTREAKR 82
Cdd:cd00882 4 GRGGVGKSSLLNALLGGEVGEVSDVP--GTTRDPDV 37
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
47-71 |
6.83e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.61 E-value: 6.83e-03
10 20
....*....|....*....|....*
gi 2791281350 47 GPSGSGKSTLLRCLIGLNHAESGEI 71
Cdd:cd01854 92 GQSGVGKSTLLNALLPELVLATGEI 116
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
44-82 |
8.06e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 35.68 E-value: 8.06e-03
10 20 30
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gi 2791281350 44 GVKGPSGSGKSTLLRCLIGLNHAESGEIecAGVTREAKR 82
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNVGIVSPI--PGTTRDPVR 37
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| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
143-215 |
9.19e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 36.40 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2791281350 143 QLAQRKPSG--------LSGGQRQRVAIARALAVR-----PKLLLcDEITSALDYQAATKVMSVLQELNSEGMGIVLVSH 209
Cdd:cd03275 139 SIASKNPPGkrfrdmdnLSGGEKTMAALALLFAIHsyqpaPFFVL-DEVDAALDNTNVGKVASYIREQAGPNFQFIVISL 217
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....*.
gi 2791281350 210 DDELLQ 215
Cdd:cd03275 218 KEEFFS 223
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