|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-253 |
4.43e-105 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 304.32 E-value: 4.43e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNvvNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfkDWQK 80
Cdd:COG1121 1 MMM--MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKAnSFNSGFPATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLV 160
Cdd:COG1121 77 IGYVPQRA-EVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 161 SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNKKLHFHGDACEYneLDEGELS 240
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEV--LTPENLS 232
|
250
....*....|...
gi 1025889903 241 SIYGHGVQFLNHD 253
Cdd:COG1121 233 RAYGGPVALLAHG 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-226 |
6.83e-90 |
|
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: 264.78 E-value: 6.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRrfKDWQKVGFVSQKAn 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKRIGYVPQRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSGFPATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILD 169
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 170 EPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNKKLHFHG 226
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-254 |
9.61e-59 |
|
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: 186.79 E-value: 9.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDW-QKVGFV 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLsrRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkanSFNSGFPATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:COG1120 81 PQ---EPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG---TVTDkvtHVACLNK-KLHFHGDACEynELDEGELS 240
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNlaaRYAD---RLVLLKDgRIVAQGPPEE--VLTPELLE 232
|
250
....*....|....
gi 1025889903 241 SIYGHGVQFLNHDH 254
Cdd:COG1120 233 EVYGVEARVIEDPV 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-218 |
4.55e-53 |
|
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: 172.19 E-value: 4.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGK-IEIFGE--------DIRRfk 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggedvwELRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 dwqKVGFVSqkaNSFNSGFPA--TVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVF 154
Cdd:COG1119 79 ---RIGLVS---PALQLRFPRdeTVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACL 218
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-230 |
1.32e-52 |
|
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: 170.21 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW---QKVGFV 84
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkaNSFNSGFPATVFEVVQSGLtKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:COG1122 81 FQ--NPDDQLFAPTVEEDVAFGP-ENLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDACE 230
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPRE 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-220 |
7.28e-50 |
|
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: 162.64 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW---QKVGFV 84
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANS--FNSgfpaTVFEVVQSGLtkkiGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:cd03225 81 FQNPDDqfFGP----TVEEEVAFGL----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-204 |
1.32e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.82 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDL----VLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDIRRFKDWQ-- 79
Cdd:COG1136 2 SPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTllnilggldrptsGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 -----KVGFVSQkanSFN--SGFpaTVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQR 152
Cdd:COG1136 82 rlrrrHIGFVFQ---FFNllPEL--TALENVALPLL----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-243 |
6.02e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.69 E-value: 6.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD--WQKVGFVSQ 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAevRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSgfpATVFEVVQsgLTKkiGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:COG1131 81 EPALYPD---LTVRENLR--FFA--RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDAceyNELDEGELSSIY 243
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTP---DELKARLLEDVF 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-204 |
6.36e-47 |
|
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: 155.34 E-value: 6.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW------ 78
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 -QKVGFVSQkanSFN--SGFpaTVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFI 155
Cdd:cd03255 81 rRHIGFVFQ---SFNllPDL--TALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD 200
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-244 |
5.45e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 5.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-----RRFKDWQ- 79
Cdd:COG3638 1 PMLELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgRALRRLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQkansfnsGFP----ATVFEVVQSGLTKKIG----LFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQ 151
Cdd:COG3638 81 RIGMIFQ-------QFNlvprLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDAce 230
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDgRVVFDGPP-- 231
|
250
....*....|....
gi 1025889903 231 yNELDEGELSSIYG 244
Cdd:COG3638 232 -AELTDAVLREIYG 244
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-226 |
3.39e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 144.90 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-----RFKD- 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQKVGFVSQkansfnsgFP------ATVFEVVQSGLTKkiglFKFAGKEDKQKVKKALESVDM-LEYQNRNIGALSGGQQ 150
Cdd:TIGR04521 81 RKKVGLVFQ--------FPehqlfeETVYKDIAFGPKN----LGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHG 226
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDG 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-208 |
4.07e-42 |
|
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: 150.05 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKD-----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---- 77
Cdd:COG1123 259 PLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 --WQKVGFVSQkaNSFNSGFPA-TVFEVVQSGLTKkigLFKFAGKEDKQKVKKALESVDM-LEYQNRNIGALSGGQQQRV 153
Cdd:COG1123 339 elRRRVQMVFQ--DPYSSLNPRmTVGDIIAEPLRL---HGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVV 468
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-204 |
2.10e-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: 144.86 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDI------RRfkdwqK 80
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfetpdsGRILLDGRDVtglppeKR-----N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQkansfnSG--FP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:COG3842 79 VGMVFQ------DYalFPhLTVAENVAFGLRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-220 |
2.58e-41 |
|
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: 147.74 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLL---LGLFKLQKGKIEIFGEDIRRFKD--- 77
Cdd:COG1123 2 TPLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALmglLPHGGRISGEVLLDGRDLLELSEalr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQKVGFVSQKA-NSFNsgfPATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:COG1123 82 GRRIGMVFQDPmTQLN---PVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
23-243 |
2.91e-41 |
|
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: 141.55 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW------QKVGFVSQkanSFNSGFP 96
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrRQIGMIFQ---QFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVVQSGLTKKI----GLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPT 172
Cdd:cd03256 93 LSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 173 VGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDAceyNELDEGELSSIY 243
Cdd:cd03256 173 ASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPP---AELTDEVLDEIY 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-212 |
3.24e-41 |
|
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: 141.10 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDL----VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI------RRFKD 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQKVGFVSQKA-NSFNSGFpaTVFEVVQSGLTKKIGLFKfaGKEDKQKVKKALESVDMLE-YQNRNIGALSGGQQQRVFI 155
Cdd:cd03257 81 RKEIQMVFQDPmSSLNPRM--TIGEQIAEPLRIHGKLSK--KEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV---TDKV 212
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVakiADRV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-204 |
3.85e-41 |
|
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: 139.11 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDW-QKVGFVSQka 88
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLspKELaRKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfnsgfpatvfevvqsgltkkiglfkfagkedkqkvkkALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMIL 168
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 1025889903 169 DEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-212 |
8.66e-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: 139.58 E-value: 8.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQK 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFnsgfP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03259 81 YALF----PhLTVAENIAFGLKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG---TVTDKV 212
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEealALADRI 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-220 |
4.34e-40 |
|
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: 138.14 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQK 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:cd03300 81 YALFPH---LTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG---TVTDKvthVACLNK 220
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEealTMSDR---IAVMNK 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-204 |
8.27e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.11 E-value: 8.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ------K 80
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQ-------KansfnsgfpaTVFEVVQ-----SGLTKkiglfkfagKEDKQKVKKALESVDMLEYQNRNIGALSGG 148
Cdd:COG2884 81 IGVVFQdfrllpdR----------TVYENVAlplrvTGKSR---------KEIRRRVREVLDLVGLSDKAKALPHELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNkKLGITLILVTHD 204
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHD 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-230 |
3.66e-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: 135.88 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI------RRFKDWQ 79
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQKANSFNSgfpATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSL 159
Cdd:COG1127 83 RIGMLFQGGALFDS---LTVFENVAFPLREHTDLSE---AEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACL-NKKLHFHGDACE 230
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEE 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-204 |
5.18e-39 |
|
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: 136.41 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD-W---QKVG 82
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWeirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQkaNSFNSGFPATVFEVVQSGLtKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:TIGR04520 81 MVFQ--NPDNQFVGATVEDDVAFGL-ENLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-226 |
9.63e-39 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 134.94 E-value: 9.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ------KVG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFNSgfpATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:cd03261 81 MLFQSGALFDS---LTVFENVAFPLREHTRLSE---EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACL-NKKLHFHG 226
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEG 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-254 |
1.21e-38 |
|
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: 134.60 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--QKVGFVSQk 87
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarRQIGVLPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfNSGFPA--TVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:COG4555 82 ----ERGLYDrlTVRENIRYFAE----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVT---DKVTHVAclNKKLHFHGDACEYNEldEGELSSI 242
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEalcDRVVILH--KGKVVAQGSLDELRE--EIGEENL 228
|
250
....*....|..
gi 1025889903 243 YGHGVQFLNHDH 254
Cdd:COG4555 229 EDAFVALIGSEE 240
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-244 |
1.71e-38 |
|
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: 134.35 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKY-TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD------WQK 80
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNsgfPATVFEVVQSG-LTKKI---GLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:TIGR02315 81 IGMIFQHYNLIE---RLTVLENVLHGrLGYKPtwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDAceyNELD 235
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAP---SELD 234
|
....*....
gi 1025889903 236 EGELSSIYG 244
Cdd:TIGR02315 235 DEVLRHIYG 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-226 |
7.36e-38 |
|
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: 131.93 E-value: 7.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFlAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--QKVGFVSQ 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KaNSFNSGFpaTVFEVVQ-SGLTKKIglfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:cd03264 80 E-FGVYPNF--TVREFLDyIAWLKGI-----PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTDKVTHVACLNK-KLHFHG 226
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKgKLVFEG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-204 |
7.66e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 131.20 E-value: 7.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDirrfkdwqKVGFVSQKAnSFNSGFPATVFEV 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--------RVAYVPQRS-EVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQ 182
Cdd:NF040873 78 VAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|..
gi 1025889903 183 FYEMLEMLNKKlGITLILVTHD 204
Cdd:NF040873 158 IIALLAEEHAR-GATVVVVTHD 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-206 |
7.77e-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: 7.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKST-----LLKLLLGLFKLQKGKIEIFGEDI----------R 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVLLDGKDIydldvdvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 74 RfkdwqKVGFVSQKANSfnsgFPATVFEVVQSGLtkKIGLFKfAGKEDKQKVKKALESVDMLEYQNRNIGA--LSGGQQQ 151
Cdd:cd03260 81 R-----RVGMVFQKPNP----FPGSIYDNVAYGL--RLHGIK-LKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlgITLILVTHDVG 206
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQ 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-220 |
2.24e-37 |
|
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: 131.16 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYT----KDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW----- 78
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 -QKVGFVSQKANSFNSgfpATVFEVVQSGLtkKIGlfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:cd03258 81 rRRIGMIFQHFNLLSS---RTVFENVALPL--EIA--GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-220 |
1.26e-36 |
|
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: 126.98 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFVSQ 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 kansfnsgfpatvfevvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrnigaLSGGQQQRVFIARSLVSEPELM 166
Cdd:cd00267 81 ----------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-210 |
1.46e-36 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 130.39 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQkANSFNSGFPATVFEVV 103
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQ-SEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 QSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQF 183
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180
....*....|....*....|....*..
gi 1025889903 184 YEMLEMLNKKlGITLILVTHDVGTVTD 210
Cdd:PRK15056 182 ISLLRELRDE-GKTMLVSTHNLGSVTE 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-220 |
4.07e-36 |
|
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: 125.97 E-value: 4.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--QKVGFVSQ 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSgfpATVFEVVQsgltkkiglfkfagkedkqkvkkalesvdmleyqnrnigaLSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03230 81 EPSLYEN---LTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-208 |
1.36e-35 |
|
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: 124.80 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKVGF 83
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNsgfpATVFEvvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrNIgaLSGGQQQRVFIARSLVSEP 163
Cdd:cd03228 81 VPQDPFLFS----GTIRE---------------------------------------NI--LSGGQRQRIAIARALLRDP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTV 208
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI 158
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-212 |
1.99e-35 |
|
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: 124.61 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW-----QKVGF 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpATVFEvvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrNIG-ALSGGQQQRVFIARSLVSE 162
Cdd:cd03229 81 VFQDFALFPH---LTVLE---------------------------------------NIAlGLSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG---TVTDKV 212
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDeaaRLADRV 171
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-205 |
2.65e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKD----LVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglFKLQKGKIEIFGEDIRRFKdwQKVG 82
Cdd:COG1116 6 PALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTllrliaglEKPTSGEVLVDGKPVTGPG--PDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSfnsgFP-ATVFEVVQSGLtKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:COG1116 84 VVFQEPAL----LPwLTVLDNVALGL-ELRGVPK---AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-212 |
1.83e-34 |
|
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: 123.02 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKDW----QKVGF 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtDDKKNInelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQkanSFNSgFP-ATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:cd03262 81 VFQ---QFNL-FPhLTVLENITLAPIKVKGMSK---AEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVG---TVTDKV 212
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGfarEVADRV 205
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-203 |
2.01e-34 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 123.29 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 17 KYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-------VGFVSQkan 89
Cdd:NF038007 14 KTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKiilrrelIGYIFQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSGFPATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILD 169
Cdd:NF038007 91 SFNLIPHLSIFDNVALPLKYR----GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 170 EPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTH 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-204 |
4.14e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.57 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDI------RRfkdwqKVG 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmiagledptsGEILIGGRDVtdlppkDR-----NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQkansfnsgFPA-----TVFEVVQSGLtkKIGlfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:COG3839 79 MVFQ--------SYAlyphmTVYENIAFPL--KLR--KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKnvhqfyemL--EM------LNKKLGITLILVTHD 204
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAK--------LrvEMraeikrLHRRLGTTTIYVTHD 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-205 |
2.03e-33 |
|
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: 120.65 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY----TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDwqKVGFV 84
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP--DRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSfnsgFP-ATVFEVVQSGLtkkiglfKFAG---KEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLV 160
Cdd:cd03293 79 FQQDAL----LPwLTVLDNVALGL-------ELQGvpkAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025889903 161 SEPELMILDEPTVGVDS---KNVHQfyEMLEMLnKKLGITLILVTHDV 205
Cdd:cd03293 148 VDPDVLLLDEPFSALDAltrEQLQE--ELLDIW-RETGKTVLLVTHDI 192
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-204 |
2.23e-33 |
|
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: 120.55 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD--WQKVGFVSQKAN 89
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRevRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 sfnsgfpatvfevVQSGLTKKIGLFKFA------GKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:cd03265 84 -------------VDDELTGWENLYIHArlygvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHY 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-218 |
2.33e-33 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 121.63 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFVSQKA 88
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 NSfnsgfPA--TVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK10253 91 TT-----PGdiTVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACL 218
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-205 |
2.63e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE--------DIRRf 75
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 76 kdwqKVGFVSQkaNSFNSGFPATVFEVVQSGLtKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFI 155
Cdd:PRK13635 82 ----QVGMVFQ--NPDNQFVGATVQDDVAFGL-ENIGVPR---EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDL 201
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-212 |
3.26e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD-----WQKV 81
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQkaNSFNSGFPATVFEVVQSGlTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:PRK13639 81 GIVFQ--NPDDQLFAPTVEEDVAFG-PLNLGLSK---EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTV---TDKV 212
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVpvyADKV 207
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-220 |
3.49e-33 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 120.29 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK-DWQKVGFVSQKANS 90
Cdd:TIGR00968 4 ANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHaRDRKIGFVFQHYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 91 FNSgfpATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:TIGR00968 84 FKH---LTVRDNIAFGLE----IRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 171 PTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-209 |
5.88e-33 |
|
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: 120.29 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--RRFKDW-QKVGFVSQKA-NSFNSGFpaT 98
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFrRRVQMVFQDPyASLHPRH--T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 99 VFEVVQSGLtkkiglfKFAGKED-KQKVKKALESVDM-LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:COG1124 98 VDRILAEPL-------RIHGLPDrEERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1025889903 177 SknVHQFyEMLEMLN---KKLGITLILVTHDVGTVT 209
Cdd:COG1124 171 V--SVQA-EILNLLKdlrEERGLTYLFVSHDLAVVA 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-204 |
6.30e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK--DW-QKVGFVSQ 86
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppEWrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KAnsfnSGFPATVFEVVQSGltkkiglFKFAGKE-DKQKVKKALESVDM-LEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:COG4619 82 EP----ALWGGTVRDNLPFP-------FQLRERKfDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHD 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-254 |
8.60e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.80 E-value: 8.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKVGFVS 85
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QkANSFNSGFpaTVFEVVQSG--------LTkkiglfkfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:COG4604 82 Q-ENHINSRL--TVRELVAFGrfpyskgrLT----------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT---DKVthVACLNKKLHFHGDACEYneL 234
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAScyaDHI--VAMKDGRVVAQGTPEEI--I 224
|
250 260
....*....|....*....|
gi 1025889903 235 DEGELSSIYGHGVQFLNHDH 254
Cdd:COG4604 225 TPEVLSDIYDTDIEVEEIDG 244
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-212 |
8.73e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.33 E-value: 8.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKDW----QKVG 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDInklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQkanSFNSgFP-ATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:COG1126 81 MVFQ---QFNL-FPhLTVLENVTLAPIKVKKMSK---AEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 162 EPELMILDEPTVGVDSKNVHqfyEMLEMLnKKL---GITLILVTHDVG---TVTDKV 212
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVG---EVLDVM-RDLakeGMTMVVVTHEMGfarEVADRV 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-212 |
9.54e-33 |
|
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: 119.36 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYtKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK-DWQKVGFVSQK 87
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfNSGFP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03299 80 ----YALFPhMTVYKNIAYGLKKR----KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD---VGTVTDKV 212
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfeeAWALADKV 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
1.09e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 2 DNVVNPIVKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRR---FK 76
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenlKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 DWQKVGFVSQkaNSFNSGFPATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:PRK13632 81 IRKKIGIIFQ--NPDNQFIGATVEDDIAFGLENK----KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT--DKV 212
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIlaDKV 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-219 |
1.12e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 119.76 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDIRRFKDWQKVG------FvsQKANSFNSgfp 96
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTlfnlitgfyrptsGRILFDGRDITGLPPHRIARlgiartF--QNPRLFPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVVQSGLTKKIGLFKFAG-----------KEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:COG0411 94 LTVLENVLVAAHARLGRGLLAAllrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLN 219
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-219 |
1.75e-32 |
|
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: 118.69 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVG------FvsQKANSFNSgfp 96
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgigrtF--QIPRLFPE--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVV----QSGLTKKIGLFKFAGKEDK--QKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:cd03219 90 LTVLENVmvaaQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 171 PTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLN 219
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-205 |
2.34e-32 |
|
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: 118.56 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFV 84
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKAnsfnsG-FP-ATVFEVVqsGLTKKigLFKFAGKEDKQKVKKALESVDM--LEYQNRNIGALSGGQQQRVFIARSLV 160
Cdd:cd03295 81 IQQI-----GlFPhMTVEENI--ALVPK--LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 161 SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI 196
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-204 |
2.79e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 117.33 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKdwqkvgfvSQKANSF 91
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLN--------SKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 92 NSGFPATVF--------EVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:TIGR03608 74 RREKLGYLFqnfalienETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHD 193
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-173 |
2.97e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.44 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQK-VGFVSQKANSFNSgfpATVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKeIGYVFQDPQLFPR---LTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 101 EVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGA----LSGGQQQRVFIARSLVSEPELMILDEPTV 173
Cdd:pfam00005 78 ENLRLGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-205 |
1.12e-31 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 116.38 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNVVNPIVKFEDISYKYT---KDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI---- 72
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGtgaGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfald 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 73 -------RRfkdwQKVGFVSQkanSF----------NSGFPAtvfevvqsgltkkiglfKFAG-KEDKQKVKKALESVDM 134
Cdd:COG4181 81 edararlRA----RHVGFVFQ---SFqllptltaleNVMLPL-----------------ELAGrRDARARARALLERVGL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 135 LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:COG4181 137 GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-204 |
2.42e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.98 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFVSQKA 88
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfNSGFPATVFEVVQSGLTKKIGlfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSL--VSEPE-- 164
Cdd:COG4559 85 ---SLAFPFTVEEVVALGRAPHGS----SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdg 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 165 ---LMILDEPTVGVDSKNVHQFYEMLemlnKKL---GITLILVTHD 204
Cdd:COG4559 158 gprWLFLDEPTSALDLAHQHAVLRLA----RQLarrGGGVVAVLHD 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-204 |
3.55e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.64 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFVSQKA 88
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfNSGFPATVFEVVQSGLTKkiglFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLV------SE 162
Cdd:PRK13548 86 ---SLSFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-220 |
5.15e-31 |
|
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: 114.74 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfKDWQK--VGFVSQ 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-VPVQErnVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSgfpATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03296 82 HYALFRH---MTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-204 |
5.64e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.89 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfKDWQ----KVGFV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPpkdrDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkanSFnSGFP-ATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:cd03301 78 FQ---NY-ALYPhMTVYDNIAFGLK----LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-205 |
7.25e-31 |
|
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: 114.07 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKV----GFVSQK 87
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragiGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGltkkiglfkfAGKEDKQKVKKALESV-DML----EYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:cd03224 84 RRIFPE---LTVEENLLLG----------AYARRRAKRKARLERVyELFprlkERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDV 205
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNA 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-204 |
1.06e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.97 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVS 85
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRhVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QkanSFnSGFP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:PRK09452 93 Q---SY-ALFPhMTVFENVAFGLRMQ----KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
1.09e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNvvnpIVKFEDISYKYTKDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKDW 78
Cdd:PRK13647 1 MDN----IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 --QKVGFVSQKANsfNSGFPATVFEVVQSGlTKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:PRK13647 77 vrSKVGLVFQDPD--DQVFSSTVWDDVAFG-PVNMGL---DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDV 205
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDV 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-203 |
2.68e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKD------LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD-W 78
Cdd:PRK13633 2 NEMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 ---QKVGFVSQkaNSFNSGFPATVFEVVQSGlTKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFI 155
Cdd:PRK13633 82 dirNKAGMVFQ--NPDNQIVATIVEEDVAFG-PENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-213 |
4.97e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.40 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD----LVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDI--------RRF 75
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlircinllerptsGSVLVDGVDLtalserelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 76 KdwQKVGFVSQKANSFNSgfpATVFEVV-----QSGLTKKiglfkfagkEDKQKVKKALESVDMLEYQNRNIGALSGGQQ 150
Cdd:COG1135 81 R--RKIGMIFQHFNLLSS---RTVAENValpleIAGVPKA---------EIRKRVAELLELVGLSDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD---VGTVTDKVT 213
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvVRRICDRVA 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-214 |
6.08e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 111.19 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ------K 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQkanSFNSGFPATVFEVVQSGLtkkiglfKFAGKED---KQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:TIGR02673 81 IGVVFQ---DFRLLPDRTVYENVALPL-------EVRGKKEreiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNkKLGITLILVTHDVgTVTDKVTH 214
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDL-SLVDRVAH 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-208 |
7.94e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 117.24 E-value: 7.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDW-QKVGF 83
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdpASLrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNsgfpATVFEvvqsgltkKIGLfkFAGKEDKQKVKKALESVDMLE--------YqNRNIG----ALSGGQQQ 151
Cdd:COG2274 554 VLQDVFLFS----GTIRE--------NITL--GDPDATDEEIIEAARLAGLHDfiealpmgY-DTVVGeggsNLSGGQRQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTV 208
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI 673
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-220 |
1.15e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGkiEIFGEDIR----RFKDWQ 79
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAitddNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 K-VGFVSQkaNSFNSGFPATVFEVVQSGLTKkiglFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:PRK13648 83 KhIGIVFQ--NPDNQFVGSIVKYDVAFGLEN----HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVgTVTDKVTHVACLNK 220
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNK 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
23-206 |
1.49e-29 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 110.52 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW-------QKVGFVSQkansFNSGF 95
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraklrnKKLGFIYQ----FHHLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 PA-TVFEVVQSGLTkkIGlfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:TIGR02211 96 PDfTALENVAMPLL--IG--KKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190
....*....|....*....|....*....|..
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVG 206
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLE 203
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
8-212 |
2.25e-29 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 110.85 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTL-----LKLLLGLFKLQKGKIEIFGEDI---------- 72
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrslnRMNDLVPGVRIEGKVLFDGQDIydkkidvvel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 73 RRfkdwqKVGFVSQKANSFnsgfPATVFEVVQSGLtkkiglfKFAGKEDKQK----VKKALESV-------DMLeyqNRN 141
Cdd:TIGR00972 81 RR-----RVGMVFQKPNPF----PMSIYDNIAYGP-------RLHGIKDKKEldeiVEESLKKAalwdevkDRL---HDS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTHDVGT---VTDKV 212
Cdd:TIGR00972 142 ALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQaarISDRT 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-205 |
2.35e-29 |
|
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: 109.65 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQkaNS 90
Cdd:cd03226 3 ENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQ--DV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 91 FNSGFPATVFEVVQSGLTkkiglfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:cd03226 81 DYQLFTDSVREELLLGLK--------ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1025889903 171 PTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDV 205
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDY 186
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-203 |
3.38e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.51 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllg-----lfklqkGKIEIFGEDI-------- 72
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndlipgarveGEILLDGEDIydpdvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 73 --RRfkdwqKVGFVSQKANsfnsGFPATVFEVVQSGLtkkiglfKFAGKEDKQK----VKKALESV-------DMLeyqN 139
Cdd:COG1117 89 elRR-----RVGMVFQKPN----PFPKSIYDNVAYGL-------RLHGIKSKSEldeiVEESLRKAalwdevkDRL---K 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 140 RNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTH 203
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTH 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-204 |
7.78e-29 |
|
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: 108.34 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD--WQKVGFV 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkANSFNSGFpaTVFEVVQSgltkkigLFKFAGKE-DKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:COG4133 81 GH-ADGLKPEL--TVRENLRF-------WAALYGLRaDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGItLILVTHD 204
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-204 |
8.21e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 8.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKST------------LlklllglfklqkGKIEIFGEDIRRFKDWQ 79
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTllriiagletpdS------------GRIVLNGRDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 --KVGFVSQkansfNSG-FP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFI 155
Cdd:COG1118 74 erRVGFVFQ-----HYAlFPhMTVAENIAFGLRVR----PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSK----------NVHqfyemlemlnKKLGITLILVTHD 204
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKvrkelrrwlrRLH----------DELGGTTVFVTHD 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-210 |
1.05e-28 |
|
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: 108.47 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGF 83
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpaTVFEVVQSGLTKkiglfkfAGKEDkqkVKKALESVDMLEYQNR-------NIG----ALSGGQQQR 152
Cdd:cd03251 81 VSQDVFLFND----TVAENIAYGRPG-------ATREE---VEEAARAANAHEFIMElpegydtVIGergvKLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-204 |
1.05e-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: 113.71 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKV 81
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddlRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANSFNsgfpATVFE---VVQSGLTkkiglfkfagkeDKQkVKKALESV---DMLEYQ----NRNIG----ALSG 147
Cdd:COG4987 412 AVVPQRPHLFD----TTLREnlrLARPDAT------------DEE-LWAALERVglgDWLAALpdglDTWLGeggrRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 148 GQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHD 204
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-205 |
3.63e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 5 VNPIVKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGL---FKLQKGKIEIFGEDIRRFKDW- 78
Cdd:PRK13640 2 KDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 --QKVGFVSQkaNSFNSGFPATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:PRK13640 82 irEKVGIVFQ--NPDNQFVGATVGDDVAFGLENR----AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-204 |
4.88e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDwQKVGFVSQ 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhaRD-RKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSgfpATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK10851 82 HYALFRH---MTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHD 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-212 |
5.02e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfGEDI----RRFKDW- 78
Cdd:PRK13634 3 ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagKKNKKLk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 ---QKVGFVSQkansfnsgFP-ATVFE-VVQsgltKKI--GLFKFAGKED--KQKVKKALESVDMLE-YQNRNIGALSGG 148
Cdd:PRK13634 82 plrKKVGIVFQ--------FPeHQLFEeTVE----KDIcfGPMNFGVSEEdaKQKAREMIELVGLPEeLLARSPFELSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH---DVGTVTDKV 212
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeDAARYADQI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-204 |
6.88e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.95 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLV-LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD------WQKV 81
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQ------KANSF-NSGFPatvFEVVQSGltkkiglfkfaGKEDKQKVKKALESVDmLEYQNRNIGA-LSGGQQQRV 153
Cdd:cd03292 81 GVVFQdfrllpDRNVYeNVAFA---LEVTGVP-----------PREIRKRVPAALELVG-LSHKHRALPAeLSGGEQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-206 |
1.71e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.56 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFG-------EDIRRFKdwQK 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkVDERLIR--QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKansFNSgFPA-TVFEVVQSGLTKKIGlfkfAGKEDKQKVKKAL-ESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:PRK09493 79 AGMVFQQ---FYL-FPHlTALENVMFGPLRVRG----ASKEEAEKQARELlAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVG 206
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-210 |
1.74e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDIRRF--KDW-QKVGFV 84
Cdd:COG1132 340 IEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTlvnlllrfydptsGRILIDGVDIRDLtlESLrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNsgfpATVFEvvqsgltkKIGLfkfaGKED--KQKVKKALESVDMLEYQNR-------NIG----ALSGGQQQ 151
Cdd:COG1132 420 PQDTFLFS----GTIRE--------NIRY----GRPDatDEEVEEAAKAAQAHEFIEAlpdgydtVVGergvNLSGGQRQ 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN 540
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-204 |
2.45e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ---KVGFV 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSfnsgfPA--TVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:PRK11231 82 PQHHLT-----PEgiTVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHD 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-208 |
2.92e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE--DIRR---FKDWQKV 81
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANsfNSGFPATVFEVVQSGLTKkiglFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:PRK13636 85 GMVFQDPD--NQLFSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIV 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-212 |
3.67e-27 |
|
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: 106.29 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKL---LLGLFKLQKGKIEIFGEDIRRFKD-------WQKVGFVSQKA-NSF 91
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEDLLKLSEkelrkirGREIQMIFQDPmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 92 NsgfPA-TVFEVVQSGLTkkigLFKFAGKED-KQKVKKALESVDMLEYQNRnIGA----LSGGQQQRVFIARSLVSEPEL 165
Cdd:COG0444 100 N---PVmTVGDQIAEPLR----IHGGLSKAEaRERAIELLERVGLPDPERR-LDRypheLSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV---TDKV 212
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVaeiADRV 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-210 |
6.80e-27 |
|
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: 108.69 E-value: 6.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQK-VGFV 84
Cdd:COG4988 337 IELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpASWRRqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkansfNSG-FPATVFEVVQsgltkkiglfkFAGKE-DKQKVKKALESVDMLEYQNR-------NIGA----LSGGQQQ 151
Cdd:COG4988 417 PQ-----NPYlFAGTIRENLR-----------LGRPDaSDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ 537
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-204 |
9.45e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNvvNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK 80
Cdd:PRK11432 1 MTQ--KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 -VGFVSQkanSFnSGFP-ATVFEVVQSGLtKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:PRK11432 79 dICMVFQ---SY-ALFPhMSLGENVGYGL-KMLGVPK---EERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-212 |
9.82e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.43 E-value: 9.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNvvnpIVKFEDISYKYTKD---LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD 77
Cdd:PRK13650 1 MSN----IIEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 W---QKVGFVSQkaNSFNSGFPATVFEVVQSGLTKKiGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVF 154
Cdd:PRK13650 77 WdirHKIGMVFQ--NPDNQFVGATVEDDVAFGLENK-GI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT--DKV 212
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAlsDRV 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-227 |
1.07e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYtKDLVLeHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI------RRfkdwqKVGF 83
Cdd:COG3840 3 RLDDLTYRY-GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalppaER-----PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpATVFEVVQSGLTKKIGLfkfaGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:COG3840 76 LFQENNLFPH---LTVAQNIGLGLRPGLKL----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 164 ELMILDEPtvgvdsknvhqF--------YEMLEMLN---KKLGITLILVTH---DVGTVTDKVTHVAclNKKLHFHGD 227
Cdd:COG3840 149 PILLLDEP-----------FsaldpalrQEMLDLVDelcRERGLTVLMVTHdpeDAARIADRVLLVA--DGRIAADGP 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
23-204 |
1.32e-26 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 105.50 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF----KDWqkvGFVSQkanSFnSGFPA- 97
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLppqkRDY---GIVFQ---SY-ALFPNl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 98 TVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDS 177
Cdd:TIGR03265 92 TVADNIAYGLKNR----GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167
|
170 180
....*....|....*....|....*...
gi 1025889903 178 K-NVHQFYEMLEmLNKKLGITLILVTHD 204
Cdd:TIGR03265 168 RvREHLRTEIRQ-LQRRLGVTTIMVTHD 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-220 |
1.42e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.36 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrRFKDWQKVGFVSQka 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIGYLPE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfnsgfpatvfevvQSGLTKK---------IGLFKFAGKEDKQK-VKKALESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:cd03269 78 ---------------ERGLYPKmkvidqlvyLAQLKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-220 |
2.06e-26 |
|
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: 101.91 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKDWQKVGfVSQK 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEALRRIG-ALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFnsgFPA-TVFEVVQSGLTKKIGlfkfagkeDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03268 80 APGF---YPNlTARENLRLLARLLGI--------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINK 201
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-204 |
4.51e-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: 103.73 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 39 IVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKDWQKVGFVSQKAnsfnSGFP-ATVFEVVQSGLTKKiglfKF 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtNVPPHLRHINMVFQSY----ALFPhMTVEENVAFGLKMR----KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 117 AGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGI 196
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
....*...
gi 1025889903 197 TLILVTHD 204
Cdd:TIGR01187 153 TFVFVTHD 160
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
8-203 |
5.93e-26 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 103.62 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYtKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQ 86
Cdd:NF040840 1 MIRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRgIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KAnsfnSGFP-ATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:NF040840 80 NY----MLFPhKTVFENIAFGLK----LRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:NF040840 152 LLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTH 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-212 |
8.07e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfGEDIrrfkdwqKVGFVS 85
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QKANSFNSGfpATVFEVVQSGltkkiglfkfAGKEDKQKVKKALEsvDML---EYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:COG0488 385 QHQEELDPD--KTVLDELRDG----------APGGTEQEVRGYLG--RFLfsgDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 163 PELMILDEPTvgvdskNvHQFYEMLEMLNKKL----GiTLILVTHD---VGTVTDKV 212
Cdd:COG0488 451 PNVLLLDEPT------N-HLDIETLEALEEALddfpG-TVLLVSHDryfLDRVATRI 499
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-212 |
8.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 8.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL-----VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR----RFKDWQ 79
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 K-VGFVSQKANsfNSGFPATVFEVVQSGLtKKIGLFKfagKEDKQKVKKALESV--DMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:PRK13637 83 KkVGLVFQYPE--YQLFEETIEKDIAFGP-INLGLSE---EEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH---DVGTVTDKV 212
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmeDVAKLADRI 215
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
23-214 |
1.02e-25 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 100.48 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKV------GFVSQKANSFNSgfp 96
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVqlrrriGYIFQAHNLLGF--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:TIGR02982 97 LTARQNVQMALELQPNLSY---QEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 177 SKNVHQFYEMLEMLNKKLGITLILVTHD--VGTVTDKVTH 214
Cdd:TIGR02982 174 SKSGRDVVELMQKLAKEQGCTILMVTHDnrILDVADRILQ 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-220 |
1.49e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfKDWQKVGFVsqk 87
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRRIGYL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfnsgfPA--------TVFEVVQ-----SGLTKKiglfkfagkEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRV- 153
Cdd:COG4152 77 --------PEerglypkmKVGEQLVylarlKGLSKA---------EAKRRADEWLERLGLGDRANKKVEELSKGNQQKVq 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 154 FIArSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:COG4152 140 LIA-ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-201 |
1.88e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 100.06 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKV----G 82
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSfnsgFPA-TVFEVVQSGLtkkiglfkFAGKeDKQKVKKALESV-----DMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:COG0410 82 YVPEGRRI----FPSlTVEENLLLGA--------YARR-DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILV 201
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLV 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-205 |
2.83e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW---QKVGF 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKAN-SFNsgFpaTVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:PRK09536 82 VPQDTSlSFE--F--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 163 PELMILDEPTVGVDsknVHQFYEMLEMLNKKL--GITLILVTHDV 205
Cdd:PRK09536 158 TPVLLLDEPTASLD---INHQVRTLELVRRLVddGKTAVAAIHDL 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-219 |
3.47e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 99.80 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEifgedirrFKDWQKVGFVSQ 86
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANsFNSGFPATV--FEVVQSGLTKKiglfkfagkedkqKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:PRK09544 75 KLY-LDTTLPLTVnrFLRLRPGTKKE-------------DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLN 219
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-204 |
4.28e-25 |
|
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: 100.03 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLE---------HVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK 76
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 DWQ-------KVGFVSQkanSFnSGFP-ATVFEVVQSGLtkkiglfKFAG---KEDKQKVKKALESVDMLEYQNRNIGAL 145
Cdd:cd03294 93 RKElrelrrkKISMVFQ---SF-ALLPhRTVLENVAFGL-------EVQGvprAEREERAAEALELVGLEGWEHKYPDEL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 146 SGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHD 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-216 |
4.31e-25 |
|
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: 98.72 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVleHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQK 87
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGLTKKIGLfkfaGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:cd03298 79 NNLFAH---LTVEQNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH---DVGTVTDKVTHVA 216
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHqpeDAKRLAQRVVFLD 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-212 |
5.91e-25 |
|
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: 97.29 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFkDW----QKVGFVS 85
Cdd:cd03246 4 ENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPnelgDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QKANSfnsgFPATVFEvvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrNIgaLSGGQQQRVFIARSLVSEPEL 165
Cdd:cd03246 83 QDDEL----FSGSIAE---------------------------------------NI--LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVT--DKV 212
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAsaDRI 165
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-228 |
6.85e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 6.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE-----------DIRRFKd 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpsekAIRLLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 wQKVGFVSQKANSFnsgfP-ATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:COG4161 82 -QKVGMVFQQYNLW----PhLTVMENLIEAPCKVLGLSK---EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDA 228
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKgRIIEQGDA 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
13-204 |
7.97e-25 |
|
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: 97.75 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 13 DISYKYtKDLVLEhVSLEIPrGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE---DIRRFKDW----QKVGFVS 85
Cdd:cd03297 5 DIEKRL-PDFTLK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINLppqqRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QKAnsfnSGFP-ATVFEVVQSGLTKKiglfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:cd03297 82 QQY----ALFPhLNVRENLAFGLKRK------RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHD 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-208 |
9.06e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.78 E-value: 9.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL-----VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-----RFKDW 78
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKnkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 QKVGFVSQKansfnsgfpaTVFEVVQ--SGLTKKIG-LFKFA-----------------------GKEDKQKVKKALESV 132
Cdd:PRK13651 83 VLEKLVIQK----------TRFKKIKkiKEIRRRVGvVFQFAeyqlfeqtiekdiifgpvsmgvsKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 133 DM-LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTV 208
Cdd:PRK13651 153 GLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNV 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-210 |
1.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLE-----HVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI------RRFKD 77
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQK-VGFVSQKANsfNSGFPATVFEVVQSGLTKkiglFKFAGKEDKQKVKKALESVDMLE-YQNRNIGALSGGQQQRVFI 155
Cdd:PRK13641 83 LRKkVSLVFQFPE--AQLFENTVLKDVEFGPKN----FGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVTD 210
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAE 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-201 |
2.11e-24 |
|
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: 97.21 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKV----GFVSQK 87
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragiAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFnsgfPA-TVFEVVQSGLTKkiglfkfAGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:TIGR03410 84 REIF----PRlTVEENLLTGLAA-------LPRRSRKIPDEIYELFPVLkEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILV 201
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLV 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-208 |
4.77e-24 |
|
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: 95.90 E-value: 4.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 22 LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRR--FKDWQKVGFVSQKANSFNSgfpATV 99
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARRRLGFVSDSTGLYDR---LTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 100 FEVVQSgltkKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKN 179
Cdd:cd03266 96 RENLEY----FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180
....*....|....*....|....*....
gi 1025889903 180 VHQFYEMLEMLnKKLGITLILVTHDVGTV 208
Cdd:cd03266 172 TRALREFIRQL-RALGKCILFSTHIMQEV 199
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-208 |
6.41e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ--KVGFV 84
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 S--QKANSFNSgfpATVFE---VVQ-----SGLTKkiGLFKFAG--KEDKQKVKKA---LESVDMLEYQNRNIGALSGGQ 149
Cdd:PRK11300 84 RtfQHVRLFRE---MTVIEnllVAQhqqlkTGLFS--GLLKTPAfrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 150 QQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-228 |
7.30e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 14 ISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE-----------DIRRFKdwQKVG 82
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIRELR--RNVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFnsgfP-ATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:PRK11124 86 MVFQQYNLW----PhLTVQQNLIEAPCRVLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDA 228
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENgHIVEQGDA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-220 |
7.73e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE--------DIRRFkdw 78
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirEVRKF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 qkVGFVSQkaNSFNSGFPATVFEVVQSGLTKkIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:PRK13652 80 --VGLVFQ--NPDDQIFSPTVEQDIAFGPIN-LGLDE---ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-225 |
8.04e-24 |
|
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: 95.76 E-value: 8.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY-TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKVGFV 84
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNsgfpATVFEVVQSGLTKkiglfkfAGKEDKQKVKKALESVDMLE-----YQNRnIGA----LSGGQQQRVFI 155
Cdd:cd03253 81 PQDTVLFN----DTIGYNIRYGRPD-------ATDEEVIEAAKAAQIHDKIMrfpdgYDTI-VGErglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVT--DKV------------THVACLNKK 221
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVnaDKIivlkdgrivergTHEELLAKG 226
|
....
gi 1025889903 222 LHFH 225
Cdd:cd03253 227 GLYA 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-204 |
1.21e-23 |
|
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: 94.88 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 16 YKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD--WQKVGFVSQkansFNS 93
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaaRQSLGYCPQ----FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 94 GFPA-TVFEVVQ--SGLTkkiGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:cd03263 86 LFDElTVREHLRfyARLK---GLPK---SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 171 PTVGVDSKNVHQFYEMLEMLnkKLGITLILVTHD 204
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEV--RKGRSIILTTHS 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-205 |
1.66e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLL---GLFKLQKGKIEIFGEDIRR----FKDWQK 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTVQRegrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 ----VGFVSQKANSFNSgfpATVFEVVQSGLTKKIGL----FKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQR 152
Cdd:PRK09984 84 sranTGYIFQQFNLVNR---LSVLENVLIGALGSTPFwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-209 |
4.55e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKST-----LLKLLLGLFKLQKGKIEIFGEDI--RRF---K 76
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclNRMNELESEVRVEGRVEFFNQNIyeRRVnlnR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 DWQKVGFVSQKANSFnsgfPATVFEVVQSGLtkkiglfKFAGKEDKQK----VKKALESVDMLEYQNRNIGA----LSGG 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLF----PMSVYDNVAYGV-------KIVGWRPKLEiddiVESALKDADLWDEIKHKIHKsaldLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT 209
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVS 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-205 |
4.93e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 95.16 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDIRRFKDWQ---KVGFVS 85
Cdd:COG1125 3 EFENVTKRYPDGtVAVDDLSLTIPAGEFTVLVGPSGCGKTTtlrminrlieptsGRILIDGEDIRDLDPVElrrRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QkansfNSG-FP-ATVFEvvqsgltkKIG----LFKFAGKEDKQKVKKALESVDM--LEYQNRNIGALSGGQQQRVFIAR 157
Cdd:COG1125 83 Q-----QIGlFPhMTVAE--------NIAtvprLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 158 SLVSEPELMILDEPTVGVD--SKNVHQFyEMLEmLNKKLGITLILVTHDV 205
Cdd:COG1125 150 ALAADPPILLMDEPFGALDpiTREQLQD-ELLR-LQRELGKTIVFVTHDI 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-204 |
6.48e-23 |
|
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: 97.05 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKVG 82
Cdd:TIGR02868 333 PTLELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdevRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFNSgfpaTVFEVVQSGltkkiglfkfAGKEDKQKVKKALESVDMLEYQNRNIG-----------ALSGGQQQ 151
Cdd:TIGR02868 413 VCAQDAHLFDT----TVRENLRLA----------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHqfyEMLEMLNKKL-GITLILVTHD 204
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETAD---ELLEDLLAALsGRTVVLITHH 529
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-205 |
6.97e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.77 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKD----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-----Rfkdwqk 80
Cdd:COG4525 5 TVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 vGFVSQKansfNSGFP-ATVFEVVQSGLtkkiglfKFAG---KEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:COG4525 79 -GVVFQK----DALLPwLNVLDNVAFGL-------RLRGvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-204 |
7.64e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.67 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 4 VVNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVgf 83
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFnSGFP-ATVFEVVQSGLTKKiglfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:PRK11607 93 INMMFQSY-ALFPhMTVEQNIAFGLKQD----KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQF-YEMLEMLnKKLGITLILVTHD 204
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHD 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-205 |
1.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.00 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 5 VNPIVKFEDISYKYTKDL---VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--- 78
Cdd:PRK13642 1 MNKILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 QKVGFVSQkaNSFNSGFPATVFEVVQSGLTKKiGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARS 158
Cdd:PRK13642 81 RKIGMVFQ--NPDNQFVGATVEDDVAFGMENQ-GIPR---EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDL 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-205 |
1.24e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.57 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW-------QKVGFVSQkansFNSGF 95
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrnQKLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 PA-TVFEVVQSGLTkkIGlfKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:PRK11629 100 PDfTALENVAMPLL--IG--KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|.
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-203 |
1.45e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGL-----FKLQKGKIEIFGEDIRRFK----D 77
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRtdtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQK-VGFVSQKANSFnsgfPATVFEVVQSGLtkkiglfKFAGKEDKQKVKKALESV-------DmlEYQNR---NIGALS 146
Cdd:PRK14239 84 LRKeIGMVFQQPNPF----PMSIYENVVYGL-------RLKGIKDKQVLDEAVEKSlkgasiwD--EVKDRlhdSALGLS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 147 GGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTH 203
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTR 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-203 |
2.01e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLG-----LFKLQKGKIEIFGEDIrrFKD-----WQKVGFVSQKANSFN 92
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDI--FKMdvielRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 93 SgfpATVFEVVQSGLtkKIGLFKFAGKEDKQKVKKALESVDML-EYQNR---NIGALSGGQQQRVFIARSLVSEPELMIL 168
Cdd:PRK14247 96 N---LSIFENVALGL--KLNRLVKSKKELQERVRWALEKAQLWdEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1025889903 169 DEPTVGVDSKNVHQFYEMleMLNKKLGITLILVTH 203
Cdd:PRK14247 171 DEPTANLDPENTAKIESL--FLELKKDMTIVLVTH 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-205 |
3.07e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.45 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK----VGFVSQK 87
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:cd03218 84 ASIFRK---LTVEENILAVLE----IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLnKKLGITlILVT-HDV 205
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNV 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-208 |
3.19e-22 |
|
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: 91.45 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD---LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDW-QKVG 82
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnlRWLrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFNsgfpATVFEVVqsgltkKIGLFKFAGKEDKQKVKKAL--ESVDMLEYQ-NRNIGA----LSGGQQQRVFI 155
Cdd:cd03249 81 LVSQEPVLFD----GTIAENI------RYGKPDATDEEVEEAAKKANihDFIMSLPDGyDTLVGErgsqLSGGQKQRIAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEmlNKKLGITLILVTHDVGTV 208
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTI 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-203 |
7.91e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.79 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--RRFKDWQKVGFV 84
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANsFNSGFpaTVFEVVQSgLTKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPE 164
Cdd:PRK13537 86 PQFDN-LDPDF--TVRENLLV-FGRYFGL---SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-203 |
8.55e-22 |
|
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: 89.45 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGedirrfkdwqKVGF 83
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------SIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNsgfpATVFEVVqsgltkkigLFkfaGKE-DKQKVKKALES------VDMLEYQ-NRNIG----ALSGGQQQ 151
Cdd:cd03250 71 VSQEPWIQN----GTIRENI---------LF---GKPfDEERYEKVIKAcalepdLEILPDGdLTEIGekgiNLSGGQKQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEML---EMLNKKlgiTLILVTH 203
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilgLLLNNK---TRILVTH 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-204 |
1.12e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLklllglfklqkgKIeIFGE------DIRRFKDWqKVGFV 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL------------KI-LAGElepdsgEVSIPKGL-RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNSGfpaTVFEVVQSGLTKKIGLFK-------------------------FA---GKEDKQKVKKALESVDM-L 135
Cdd:COG0488 67 PQEPPLDDDL---TVLDTVLDGDAELRALEAeleeleaklaepdedlerlaelqeeFEalgGWEAEARAEEILSGLGFpE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 136 EYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDsknvhqfyemLEMLN------KKLGITLILVTHD 204
Cdd:COG0488 144 EDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEwleeflKNYPGTVLVVSHD 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-220 |
1.52e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 5 VNPIVKFEDISYKY---TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---W 78
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhylH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 QKVGFVSQKANSFNsgfpATVFEVVQSGLTkkiglfkFAGKEDKQKVKKALESVD----MLEYQNRNIGA----LSGGQQ 150
Cdd:TIGR00958 555 RQVALVGQEPVLFS----GSVRENIAYGLT-------DTPDEEIMAAAKAANAHDfimeFPNGYDTEVGEkgsqLSGGQK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEmlemLNKKLGITLILVTHDVGTVtDKVTHVACLNK 220
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTV-ERADQILVLKK 688
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-212 |
1.93e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIeIFG--------EDIR-RFKD----- 77
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplaearEDTRlMFQDarllp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQKVgfvsqkansfnsgfpatvFEVVQSGLTKKIglfkfagkedKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:PRK11247 95 WKKV------------------IDNVGLGLKGQW----------RDAALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG---TVTDKV 212
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeavAMADRV 204
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-220 |
2.45e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 13 DISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQKAN--- 89
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 ----------SFNSGFPATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEY-QNRNIGALSGGQQQRVFIARS 158
Cdd:PRK10619 90 lrtrltmvfqHFNLWSHMTVLENVMEAPIQVLGLSK---QEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-203 |
3.61e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKL-----LLGLFKLQKGKIEIFG-----EDIRRFKDWQKV 81
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGrniysPDVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANSFNSgfpATVFEVVQSGLtKKIGLFKfAGKEDKQKVKKALESVDML-EYQNR---NIGALSGGQQQRVFIAR 157
Cdd:PRK14267 88 GMVFQYPNPFPH---LTIYDNVAIGV-KLNGLVK-SKKELDERVEWALKKAALWdEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTH 203
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-212 |
5.28e-21 |
|
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: 91.28 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKST--------LLKLllglfklqkGKIEIFGEDIRRFKDWQ------KVGFVSQkaN 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglallrlIPSE---------GEIRFDGQDLDGLSRRAlrplrrRMQVVFQ--D 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSGFP-ATVFEVVQSGLT-KKIGLfkfAGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:COG4172 371 PFGSLSPrMTVGQIIAEGLRvHGPGL---SAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV---TDKV 212
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVralAHRV 496
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-212 |
5.67e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEdirRFKDW----QKVGFV 84
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVppaeRGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQkanSFnSGFP-ATVFEVVQSGLtkkiglfKFAG---KEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLV 160
Cdd:PRK11000 81 FQ---SY-ALYPhLSVAENMSFGL-------KLAGakkEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 161 SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD---VGTVTDKV 212
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDqveAMTLADKI 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-215 |
6.08e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.19 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYT-KDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQK-VG 82
Cdd:TIGR02857 320 SSLEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdaDSWRDqIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSfnsgFPATVFEvvqsgltkKIGLFKFAGKEDkqKVKKALESVDMLEY-------QNRNIG----ALSGGQQQ 151
Cdd:TIGR02857 400 WVPQHPFL----FAGTIAE--------NIRLARPDASDA--EIREALERAGLDEFvaalpqgLDTPIGeggaGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVT--DKVTHV 215
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAlaDRIVVL 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-201 |
6.85e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 4 VVNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfKDWQKVGF 83
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSGFPATVFEVVQSGLTkkIGLFkFAGKED-KQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLA--MGGF-FAERDQfQERIKWVYELFPRLhERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILV 201
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLV 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
2.25e-20 |
|
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: 86.62 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 17 KYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGED--IRRFKDWQKVGFV-SQK------ 87
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKKFLRRIGVVfGQKtqlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ---ANSFNsgfpatvfevvqsgLTKKI-GLFKFAGKEDKQKVKKALESVDMLEYQNRNigaLSGGQQQRVFIARSLVSEP 163
Cdd:cd03267 110 lpvIDSFY--------------LLAAIyDLPPARFKKRLDELSELLDLEELLDTPVRQ---LSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-203 |
2.48e-20 |
|
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: 85.06 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--QKVGFVSQ 86
Cdd:cd03247 3 INNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAlsSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNsgfpATVFEvvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrNIGA-LSGGQQQRVFIARSLVSEPEL 165
Cdd:cd03247 83 RPYLFD----TTLRN---------------------------------------NLGRrFSGGERQRLALARILLQDAPI 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 166 MILDEPTVGVDSKNVHQFYE-MLEMLNKKlgiTLILVTH 203
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSlIFEVLKDK---TLIWITH 155
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-211 |
2.97e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 3 NVVNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKST-----LLKLLLGLFKLQKGKI-----EIFGEDI 72
Cdd:PRK14243 5 NGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrcfNRLNDLIPGFRVEGKVtfhgkNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 73 RRFKDWQKVGFVSQKANSFnsgfPATVFEVVQSGltKKIGLFKfaGKEDkQKVKKALESV---DMLEYQNRNIG-ALSGG 148
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPF----PKSIYDNIAYG--ARINGYK--GDMD-ELVERSLRQAalwDEVKDKLKQSGlSLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTHDV---GTVTDK 211
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMqqaARVSDM 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-210 |
3.14e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 86.13 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRR--FKDW-QKVGFV 84
Cdd:cd03254 3 IEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisRKSLrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNSgfpaTVFEvvqsgltkKIGLFK-FAGKEDKQKVKKALESVDMLE--------YQNRNIGALSGGQQQRVFI 155
Cdd:cd03254 83 LQDTFLFSG----TIME--------NIRLGRpNATDEEVIEAAKEAGAHDFIMklpngydtVLGENGGNLSQGERQLLAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-220 |
3.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.11 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLE-----HVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR---RFKDW-- 78
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsKNKDIkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 --QKVGFVSQKANSfnSGFPATVFEVVQSGlTKKIGLfkfaGKEDKQKVkkALESVDML----EYQNRNIGALSGGQQQR 152
Cdd:PRK13649 83 irKKVGLVFQFPES--QLFEETVLKDVAFG-PQNFGV----SQEEAEAL--AREKLALVgiseSLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-208 |
4.06e-20 |
|
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: 86.00 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF-KDW--QKVGF 83
Cdd:cd03252 1 ITFEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWlrRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpaTVFEVVQSG-----LTKKIGLFKFAGKEDkqKVKKALESVDMLEYQNrniGA-LSGGQQQRVFIAR 157
Cdd:cd03252 81 VLQENVLFNR----SIRDNIALAdpgmsMERVIEAAKLAGAHD--FISELPEGYDTIVGEQ---GAgLSGGQRQRIAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFyeMLEMLNKKLGITLILVTHDVGTV 208
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAI--MRNMHDICAGRTVIIIAHRLSTV 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-203 |
4.79e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDIS---YKYTKDLV-LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--------RRFK 76
Cdd:PRK11153 2 IELKNISkvfPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsekelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 dwQKVGFVSQKANSFNSgfpATVFEVVQSGLtkkiglfKFAGK---EDKQKVKKALESVDMLEYQNRNIGALSGGQQQRV 153
Cdd:PRK11153 82 --RQIGMIFQHFNLLSS---RTVFDNVALPL-------ELAGTpkaEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-208 |
6.89e-20 |
|
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: 88.23 E-value: 6.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR--RFKDWQK-VGF 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRqVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpaTVFEVVQSGLTKKIglfkfagkeDKQKVKKALESVDMLEYQNR-----------NIGALSGGQQQR 152
Cdd:TIGR02203 411 VSQDVVLFND----TIANNIAYGRTEQA---------DRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQR 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTV 208
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI 531
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-220 |
7.28e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD-----LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFG---------EDIR 73
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 74 RFKdwQKVGFVSQKANSfnSGFPATVFEVVQSGlTKKIGLfkfaGKEDKQKVkkALESVDML----EYQNRNIGALSGGQ 149
Cdd:PRK13643 81 PVR--KKVGVVFQFPES--QLFEETVLKDVAFG-PQNFGI----PKEKAEKI--AAEKLEMVgladEFWEKSPFELSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 150 QQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-220 |
8.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL-----VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKD----- 77
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 -WQKVGFVSQkansfnsgFPATvfEVVQSGLTKKIglfKFAGKEDKQKVKKALESVDMLEYQ---NRNIGALS-----GG 148
Cdd:PRK13646 83 vRKRIGMVFQ--------FPES--QLFEDTVEREI---IFGPKNFKMNLDEVKNYAHRLLMDlgfSRDVMSQSpfqmsGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-216 |
1.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKYTKDL-----VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIeIFGE--------DIRRFKD 77
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipanlkKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQK-VGFVSQkansfnsgFPAtvFEVVQSGLTKKIGLFKFAGKEDKQKV-KKALESVDML----EYQNRNIGALSGGQQQ 151
Cdd:PRK13645 88 LRKeIGLVFQ--------FPE--YQLFQETIEKDIAFGPVNLGENKQEAyKKVPELLKLVqlpeDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVgtvtDKVTHVA 216
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNM----DQVLRIA 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-210 |
1.25e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.80 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI----------FGED---IRRFKdwQKVGFVSQkan 89
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQkglIRQLR--QHVGFVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSgFP-ATVFEVVQSG------------------LTKKIGLfkfAGKEDKqkvkkalesvdmleYQNRnigaLSGGQQ 150
Cdd:PRK11264 93 NFNL-FPhRTVLENIIEGpvivkgepkeeatarareLLAKVGL---AGKETS--------------YPRR----LSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHqfyemlEMLNKKLGI-----TLILVTHDVGTVTD 210
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVG------EVLNTIRQLaqekrTMVIVTHEMSFARD 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-215 |
1.26e-19 |
|
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: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfgedirrfKDWQKVGFVSQka 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------GSTVKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfnsgfpatvfevvqsgltkkiglfkfagkedkqkvkkalesvdmleyqnrnigaLSGGQQQRVFIARSLVSEPELMIL 168
Cdd:cd03221 71 --------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 169 DEPTVGVDSKNVHQFYEMLemlnKKLGITLILVTHD---VGTVTDKVTHV 215
Cdd:cd03221 95 DEPTNHLDLESIEALEEAL----KEYPGTVILVSHDryfLDQVATKIIEL 140
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-205 |
1.37e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKL---LLGLFKLQKGKIEIFGEDI-------RR----F 75
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAiagTLSPAFSASGEVLLNGRRLtalpaeqRRigilF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 76 KD---------WQKVGFvsqkansfnsGFPATVfevvqsgltkkiglfkfAGKEDKQKVKKALESVDMLEYQNRNIGALS 146
Cdd:COG4136 83 QDdllfphlsvGENLAF----------ALPPTI-----------------GRAQRRARVEQALEEAGLAGFADRDPATLS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 147 GGQQQRVFIARSLVSEPELMILDEPTVGVDS---KNVHQF-YEMLemlnKKLGITLILVTHDV 205
Cdd:COG4136 136 GGQRARVALLRALLAEPRALLLDEPFSKLDAalrAQFREFvFEQI----RQRGIPALLVTHDE 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-252 |
1.65e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNVVNPIVKF--EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfKDW 78
Cdd:PRK10575 2 QEYTNHSDTTFalRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL---ESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 QKVGFVSQKAnSFNSGFPA----TVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVF 154
Cdd:PRK10575 79 SSKAFARKVA-YLPQQLPAaegmTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTH-VACLNKKLHFHGDAceyNE 233
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYlVALRGGEMIAQGTP---AE 234
|
250 260
....*....|....*....|
gi 1025889903 234 LDEGE-LSSIYGHGVQFLNH 252
Cdd:PRK10575 235 LMRGEtLEQIYGIPMGILPH 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-243 |
2.48e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.33 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 16 YKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI------FGEDIRRF---KDWQKVGFVS 85
Cdd:PRK14246 17 YLYINDkAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDIFQIdaiKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QKANSFNSgfpATVFEVVQSGLtkkiglfKFAGKEDKQKVKKALESV--------DMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:PRK14246 97 QQPNPFPH---LSIYDNIAYPL-------KSHGIKEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlgITLILVTHDVGTVTDKVTHVACL-NKKLHFHGDACEYNELDE 236
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLyNGELVEWGSSNEIFTSPK 244
|
....*..
gi 1025889903 237 GELSSIY 243
Cdd:PRK14246 245 NELTEKY 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-205 |
2.53e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-------VGFVSQkanSFNSGF 95
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhVGFVFQ---SFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 PATVFEVVQ-SGLTKkiglfkfaGKEDKQKVKKALESVDMLEYQNR--NIGA-LSGGQQQRVFIARSLVSEPELMILDEP 171
Cdd:PRK10584 102 TLNALENVElPALLR--------GESSRQSRNGAKALLEQLGLGKRldHLPAqLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 172 TVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-213 |
4.35e-19 |
|
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: 81.32 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRrfkdwqkvgfvsqka 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 nsfnsgfPATVFEVVQSGltkkIGLFkfagkedkqkvkkalesvdmleYQnrnigaLSGGQQQRVFIARSLVSEPELMIL 168
Cdd:cd03216 66 -------FASPRDARRAG----IAMV----------------------YQ------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025889903 169 DEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrldEVFEIADRVT 153
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
9-218 |
4.44e-19 |
|
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: 82.60 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYtKDLVLEhVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQK 87
Cdd:TIGR01277 1 LALDKVRYEY-EHLPME-FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGLTKKIGLfkfaGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:TIGR01277 79 NNLFAH---LTVRQNIGLGLHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACL 218
Cdd:TIGR01277 152 LDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-208 |
4.81e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.40 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--------RRFKdwQKVGFVSQkaNSFNS-- 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelRPLR--RRMQMVFQ--DPYASln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 94 ---------GFPATVFEVVqsgltkkiglfkfAGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:COG4608 110 prmtvgdiiAEPLRIHGLA-------------SKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 164 ELMILDEPT----VGVDSknvhQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:COG4608 177 KLIVCDEPVsaldVSIQA----QVLNLLEDLQDELGLTYLFISHDLSVV 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
4.87e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.31 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNVVNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR------- 73
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 74 --RFKDWQKV-------GFVSQkanSFNSGFPATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGA 144
Cdd:COG4598 81 elVPADRRQLqrirtrlGMVFQ---SFNLWSHMTVLENVIEAPVHVLGRPK---AEAIERAEALLAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHqfyEMLEMLnKKL---GITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVG---EVLKVM-RDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQ 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-203 |
5.99e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 85.69 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-------RfkdwQ 79
Cdd:TIGR03375 464 IEFRNVSFAYPGQetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqidpadlR----R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQKANSFNsgfpATVFEVVQSGltkkiglfkfAGKEDKQKVKKALESVDMLEYQNRN-------IG----ALSGG 148
Cdd:TIGR03375 540 NIGYVPQDPRLFY----GTLRDNIALG----------APYADDEEILRAAELAGVTEFVRRHpdgldmqIGergrSLSGG 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTH 203
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTH 658
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-205 |
8.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK----VG 82
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGirklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKansfnsgfPATVF--EVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLV 160
Cdd:PRK13644 81 IVFQN--------PETQFvgRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 161 SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDV 205
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-203 |
1.18e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--RRFKDWQKVGFVSQ 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpaRARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANsFNSGFpatvfeVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK13536 122 FDN-LDLEF------TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-214 |
1.32e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKVG 82
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKansfnsgfPATVFEVVQSGLtkkigLFKFAGKEDKQKVKKALESVDMLEYQ----NRNIGALSGGQQQRVFIARS 158
Cdd:PRK10247 85 YCAQT--------PTLFGDTVYDNL-----IFPWQIRNQQPDPAIFLDDLERFALPdtilTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDvgtvTDKVTH 214
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD----KDEINH 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-204 |
1.61e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQkansfnsgfpatVFEV 102
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGR------------VFQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSG----LT------------KKIGLFKFAGKEDKQKVKKALESVDM-LEyqNR---NIGALSGGQQQrvfiARSLV-- 160
Cdd:COG1101 89 PMMGtapsMTieenlalayrrgKRRGLRRGLTKKRRELFRELLATLGLgLE--NRldtKVGLLSGGQRQ----ALSLLma 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 161 --SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:COG1101 163 tlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-226 |
1.93e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ------K 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFnsgFPATVFEVVQSGLtkkigLFKFAGKED-KQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSL 159
Cdd:PRK10908 81 IGMIFQDHHLL---MDRTVYDNVAIPL-----IIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNkKLGITLILVTHDVGTVTDKVTHVACLNKKlHFHG 226
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG-HLHG 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-203 |
2.37e-18 |
|
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: 80.78 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKD----LVLEHVSLEIPRGAFLAIVGPNGSGKST---LLKLLLGLFKLQKGKIEIFGEDIRRFKdWQK 80
Cdd:cd03234 3 VLPWWDVGLKAKNWnkyaRILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKPDQ-FQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 -VGFVSQKaNSFNSGFpaTVFE----VVQSGLTKKiglfkfagKEDKQKVKKAlESVDMLEYQNRNIG-----ALSGGQQ 150
Cdd:cd03234 82 cVAYVRQD-DILLPGL--TVREtltyTAILRLPRK--------SSDAIRKKRV-EDVLLRDLALTRIGgnlvkGISGGER 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:cd03234 150 RRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-203 |
4.16e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTK--DLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW---QK 80
Cdd:PRK11160 336 QVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalrQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNSgfpatvfevvqsglTKKIGLFKFAGKEDKQKVKKALESVDmLEY--QNRN-----IG----ALSGGQ 149
Cdd:PRK11160 416 ISVVSQRVHLFSA--------------TLRDNLLLAAPNASDEALIEVLQQVG-LEKllEDDKglnawLGeggrQLSGGE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 150 QQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLE--MLNKklgiTLILVTH 203
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAehAQNK----TVLMITH 532
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-203 |
5.33e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKYTKDL------VLEHVSLEIPRGAFLAIVGPNGSGKST--LLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVG 82
Cdd:cd03213 6 FRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRPLDKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKansfnsgfpatvfEVVQSGLTkkiglfkfagkedkqkVKKALesvdmleYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:cd03213 86 YVPQD-------------DILHPTLT----------------VRETL-------MFAAKLRGLSGGERKRVSIALELVSN 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSKNVHQfyeMLEMLNK--KLGITLILVTH 203
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQ---VMSLLRRlaDTGRTIICSIH 169
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-208 |
6.67e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI------RRFKDWQKV 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANSFNSgfpATVFEVVQSGLTKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVS 161
Cdd:PRK11831 87 SMLFQSGALFTD---MNVFDNVAYPLREHTQL---PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1025889903 162 EPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEV 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-205 |
1.01e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.55 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF----KDWQKVGFVSQK 87
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:PRK10895 87 ASIFRR---LSVYDNLMAVLQIRDDLSA---EQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDV 205
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNV 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-208 |
1.05e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGEDIRRFKDWQ------KVGFVSQKANS-FNSGF 95
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQllpvrhRIQVVFQDPNSsLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 paTVFEVVQSGLtkKIGLFKFAGKEDKQKVKKALESVDM-LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:PRK15134 380 --NVLQIIEEGL--RVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-203 |
1.15e-17 |
|
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: 78.79 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-------RfkdwQ 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldpadlR----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQKANSFNsgfpATVFEVVQSGltkkiglfkfAGKEDKQKVKKALESVDMLEYQNRN-------IG----ALSGG 148
Cdd:cd03245 79 NIGYVPQDVTLFY----GTLRDNITLG----------APLADDERILRAAELAGVTDFVNKHpngldlqIGergrGLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTH 203
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH 197
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-208 |
1.24e-17 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 79.49 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKI----------EIF--GEDIRR 74
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaelELYqlSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 75 F---KDWqkvGFVSQKAN-----SFNSGfpATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEyqnrniGALS 146
Cdd:TIGR02323 82 RlmrTEW---GFVHQNPRdglrmRVSAG--ANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLP------RAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 147 GGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVA 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-208 |
1.35e-17 |
|
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: 79.05 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTK---DLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD---WQKV 81
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkylHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQK--------ANSFNSGFPATVFEVVQSgLTKKIGLFKFAGKEDKQKVKKALESvdmleyqnrniGA-LSGGQQQR 152
Cdd:cd03248 91 SLVGQEpvlfarslQDNIAYGLQSCSFECVKE-AAQKAHAHSFISELASGYDTEVGEK-----------GSqLSGGQKQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTHDVGTV 208
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV 212
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-212 |
1.51e-17 |
|
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: 81.63 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfkdWQK------VGFVSQKANSFnsgfP 96
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ---WDRetfgkhIGYLPQDVELF----P 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEvvqsgltkkiGLFKFAGKEDKQKVKKALESVDMLEYQNR-------NIG----ALSGGQQQRVFIARSLVSEPEL 165
Cdd:TIGR01842 406 GTVAE----------NIARFGENADPEKIIEAAKLAGVHELILRlpdgydtVIGpggaTLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVG--TVTDKV 212
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSllGCVDKI 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-172 |
1.86e-17 |
|
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: 81.13 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfGEDIrrfkdwqKVGFVS 85
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 86 QKANSFNSGfpATVFEVVQSGL------TKKI------GLFKFAGkEDKQKvkkalesvdmleyqnrNIGALSGGQQQRV 153
Cdd:TIGR03719 392 QSRDALDPN--KTVWEEISGGLdiiklgKREIpsrayvGRFNFKG-SDQQK----------------KVGQLSGGERNRV 452
|
170
....*....|....*....
gi 1025889903 154 FIARSLVSEPELMILDEPT 172
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPT 471
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-204 |
1.91e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-----------RRfkdwQKVGFVSQK---- 87
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadalaqlRR----EHFGFIFQRyhll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ---ANSFNSGFPATvfevvqsgltkkiglfkFAGKEDKQKVKKALESV------DMLEYQNrniGALSGGQQQRVFIARS 158
Cdd:PRK10535 99 shlTAAQNVEVPAV-----------------YAGLERKQRLLRAQELLqrlgleDRVEYQP---SQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-212 |
2.04e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.14 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 25 EHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQKVG------FVSQKAnSFNsgfP 96
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkdDEWRAVRsdiqmiFQDPLA-SLN---P 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 -ATVFEVVQSGLtkKIGLFKFAGKEDKQKVKKALESVDMLEYQ-NRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:PRK15079 114 rMTIGEIIAEPL--RTYHPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV---TDKV 212
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVkhiSDRV 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-208 |
2.23e-17 |
|
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: 79.08 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGF------VSQKA-NSFNSgf 95
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdvqlVFQDSpSAVNP-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 PATVFEVVQSGLTKkigLFKFAGKEDKQKVKKALESVDM-LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:TIGR02769 104 RMTVRQIIGEPLRH---LTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLV 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-205 |
2.59e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfkdwqkVGFVSQKANSF 91
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--------EGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 92 -NSGF-P-ATVFEVVQSGLtkkiglfKFAGKEDKQKVKKA---LESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:PRK11248 77 qNEGLlPwRNVQDNVAFGL-------QLAGVEKMQRLEIAhqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-208 |
3.17e-17 |
|
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: 80.50 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKS----TLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQKV-----GFVSQKA-NS 90
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLseRELRRIrgnriAMIFQEPmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 91 FNsgfPA-TVFEVVQSGLTKKIGLfkfAGKEDKQKVKKALESVDMLEYQNRnIGA----LSGGQQQRVFIARSLVSEPEL 165
Cdd:COG4172 105 LN---PLhTIGKQIAEVLRLHRGL---SGAAARARALELLERVGIPDPERR-LDAyphqLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 166 MILDEPTVGVDsknV---HQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:COG4172 178 LIADEPTTALD---VtvqAQILDLLKDLQRELGMALLLITHDLGVV 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-206 |
3.31e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI------------FGEDIRR 74
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgqlrdlyaLSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 75 F---KDWqkvGFVSQKAN-----SFNSGfpATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEyqnrniGALS 146
Cdd:PRK11701 85 RllrTEW---GFVHQHPRdglrmQVSAG--GNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLP------TTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 147 GGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVG 206
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLA 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-236 |
3.46e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfKDWQKVGFVSQKANSFNSGFPATVFEVV 103
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR-RSRQVIELSEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 QSGLT-------------KKIGLFKFAGKEDK-QKVKKALESVDMLEYQ---NRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK10261 111 QEPMTslnpvftvgeqiaESIRLHQGASREEAmVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLnkklhFHGDACEYNELDE 236
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM-----YQGEAVETGSVEQ 255
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-205 |
3.99e-17 |
|
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: 77.51 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQkansfnSGFP-ATVFEV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNY------SLLPwLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VqsGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQ 182
Cdd:TIGR01184 75 I--ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|...
gi 1025889903 183 FYEMLEMLNKKLGITLILVTHDV 205
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDV 175
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-208 |
4.85e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGF------VSQKANS-FNSGF 95
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdiqmVFQDSISaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 paTVFEVVQSGLTKKIGLFKfagKEDKQKVKKALESVDM-LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:PRK10419 107 --TVREIIREPLRHLLSLDK---AERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-210 |
1.00e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 76.38 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDW-QKVGF 83
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIglHDLrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFnsgfpatvfevvqSG-LTKKIGLFkfaGKEDKQKVKKALESVDMLEYQNRNIGAL-----------SGGQQQ 151
Cdd:cd03244 83 IPQDPVLF-------------SGtIRSNLDPF---GEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQfyeMLEMLNKKL-GITLILVTHDVGTVTD 210
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDAL---IQKTIREAFkDCTVLTIAHRLDTIID 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-212 |
1.06e-16 |
|
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: 79.02 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY--TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRfkdWQK------ 80
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDReelgrh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKAnsfnSGFPATVFEVvqsgltkkIGLFkfaGKEDKQKVKKALESVDMLE--------YQNRnIGA----LSGG 148
Cdd:COG4618 408 IGYLPQDV----ELFDGTIAEN--------IARF---GDADPEKVVAAAKLAGVHEmilrlpdgYDTR-IGEggarLSGG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVG--TVTDKV 212
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSllAAVDKL 536
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-213 |
1.74e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGE--DIRRFKDWQK--VG 82
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTlmkilyglyqpdsGEILIDGKpvRIRSPRDAIAlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQkanSFnSGFPA-TVFEVVQSGLTKKIGLFKfagkeDKQKVKKALESVdMLEYQ-----NRNIGALSGGQQQRVFIA 156
Cdd:COG3845 84 MVHQ---HF-MLVPNlTVAENIVLGLEPTKGGRL-----DRKAARARIREL-SERYGldvdpDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 157 RSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHklrEVMAIADRVT 212
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-230 |
1.90e-16 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 75.87 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 26 HVSLEIPRGAFLAIVGPNGSGKSTLLKLLL----GLFKLQKGKIEIFGEDIRRFKDWQK-VGFVSQKansfnsgfPATVF 100
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILgllpPGLTQTSGEILLDGRPLLPLSIRGRhIATIMQN--------PRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 101 EVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDM--LEYQNRNIGA----LSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQARALILEALEAvgLPDPEEVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDACE 230
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDgRIVERGTVKE 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-213 |
2.28e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDIRRF--KDWQK--V 81
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTlmkilsgvyqpdsGEILLDGEPVRFRspRDAQAagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANSFNSgfpATV----F---EVVQSGLTKKiglfkfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVF 154
Cdd:COG1129 82 AIIHQELNLVPN---LSVaeniFlgrEPRRGGLIDW--------RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrldEVFEIADRVT 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-212 |
2.46e-16 |
|
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: 74.84 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD-WQKVGFVSQKANSfnsgfpatvfe 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGHAPG----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 102 vVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVH 181
Cdd:cd03231 84 -IKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|.
gi 1025889903 182 QFYEMLEMLNKKLGITLILVTHDVGTVTDKV 212
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGA 193
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-208 |
2.51e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY-TKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK---DWQKVGF 83
Cdd:PRK11176 342 IEFRNVTFTYpGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlasLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpaTVFEVVQSGLTKKiglFKFAGKEDKQKVKKALESVDMLEYQ-NRNIG----ALSGGQQQRVFIARS 158
Cdd:PRK11176 422 VSQNVHLFND----TIANNIAYARTEQ---YSREQIEEAARMAYAMDFINKMDNGlDTVIGengvLLSGGQRQRIAIARA 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTHDVGTV 208
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI 542
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-205 |
3.51e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYtkdlvlEHV----SLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK-VGF 83
Cdd:PRK10771 2 LKLTDITWLY------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKANSFNSgfpATVFEVVQSGLTKKIGLfkfaGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:PRK10771 76 LFQENNLFSH---LTVAQNIGLGLNPGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 164 ELMILDEPTVGVDSKNVHqfyEMLEMLN---KKLGITLILVTHDV 205
Cdd:PRK10771 149 PILLLDEPFSALDPALRQ---EMLTLVSqvcQERQLTLLMVSHSL 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-208 |
5.01e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 21 DLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKD-WQKVGFVSQKANSFNSGFpaTV 99
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPEL--SA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 100 FEVVQSgltkkigLFKFAGKEDKQkVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKN 179
Cdd:TIGR01189 91 LENLHF-------WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*....
gi 1025889903 180 VHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-230 |
5.56e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW---QKVGFV 84
Cdd:PRK10790 341 IDIDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNSGFPATVfevvqsGLTKKIglfkfagkeDKQKVKKALESVDMLEY--------------QNRNigaLSGGQQ 150
Cdd:PRK10790 421 QQDPVVLADTFLANV------TLGRDI---------SEEQVWQALETVQLAELarslpdglytplgeQGNN---LSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlgITLILVTHDVGTVTDKVTHVAclnkkLHfHGDACE 230
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILV-----LH-RGQAVE 554
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-216 |
6.44e-16 |
|
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: 75.92 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE---DIRRFKDW----QKVGFVSQKAnsfnSGFP-AT 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLppekRRIGYVFQEA----RLFPhLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 99 VFEVVQSGLTKKIGLFKFAGKEdkqKVKKALESVDMLEyqnRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSK 178
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFE---RVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025889903 179 NVHQFYEMLEMLNKKLGITLILVTHDVgtvtDKVTHVA 216
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSL----QEVLRLA 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
6.84e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.66 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 2 DNVVNPIVKFEDISYKYTKDLVLehvsleiprgaflAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI-------------- 67
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIY-------------FIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 68 ----FGEDIRRFKDWQK-VGFVSQkansfnsgFPAtvFEVVQSGLTKKIGL----FKFAGKEDKQKVKKALESVDMLE-Y 137
Cdd:PRK13631 100 itnpYSKKIKNFKELRRrVSMVFQ--------FPE--YQLFKDTIEKDIMFgpvaLGVKKSEAKKLAKFYLNKMGLDDsY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 138 QNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHqfyEMLEML--NKKLGITLILVTHDVGTVTDKVTHV 215
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH---EMMQLIldAKANNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|....*.
gi 1025889903 216 ACLNK-KLHFHGDACE 230
Cdd:PRK13631 247 IVMDKgKILKTGTPYE 262
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-210 |
9.62e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY-TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-------RfkdwQK 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvtraslR----RN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNSgfpaTVFEVVQSGLTKkiglfkfAGKEDKQKVKKALESVDMLEYQ----NRNIG----ALSGGQQQR 152
Cdd:PRK13657 411 IAVVFQDAGLFNR----SIEDNIRVGRPD-------ATDEEMRAAAERAQAHDFIERKpdgyDTVVGergrQLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN 535
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-212 |
1.09e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.32 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYT-KDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFG---EDIRRFKDWQKVGFV 84
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNsgfpATVFEVVQSGLTKKIglfkfagkeDKQKVKKALESVDM--------LEYQNR---NIGALSGGQQQRV 153
Cdd:TIGR01193 554 PQEPYIFS----GSILENLLLGAKENV---------SQDEIWAACEIAEIkddienmpLGYQTElseEGSSISGGQKQRI 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlgiTLILVTH--DVGTVTDKV 212
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHrlSVAKQSDKI 678
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-204 |
1.39e-15 |
|
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: 72.46 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISykytKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQK--VG 82
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRagIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSqkansfnsgfpatvfevvqsgltkkiglfkfagkEDKQKVKKALE-SVdmleYQNRNIGA-LSGGQQQRVFIARSLV 160
Cdd:cd03215 79 YVP----------------------------------EDRKREGLVLDlSV----AENIALSSlLSGGNQQKVVLARWLA 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025889903 161 SEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSE 163
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-210 |
1.89e-15 |
|
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: 72.83 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI--------RRfkdw 78
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstipledlRS---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 79 qKVGFVSQKansfnsgfpATVFevvqSGlTKKIGLFKFaGKEDKQKVKKALEsvdmLEYQNRNigaLSGGQQQRVFIARS 158
Cdd:cd03369 83 -SLTIIPQD---------PTLF----SG-TIRSNLDPF-DEYSDEEIYGALR----VSEGGLN---LSQGQRQLLCLARA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 159 LVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-216 |
2.14e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 72.85 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI---FGE------------DIRRfkdwQKVGFVSQk 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvdlaqaspreilALRR----RTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansFNSGFP-ATVFEVVQSGLTKkiglfkfAGKEDKQKVKKALEsvdMLEYQN--RNIGAL-----SGGQQQRVFIARSL 159
Cdd:COG4778 101 ---FLRVIPrVSALDVVAEPLLE-------RGVDREEARARARE---LLARLNlpERLWDLppatfSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHD---VGTVTDKVTHVA 216
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDeevREAVADRVVDVT 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-205 |
2.33e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 13 DISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfkDWQKVGFVS---QKAN 89
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL----DYSKRGLLAlrqQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSGFPATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILD 169
Cdd:PRK13638 82 VFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1025889903 170 EPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDV 205
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDI 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-206 |
2.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKG-----KIEIFGEDIRRFKD---- 77
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlef 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 WQKVGFVSQKANSFnsgfPATVFEVVQSGLTKKiglfKFAGKEDKQKVKKA-LESVDMLEYQNRNIG----ALSGGQQQR 152
Cdd:PRK14271 100 RRRVGMLFQRPNPF----PMSIMDNVLAGVRAH----KLVPRKEFRGVAQArLTEVGLWDAVKDRLSdspfRLSGGQQQL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLgiTLILVTHDVG 206
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLA 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-253 |
6.07e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGEDIRrfkDW------QKVGFVSQKANSfnsGFPATVF 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLS---DWsaaelaRHRAYLSQQQSP---PFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 101 EVVQSGLtkkiglfkfAGKEDKQKVKKALESV-------DMLeyqNRNIGALSGGQQQRVFIARSLV-------SEPELM 166
Cdd:COG4138 88 QYLALHQ---------PAGASSEAVEQLLAQLaealgleDKL---SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 167 ILDEPTVGVDsknVHQFYEMLEMLNK--KLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDACEYneLDEGELSSIY 243
Cdd:COG4138 156 LLDEPMNSLD---VAQQAALDRLLRElcQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEV--MTPENLSEVF 230
|
250
....*....|
gi 1025889903 244 GHGVQFLNHD 253
Cdd:COG4138 231 GVKFRRLEVE 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-208 |
7.41e-15 |
|
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: 72.83 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 21 DLVLEhVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDirrfkdWQ-------------KVGFVSQK 87
Cdd:COG4148 13 GFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV------LQdsargiflpphrrRIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 AnsfnSGFP-ATVFEVVQSGLtkkiglfKFAGKEDKQKvkkALES-VDMLEYQ---NRNIGALSGGQQQRVFIARSLVSE 162
Cdd:COG4148 86 A----RLFPhLSVRGNLLYGR-------KRAPRAERRI---SFDEvVELLGIGhllDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV 208
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEV 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-188 |
9.14e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVG----F 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCpriaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQkansfnsG-----FPA-TVFEVVQSgltkkIG-LFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIA 156
Cdd:NF033858 81 MPQ-------GlgknlYPTlSVFENLDF-----FGrLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190
....*....|....*....|....*....|....
gi 1025889903 157 RSLVSEPELMILDEPTVGVD--SKNvhQFYEMLE 188
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDplSRR--QFWELID 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-205 |
9.86e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.21 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQK----VGFVSQK 87
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSgfpATVFE----VVQsgltkkigLFKFAGKEDKQKVKKALESVDmLEYQNRNIG-ALSGGQQQRVFIARSLVSE 162
Cdd:COG1137 87 ASIFRK---LTVEDnilaVLE--------LRKLSKKEREERLEELLEEFG-ITHLRKSKAySLSGGERRRVEIARALATN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITlILVT-HDV 205
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIG-VLITdHNV 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-210 |
1.27e-14 |
|
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: 72.93 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIR-------RfkdwQK 80
Cdd:COG5265 358 VRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvtqaslR----AA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNsgfpATVFEVVQSGltkKIGlfkfAGKEDKQKVKKALESVDMLE-----YQNRnIG----ALSGGQQQ 151
Cdd:COG5265 434 IGIVPQDTVLFN----DTIAYNIAYG---RPD----ASEEEVEAAARAAQIHDFIEslpdgYDTR-VGerglKLSGGEKQ 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD 558
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-187 |
2.40e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.97 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLL-------GLFKLQKGKIEIFGEDIRRFKdwQ 79
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgySNDLTLFGRRRGSGETIWDIK--K 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSqkaNSFNSGF--PATVFEVVQSGLTKKIGLFKFAgkEDKQKvKKALESVDMLEYQNRNIGA----LSGGQQQRV 153
Cdd:PRK10938 337 HIGYVS---SSLHLDYrvSTSVRNVILSGFFDSIGIYQAV--SDRQQ-KLAQQWLDILGIDKRTADApfhsLSWGQQRLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKN---VHQFYEML 187
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNrqlVRRFVDVL 447
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-210 |
4.27e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkGKIEIFGEDI--RRFKDWQKVGFVS-QK---------ANSF 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmltgilvptsGEVRVLGYVPfkRRKEFARRIGVVFgQRsqlwwdlpaIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 92 NsgfpatvfevvqsgLTKKI-GLfkfagkeDKQKVKKALES-VDMLEYQN------RNigaLSGGQQQRVFIARSLVSEP 163
Cdd:COG4586 118 R--------------LLKAIyRI-------PDAEYKKRLDElVELLDLGElldtpvRQ---LSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 164 ELMILDEPTVGVD--SK-NVHQFyemLEMLNKKLGITLILVTHDVGTVTD 210
Cdd:COG4586 174 KILFLDEPTIGLDvvSKeAIREF---LKEYNRERGTTILLTSHDMDDIEA 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-203 |
9.95e-14 |
|
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: 70.22 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkgkiEIFGEDIRRFKDWQKVGFVSQKA 88
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYE----PTSGRIIYHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 89 ----NSFNSGFPATVFEV--------VQSGLTKKIGLF---KFA------------------GKEDKQKVKKALESVDML 135
Cdd:TIGR03269 77 kvgePCPVCGGTLEPEEVdfwnlsdkLRRRIRKRIAIMlqrTFAlygddtvldnvlealeeiGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 136 EYQNRNIGA---LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:TIGR03269 157 QLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-204 |
2.37e-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: 69.19 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLklllglfklqkgKI------EIFGEdiRRFKDWQKVGFVSQKANSFNSgfp 96
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RImagvdkDFNGE--ARPQPGIKVGYLPQEPQLDPT--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVVQSGLTKKIGLF--------KFAGKED-------KQ-KVKKALESVDMLEYQNR---------------NIGAL 145
Cdd:TIGR03719 83 KTVRENVEEGVAEIKDALdrfneisaKYAEPDAdfdklaaEQaELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 146 SGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVhqfyEMLEMLNKKLGITLILVTHD 204
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----AWLERHLQEYPGTVVAVTHD 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-203 |
2.42e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 21 DLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfkDWQKVGFVSQKANSFNSGFPA-TV 99
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEACHYLGHRNAMKPAlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 100 FEVVQsgltkkiglF--KFAGKEDKQkVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDS 177
Cdd:PRK13539 91 AENLE---------FwaAFLGGEELD-IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 1025889903 178 KNVHQFYE-MLEMLNKklGITLILVTH 203
Cdd:PRK13539 161 AAVALFAElIRAHLAQ--GGIVIAATH 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-204 |
3.04e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKdwqkvgfvsqkansfnsgfPA----- 97
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-------------------PAdrdia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 98 ------------TVFEVVQSGLtkKIGlfKFAGKEDKQKVKKA---LESVDMLEYQNRnigALSGGQQQRVFIARSLVSE 162
Cdd:PRK11650 80 mvfqnyalyphmSVRENMAYGL--KIR--GMPKAEIEERVAEAariLELEPLLDRKPR---ELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1025889903 163 PELMILDEPTVGVDSK-NVHQFYEMLEmLNKKLGITLILVTHD 204
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKlRVQMRLEIQR-LHRRLKTTSLYVTHD 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-216 |
3.32e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI----------RRfkdwQKVGFVSQkaNSFNS 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqklLR----QKIQIVFQ--NPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 94 GFPatvfevvqsglTKKIGLF---------KFAGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEP 163
Cdd:PRK11308 105 LNP-----------RKKVGQIleepllintSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 164 ELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTvtdkVTHVA 216
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSV----VEHIA 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
142-202 |
3.85e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 3.85e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD--SKnvHQFYEMLEMLNKKlGITLILVT 202
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAK--AEIYRLIRELAAE-GKAVIVIS 451
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-203 |
4.44e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 26 HVSLEIPRG---AFLaivGPNGSGKSTLLKLLLGLFKLQKGKIEIFGE-------DIRRfkdwqKVGFVSQkANSFNSgf 95
Cdd:NF033858 284 HVSFRIRRGeifGFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiATRR-----RVGYMSQ-AFSLYG-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 patvfEV-VQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:NF033858 353 -----ELtVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180
....*....|....*....|....*....
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:NF033858 428 VDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-210 |
5.56e-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: 67.91 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKY---TKDLV--LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI-FGED-------- 71
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 72 -IRRFKDWQKVGFVSQKANSFNSgfpATVFEvvqsGLTKKIGL---FKFAgkedKQKVKKALESVDMLEYQNRNI----- 142
Cdd:TIGR03269 357 pDGRGRAKRYIGILHQEYDLYPH---RTVLD----NLTEAIGLelpDELA----RMKAVITLKMVGFDEEKAEEIldkyp 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 143 GALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTD 210
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-172 |
8.39e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 3 NVVnpiVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfGEDIrrfkdwqKVG 82
Cdd:PRK11819 322 DKV---IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFNSGfpATVFEVVQSGL-TKKIG-----------LFKFAGKeDKQKvkkalesvdmleyqnrNIGALSGGQQ 150
Cdd:PRK11819 391 YVDQSRDALDPN--KTVWEEISGGLdIIKVGnreipsrayvgRFNFKGG-DQQK----------------KVGVLSGGER 451
|
170 180
....*....|....*....|..
gi 1025889903 151 QRVFIARSLVSEPELMILDEPT 172
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-214 |
9.75e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQ------KVGFVSQkaNSFNSGFP- 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrrDIQFIFQ--DPYASLDPr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 ATVFEVVQSGLtKKIGLFKfaGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGV 175
Cdd:PRK10261 418 QTVGDSIMEPL-RVHGLLP--GKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 176 DSKNVHQFYEMLEMLNKKLGITLILVTHDVGtVTDKVTH 214
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMA-VVERISH 532
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-218 |
1.04e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 19 TKDLVLEHvsLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRR--FKDWQKVgfVSQKANSFNSG-- 94
Cdd:PRK10938 16 TKTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsFEQLQKL--VSDEWQRNNTDml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 95 ------FPATVFEVVQSGLtkkiglfkfagkEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMIL 168
Cdd:PRK10938 92 spgeddTGRTTAEIIQDEV------------KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 169 DEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACL 218
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-212 |
1.11e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKV----GFV--SQKANSFNSGFP---- 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmAYIteSRRDNGFFPNFSiaqn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 -ATVFEVVQSGLTKKIGLFkfagkEDKQKVKKALESVDMLEYQ----NRNIGALSGGQQQRVFIARSLVSEPELMILDEP 171
Cdd:PRK09700 362 mAISRSLKDGGYKGAMGLF-----HEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025889903 172 TVGVDSKNVHQFYEMLEMLNKKlGITLILVTH---DVGTVTDKV 212
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSelpEIITVCDRI 479
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-215 |
1.20e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLF----KLQKGKIEIFGEDIRRFKDWQK-------VGFVSQKA-NSF 91
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERrnlvgaeVAMIFQDPmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 92 NSGFpaTV-FEV-----VQSGLTKK------IGLFKFAGKEDKQkvkkalESVDMLEYQnrnigaLSGGQQQRVFIARSL 159
Cdd:PRK11022 103 NPCY--TVgFQImeaikVHQGGNKKtrrqraIDLLNQVGIPDPA------SRLDVYPHQ------LSGGMSQRVMIAMAI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHV 215
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-203 |
1.25e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.14 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkgkieIF---------GE-DIRRFKDwQKVGFVSQKAnSFN 92
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKST-----------------LLraiaglwpyGSgRIARPAG-ARVLFLPQRP-YLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 93 SG-------FPATvfevvqsgltkkiglfkfAGKEDKQKVKKALESV------DMLEYQNR--NIgaLSGGQQQRVFIAR 157
Cdd:COG4178 439 LGtlreallYPAT------------------AEAFSDAELREALEAVglghlaERLDEEADwdQV--LSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEML-EMLnkkLGITLILVTH 203
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLrEEL---PGTTVISVGH 542
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
127-212 |
1.44e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 127 KALESVDMLEYQNRnIG----ALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVT 202
Cdd:PRK09473 141 RMLDAVKMPEARKR-MKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMIT 219
|
90
....*....|...
gi 1025889903 203 HDVGTVT---DKV 212
Cdd:PRK09473 220 HDLGVVAgicDKV 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-216 |
1.72e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.11 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDLVlEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGL----FKLQKGKIEIFGE-----DIRRfkdwQ 79
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKpvapcALRG----R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQKansfnsgfPATVFEVVQSGLTKKIGLFKFAGKE-DKQKVKKALESVDmLEYQNRNIGA----LSGGQQQRVF 154
Cdd:PRK10418 80 KIATIMQN--------PRSAFNPLHTMHTHARETCLALGKPaDDATLTAALEAVG-LENAARVLKLypfeMSGGMLQRMM 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVA 216
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVA 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-205 |
2.01e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISYKYTKDLVLEHV---------SLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK 76
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgvkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 DWQ-------KVGFVSQkanSFNSGFPATVFEVVQSGLTkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQ 149
Cdd:PRK10070 97 DAElrevrrkKIAMVFQ---SFALMPHMTVLDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 150 QQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDV 205
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDL 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-203 |
2.55e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 17 KYTKDLvLEHVSLEIPRGAFLAIVGPNGSGKST---LLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQkansFNS 93
Cdd:TIGR00955 35 RPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTlmnALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQ----DDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 94 GFPA-TVFE--VVQSGLTKKIGLFKfagKEDKQKVKKALESVDMLEYQNRNIGA------LSGGQQQRVFIARSLVSEPE 164
Cdd:TIGR00955 110 FIPTlTVREhlMFQAHLRMPRRVTK---KEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 165 LMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-212 |
5.36e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 22 LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDwqkvgfvsqkanSFNS-----GFP 96
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD------------EYHQdllylGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 A------TVFEVVQSgltkkigLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:PRK13538 83 PgiktelTALENLRF-------YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1025889903 171 PTVGVDSKNVHQFYEMLEMLNKKLGITlILVTH-DVGTVTDKV 212
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHqDLPVASDKV 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
142-204 |
7.85e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 7.85e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDsknVHQFYEMLEMLN--KKLGITLILVTHD 204
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGAKKEIYQLINqfKAEGLSIILVSSE 454
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-203 |
1.12e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLL--LGLFKLQKGKIEIFGEDIrrfKDWQkvgfVSQKAN-----SFNSgf 95
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI---LELS----PDERARagiflAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 PA-----TVFEVVQSGLTKKIGLfKFAGKEDKQKVKKALESVDM-LEYQNRNIGA-LSGGQQQRVFIARSLVSEPELMIL 168
Cdd:COG0396 86 PVeipgvSVSNFLRTALNARRGE-ELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 169 DEPTVGVD-------SKNVHqfyemlEMLNKKLGItlILVTH 203
Cdd:COG0396 165 DETDSGLDidalrivAEGVN------KLRSPDRGI--LIITH 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
145-232 |
1.54e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVTDKVTHVACLNkklhf 224
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ----- 231
|
....*...
gi 1025889903 225 HGDACEYN 232
Cdd:PRK15134 232 NGRCVEQN 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-203 |
1.80e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.71 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGEDIRR--FKDW-QKVGFVSQkaNSfnSGFPATVFEvv 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELREldPESWrKHLSWVGQ--NP--QLPHGTLRD-- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 qsgltkKIGLfkfaGKED--KQKVKKALESVDMLEY------------QNRNIGaLSGGQQQRVFIARSLVSEPELMILD 169
Cdd:PRK11174 442 ------NVLL----GNPDasDEQLQQALENAWVSEFlpllpqgldtpiGDQAAG-LSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190
....*....|....*....|....*....|....*
gi 1025889903 170 EPTVGVDSKNVHQfyeMLEMLNK-KLGITLILVTH 203
Cdd:PRK11174 511 EPTASLDAHSEQL---VMQALNAaSRRQTTLMVTH 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-203 |
1.90e-11 |
|
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: 60.63 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKY-TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEI-FGEDIRrfkdwqkvgFVSQ 86
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLL---------FLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KansfnSGFPATVFevvqsgltkkiglfkfagkedKQKVKKALESVdmleyqnrnigaLSGGQQQRVFIARSLVSEPELM 166
Cdd:cd03223 72 R-----PYLPLGTL---------------------REQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLemlnKKLGITLILVTH 203
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-205 |
2.92e-11 |
|
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: 61.66 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 28 SLEIPRGAF-----LAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDirrfkdwqkvgfVSQKANSFNSGFPATVFEV 102
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VqSGLTKKIGLFKFAgkedKQKVKKALESVDMLEyqnRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKN--- 179
Cdd:cd03237 82 L-SSITKDFYTHPYF----KTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlm 153
|
170 180
....*....|....*....|....*.
gi 1025889903 180 VHQFYEMLEMLNKKlgiTLILVTHDV 205
Cdd:cd03237 154 ASKVIRRFAENNEK---TAFVVEHDI 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-205 |
3.27e-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: 63.04 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEdirrfkdwqkVGFVSQKAnsfnsgfpatvfeVV 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------VAYVPQQA-------------WI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 QSGLTKKIGLFKFAGKEDK-QKVKKA---LESVDMLEYQNRN-IGA----LSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYyQQVLEAcalLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190
....*....|....*....|....*....|....*
gi 1025889903 175 VDSKNVHQFYEML----EMLNKKlgiTLILVTHDV 205
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpeGVLKNK---TRILVTHGI 822
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-208 |
3.46e-11 |
|
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: 61.12 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLlglfklqkgkieIFGEDIRRFkdwqkVGFVSQKANSFNSGFPATVFEVV 103
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDT------------IYAEGQRRY-----VESLSAYARQFLGQMDKPDVDSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 qSGLTKKIGL-FKFAGKEDKQKVKKALESVDM---------------------LEY--QNRNIGALSGGQQQRVFIARSL 159
Cdd:cd03270 74 -EGLSPAIAIdQKTTSRNPRSTVGTVTEIYDYlrllfarvgirerlgflvdvgLGYltLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 160 VSEPE--LMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTV 208
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTI 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
5.49e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 1 MDNVVNpivkfedISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRrfKD--- 77
Cdd:PRK13540 1 MLDVIE-------LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDlct 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 -WQKVGFVSQKA--NSFNSGFPATVFEVVQS----GLTKKIGLFKFAgkedkqkvkkalesvdmlEYQNRNIGALSGGQQ 150
Cdd:PRK13540 72 yQKQLCFVGHRSgiNPYLTLRENCLYDIHFSpgavGITELCRLFSLE------------------HLIDYPCGLLSSGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLiLVTH 203
Cdd:PRK13540 134 RQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVL-LTSH 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-199 |
7.56e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 7.56e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 138 QNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYE-MLEMLNKKLGITLI 199
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQlIAELAKKDKGIIII 447
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-210 |
7.87e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 15 SYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK--DWQ-KVGFVSQK---- 87
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRsRLAVVSQTpflf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ----ANSFNSGFPAtvfevvqsgltkkiglfkfAGKEDKQKVKKaLESV--DMLE----YQNRnIGA----LSGGQQQRV 153
Cdd:PRK10789 402 sdtvANNIALGRPD-------------------ATQQEIEHVAR-LASVhdDILRlpqgYDTE-VGErgvmLSGGQKQRI 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGITLILVTHDVGTVTD 210
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE 515
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-213 |
1.53e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 5 VNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQK-- 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhKLAAQlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNSgfpATVFEVVQSG--LTKKI-GLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:PRK09700 82 IGIIYQELSVIDE---LTVLENLYIGrhLTKKVcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHklaEIRRICDRYT 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-204 |
2.01e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLklllglfklqkgKI------EIFGEdiRRFKDWQKVGFVSQKansfnsgfP 96
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RImagvdkEFEGE--ARPAPGIKVGYLPQE--------P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 97 -----ATVFEVVQSGLTKKIGLF--------KFAGKED-------KQ-KVKKALESVDMLEYQNR--------------- 140
Cdd:PRK11819 80 qldpeKTVRENVEEGVAEVKAALdrfneiyaAYAEPDAdfdalaaEQgELQEIIDAADAWDLDSQleiamdalrcppwda 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 141 NIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVH---QFyemlemLNKKLGiTLILVTHD 204
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwleQF------LHDYPG-TVVAVTHD 219
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-203 |
2.04e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 59.20 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLL--GLFKLQKGKIEIFGEDIRRFKDWQKVG---FVSQKANSFNSGFPA 97
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARaglFLAFQYPEEIPGVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 98 TVFevVQSGLT--------KKIGLFKFAgkedkQKVKKALESVDM-LEYQNR--NIGaLSGGQQQRVFIARSLVSEPELM 166
Cdd:TIGR01978 95 LEF--LRSALNarrsargeEPLDLLDFE-----KLLKEKLALLDMdEEFLNRsvNEG-FSGGEKKRNEILQMALLEPKLA 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH 203
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITH 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
145-209 |
2.36e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.53 E-value: 2.36e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT 209
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESIS 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-212 |
2.59e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKS-TLLKLLLGLFKLQKGKIEIFGE--DIRRFKDWQKVGFVSQKANSFNSGFpatvfeVV 103
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKpvDIRNPAQAIRAGIAMVPEDRKRHGI------VP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 QSGLTKKIGL-----FKFAGKEDKQKVKKAL-ESVDMLEYQNRN----IGALSGGQQQRVFIARSLVSEPELMILDEPTV 173
Cdd:TIGR02633 353 ILGVGKNITLsvlksFCFKMRIDAAAELQIIgSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 174 GVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTV---TDKV 212
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVlglSDRV 473
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-204 |
2.79e-10 |
|
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: 58.39 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 38 AIVGPNGSGKSTLlklllglfklqkgkIE-----IFGEDIRRfkdwqkvgfvsqkaNSFNSGFPATVFEvvqsglTKKIG 112
Cdd:cd03240 26 LIVGQNGAGKTTI--------------IEalkyaLTGELPPN--------------SKGGAHDPKLIRE------GEVRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 113 LFKFAGKEDKQKVKKALESVDMLEY-----QN-------RNIGALSGGQQQ------RVFIARSLVSEPELMILDEPTVG 174
Cdd:cd03240 72 QVKLAFENANGKKYTITRSLAILENvifchQGesnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|.
gi 1025889903 175 VDSKNV-HQFYEMLEMLNKKLGITLILVTHD 204
Cdd:cd03240 152 LDEENIeESLAEIIEERKSQKNFQLIVITHD 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-203 |
2.90e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTllklllglfklqkgkieIFGEDIRRFKDWQKVGFVSQKANSFNSGFPatvfeV 102
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKST-----------------LLRLLAGALKGTPVAGCVDVPDNQFGREAS-----L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSgltkkiglfkFAGKEDKQKVKKALESVDMLEYQN--RNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD---- 176
Cdd:COG2401 103 IDA----------IGRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqta 172
|
170 180 190
....*....|....*....|....*....|
gi 1025889903 177 ---SKNVHQfyemlemLNKKLGITLILVTH 203
Cdd:COG2401 173 krvARNLQK-------LARRAGITLVVATH 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-203 |
3.02e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLL--GLFKLQKGKIEIFGEDIRRfKDWQKVGFVSQK 87
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTK-QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfNSGFP-ATVFE-VVQSGLTKkigLFKFAGKEDKQKVKKALES-VDMLEYQNRNIG-----ALSGGQQQRVFIARSL 159
Cdd:PLN03211 149 ----DILYPhLTVREtLVFCSLLR---LPKSLTKQEKILVAESVISeLGLTKCENTIIGnsfirGISGGERKRVSIAHEM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
142-201 |
3.92e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 3.92e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDsknVHQFYEMLEMLNK--KLGITLILV 201
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID---VGAKYEIYKLINQlvQQGVAIIVI 461
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-212 |
4.46e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 27 VSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRrFKDW----QKVGFVSQK-ANSFNSgfPATVFE 101
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYsyrsQRIRMIFQDpSTSLNP--RQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 102 VVQSGLTKKIGLfkfAGKEDKQKVKKALESVDML-EYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNV 180
Cdd:PRK15112 109 ILDFPLRLNTDL---EPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190
....*....|....*....|....*....|....*
gi 1025889903 181 HQFYEMLEMLNKKLGITLILVTHDVGT---VTDKV 212
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMmkhISDQV 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-203 |
5.49e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDISYKY-TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLlklllglfklqkgkIEIFGE-----DIRRFKDW-QK 80
Cdd:TIGR00954 451 GIKFENIPLVTpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL--------------FRILGElwpvyGGRLTKPAkGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNSGF------PATVFEVVQSGLTkkiglfkfagkedKQKVKKALESVDMLEYQNRNIG---------AL 145
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLrdqiiyPDSSEDMKRRGLS-------------DKDLEQILDNVQLTHILEREGGwsavqdwmdVL 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 146 SGGQQQRVFIARSLVSEPELMILDEPTVGVdSKNVHQF-YEMLemlnKKLGITLILVTH 203
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAV-SVDVEGYmYRLC----REFGITLFSVSH 637
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-203 |
5.53e-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: 57.73 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKI-------EIFGEDIRRFKDWQK 80
Cdd:cd03290 1 VQVTNGYFSWGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 VGFVSQKANSFNsgfpATVFEVVqsgltkkiglfKFAGKEDKQKVKKALES------VDMLEYQNRN-IGA----LSGGQ 149
Cdd:cd03290 81 VAYAAQKPWLLN----ATVEENI-----------TFGSPFNKQRYKAVTDAcslqpdIDLLPFGDQTeIGErginLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 150 QQRVFIARSLVSEPELMILDEPTVGVD---SKNVHQfYEMLEML--NKKlgiTLILVTH 203
Cdd:cd03290 146 RQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ-EGILKFLqdDKR---TLVLVTH 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-204 |
7.54e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKL--------LLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQKANSFNSG 94
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdltggGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 95 FPATVFEVVQSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSL---------VSEPEL 165
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHD 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
38-212 |
1.18e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 38 AIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFG----EDIRRFKDWQ---KVGFVSQKANSFN------SGFPATVF---- 100
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKnehtNDMTNEQDYQgdeEQNVGMKNVNEFSltkeggSGEDSTVFknsg 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 101 EVVQSGL-----------------TKKIGLFKFA-------GKED--KQKVKKALESVDMLEY-------QNRNIG---- 143
Cdd:PTZ00265 1278 KILLDGVdicdynlkdlrnlfsivSQEPMLFNMSiyenikfGKEDatREDVKRACKFAAIDEFieslpnkYDTNVGpygk 1357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 144 ALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTV--TDKV 212
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIkrSDKI 1428
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-205 |
1.22e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYtKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEifgEDIRrfkdwqkvgfVSQ 86
Cdd:COG1245 340 TLVEYPDLTKSY-GGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK----------ISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSGFPATVFEVVQSGLTKKIGLFKFagkedKQKVKKALESVDMLEyqnRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:COG1245 406 KPQYISPDYDGTVEEFLRSANTDDFGSSYY-----KTEIIKPLGLEKLLD---KNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 167 ILDEPTVGVDsknVHQFYEMLEMLNK---KLGITLILVTHDV 205
Cdd:COG1245 478 LLDEPSAHLD---VEQRLAVAKAIRRfaeNRGKTAMVVDHDI 516
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-253 |
1.88e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGEDIRrfkDWQKV------GFVSQKANSfnsGFPA 97
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLE---AWSAAelarhrAYLSQQQTP---PFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 98 TVFEVVQsgltkkigLFKFAGKeDKQKVKKALESV-DMLEYQN---RNIGALSGGQQQRVFIA-------RSLVSEPELM 166
Cdd:PRK03695 85 PVFQYLT--------LHQPDKT-RTEAVASALNEVaEALGLDDklgRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDVGTVTDKVTHVACLNK-KLHFHGDACEYneLDEGELSSIYGH 245
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQgKLLASGRRDEV--LTPENLAQVFGV 232
|
....*...
gi 1025889903 246 GVQFLNHD 253
Cdd:PRK03695 233 NFRRLDVE 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-203 |
1.98e-09 |
|
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: 55.61 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 10 KFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLL--LGLFKLQKGKIEIFGEDIRRfkdwqkvgfvsqk 87
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfnsgfpATVFEVVQSGLTkkiglFKFAGKEDKQKVKKAlesvDMLEYQNRNigaLSGGQQQRVFIARSLVSEPELMI 167
Cdd:cd03217 69 ---------LPPEERARLGIF-----LAFQYPPEIPGVKNA----DFLRYVNEG---FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 1025889903 168 LDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH 162
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
145-203 |
2.48e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 2.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTH 203
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSH 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-203 |
3.62e-09 |
|
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: 56.95 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 38 AIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDW--QKVGFVSQKANSFNSgfpATVFEVVqsgltkkigLFk 115
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrQSLGMCPQHNILFHH---LTVAEHI---------LF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 116 FAGKEDKQKVKKALESVDMLE----YQNRNIGA--LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLem 189
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEdtglHHKRNEEAqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-- 1104
|
170
....*....|....
gi 1025889903 190 LNKKLGITLILVTH 203
Cdd:TIGR01257 1105 LKYRSGRTIIMSTH 1118
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
142-204 |
7.07e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 7.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSD 462
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
139-205 |
1.06e-08 |
|
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: 53.10 E-value: 1.06e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 139 NRNIGALSGGQQQRVFIARSLVSEPE--LMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHDV 205
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNL 149
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-172 |
1.28e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYtKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfgeDIRrfkdwqkvgfVSQ 86
Cdd:PRK13409 339 TLVEYPDLTKKL-GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK----------ISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSGFPATVFEVVqSGLTKKIGLFKFagkedKQKVKKALESVDMLEyqnRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK13409 405 KPQYIKPDYDGTVEDLL-RSITDDLGSSYY-----KSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACLSRDADLY 475
|
....*.
gi 1025889903 167 ILDEPT 172
Cdd:PRK13409 476 LLDEPS 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-204 |
1.74e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfkdwqkvgfVSQKAN 89
Cdd:PRK10522 325 LRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-----------TAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFNSGFPAtVFEVVQsgltkkigLF-KFAGKE----DKQKVKKALESVDM---LEYQNRNIG--ALSGGQQQRVFIARSL 159
Cdd:PRK10522 394 DYRKLFSA-VFTDFH--------LFdQLLGPEgkpaNPALVEKWLERLKMahkLELEDGRISnlKLSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025889903 160 VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHD 204
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-226 |
1.77e-08 |
|
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: 53.31 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFkdwqkvgfvsqkanSFNSGFpatvfev 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL--------------GLGGGF------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 vQSGLT-----KKIGLFK-FAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:cd03220 96 -NPELTgreniYLNGRLLgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 177 SKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK-KLHFHG 226
Cdd:cd03220 175 AAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKgKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-203 |
2.43e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFK--DWQKVG-- 82
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpaKAHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 83 FVSQKANSFNSgfpATVFEVVQSGLTKKiglfkfagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSE 162
Cdd:PRK15439 90 LVPQEPLLFPN---LSVKENILFGLPKR--------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1025889903 163 PELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISH 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-176 |
2.86e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTK--DLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrrfkdwQKVGFvsq 86
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI------AKIGL--- 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 kansFNSGFPATVF---EVVQSGlTKKIGLFKFAGKEDkQKVKKALESV----------DMLEYQNRNIGA-LSGGQQQR 152
Cdd:TIGR00957 1356 ----HDLRFKITIIpqdPVLFSG-SLRMNLDPFSQYSD-EEVWWALELAhlktfvsalpDKLDHECAEGGEnLSVGQRQL 1429
|
170 180
....*....|....*....|....
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVD 176
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD 1453
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-205 |
2.87e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 19 TKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKlqkgKIEIFGEDIRrfkdwQKVGFVSQKANSFNsgfpAT 98
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS----HAETSSVVIR-----GSVAYVPQVSWIFN----AT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 99 VFEVVQsgltkkiglfkFAGKEDKQKVKKALESV------------DMLEYQNRNIGaLSGGQQQRVFIARSLVSEPELM 166
Cdd:PLN03232 695 VRENIL-----------FGSDFESERYWRAIDVTalqhdldllpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190
....*....|....*....|....*....|....*....
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLeMLNKKLGITLILVTHDV 205
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSC-MKDELKGKTRVLVTNQL 800
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-176 |
3.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQKV-GF 83
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKVlGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQKAnsfnsgfpatvfeVVQSGlTKKIGLFKFAGKEDKQkVKKALESVDMLEYQNRNIGAL-----------SGGQQQR 152
Cdd:PLN03130 1318 IPQAP-------------VLFSG-TVRFNLDPFNEHNDAD-LWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQL 1382
|
170 180
....*....|....*....|....
gi 1025889903 153 VFIARSLVSEPELMILDEPTVGVD 176
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
145-217 |
3.24e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 3.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLILVTHDVGTVT---DKVTHVAC 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqwaDKINVLYC 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-204 |
3.51e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIeIFGEDIrrfkdwqKVGFVSQKANSFNSGfpaTVFEVV 103
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDL-------IVARLQQDPPRNVEG---TVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 QSGLTKKIGLFK-------FAGKEDKQKVKKALESV-DMLEYQN--------------------RNIGALSGGQQQRVFI 155
Cdd:PRK11147 88 AEGIEEQAEYLKryhdishLVETDPSEKNLNELAKLqEQLDHHNlwqlenrinevlaqlgldpdAALSSLSGGWLRKAAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 156 ARSLVSEPELMILDEPTVGVDSKNVhqfyEMLEMLNKKLGITLILVTHD 204
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETI----EWLEGFLKTFQGSIIFISHD 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
142-212 |
6.83e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 6.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD---VGTVTDKV 212
Cdd:PRK11288 394 IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlpeVLGVADRI 466
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-49 |
1.11e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.24 E-value: 1.11e-07
10 20
....*....|....*....|....*..
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKST 49
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKST 67
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-208 |
1.13e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYT--KDL-VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfgEDIRRFKD-----WQ- 79
Cdd:PTZ00265 383 IQFKNVRFHYDtrKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDinlkwWRs 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 80 KVGFVSQK----ANSFNSGFPATVFEVVQ-SGLTKKIGLFKFAGKEDKQK--------------------------VKKA 128
Cdd:PTZ00265 461 KIGVVSQDpllfSNSIKNNIKYSLYSLKDlEALSNYYNEDGNDSQENKNKrnscrakcagdlndmsnttdsnelieMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 129 LESVDMLEYQN-----------------------RNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYE 185
Cdd:PTZ00265 541 YQTIKDSEVVDvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|...
gi 1025889903 186 MLEMLNKKLGITLILVTHDVGTV 208
Cdd:PTZ00265 621 TINNLKGNENRITIIIAHRLSTI 643
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-231 |
1.22e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 5 VNPIVKF-------------EDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEifged 71
Cdd:PRK15064 303 QNPFIRFeqdkklhrnalevENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 72 irrfkdWQ---KVGFVSQ-KANSFNSGFpaTVFE-------------VVQSGLtkkiGLFKFAGKEDKQKVKkalesvdm 134
Cdd:PRK15064 378 ------WSenaNIGYYAQdHAYDFENDL--TLFDwmsqwrqegddeqAVRGTL----GRLLFSQDDIKKSVK-------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 135 leyqnrnigALSGGQQQRVFIARSLVSEPELMILDEPTvgvdskNvHQFYEMLEMLN---KKLGITLILVTHDVGTVTDK 211
Cdd:PRK15064 438 ---------VLSGGEKGRMLFGKLMMQKPNVLVMDEPT------N-HMDMESIESLNmalEKYEGTLIFVSHDREFVSSL 501
|
250 260
....*....|....*....|..
gi 1025889903 212 VTHVACL--NKKLHFHGDACEY 231
Cdd:PRK15064 502 ATRIIEItpDGVVDFSGTYEEY 523
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-203 |
1.29e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLG--LFKLQKGKIEIFGEDIRRFKDWQK---- 80
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERahlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 81 --VGF--------VSqkansfNSGFPATVFEVVQsgltKKIGLFKFAGKEDKQKVKKALESVDMLE-YQNRNIG-ALSGG 148
Cdd:CHL00131 86 ifLAFqypieipgVS------NADFLRLAYNSKR----KFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNeGFSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEPTVGVD-------SKNVHQFyemlemLNKKLGItlILVTH 203
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDidalkiiAEGINKL------MTSENSI--ILITH 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
142-199 |
1.29e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 142 IGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD---SKNVHQfyEMLEMLNKKLGITLI 199
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaIEFIHQ--RLLELRDAGAAVLLI 458
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
143-176 |
1.68e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.68e-07
10 20 30
....*....|....*....|....*....|....
gi 1025889903 143 GALSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-220 |
2.20e-07 |
|
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: 51.55 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 8 IVKFEDIS--YKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI-RRFKD-WQKVGF 83
Cdd:TIGR01257 1937 ILRLNELTkvYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDvHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 VSQkansfnsgfpatvFEVVQSGLTKKIGLFKFA------GKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIAR 157
Cdd:TIGR01257 2017 CPQ-------------FDAIDDLLTGREHLYLYArlrgvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 158 SLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHDVGTVTDKVTHVACLNK 220
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-204 |
2.28e-07 |
|
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: 51.55 E-value: 2.28e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 135 LEYQN--RNIGALSGGQQQRVFIARSLVSEPE--LMILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHD 204
Cdd:TIGR00630 477 LDYLSlsRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD 549
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-213 |
3.10e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKY-TKDLVlEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKG------KIEIFGEDIRRFK-DWQKvgf 83
Cdd:PRK11147 323 ENVNYQIdGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtKLEVAYFDQHRAElDPEK--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 84 vsqkansfnsgfpaTVF--------EVVQSGLTKKIgL-----FKFAGKEDKQKVKkalesvdmleyqnrnigALSGGQQ 150
Cdd:PRK11147 399 --------------TVMdnlaegkqEVMVNGRPRHV-LgylqdFLFHPKRAMTPVK-----------------ALSGGER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 151 QRVFIARSLVSEPELMILDEPTVGVDsknvhqfYEMLEMLNKKL----GiTLILVTHDVGTVTDKVT 213
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLD-------VETLELLEELLdsyqG-TVLLVSHDRQFVDNTVT 505
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-203 |
3.22e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFKDWQKVGFVSQ 86
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 kansfnsgFPATVFEVvqSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELM 166
Cdd:PRK13543 90 --------LPGLKADL--STLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1025889903 167 ILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLiLVTH 203
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISAHLRGGGAAL-VTTH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-231 |
3.69e-07 |
|
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: 50.68 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGedirrfkdwqKVGFVSQkansFNSGFPATVFEV 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQ----TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSGLTKKigLFKFagkedkQKVKKA--LESvDMLEYQNRN---IG----ALSGGQQQRVFIARSLVSEPELMILDEPTV 173
Cdd:TIGR01271 507 IIFGLSYD--EYRY------TSVIKAcqLEE-DIALFPEKDktvLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 174 GVDSKNVHQFYE--MLEMLNKKlgiTLILvthdvgtVTDKVTHVACLNKKLHFHGDACEY 231
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMSNK---TRIL-------VTSKLEHLKKADKILLLHEGVCYF 627
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-202 |
4.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGK-STLLKLLLGLFKLQKGKIEIFGedirrfkdwqKVGFVSQKANSFNsgfpATVFEV 102
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG----------TVAYVPQVSWIFN----ATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSGLTkkiglFKFAGKE---DKQKVKKALESV---DMLEYQNRNIGaLSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:PLN03130 699 ILFGSP-----FDPERYEraiDVTALQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180
....*....|....*....|....*...
gi 1025889903 177 SKNVHQFYE--MLEMLNKKlgiTLILVT 202
Cdd:PLN03130 773 AHVGRQVFDkcIKDELRGK---TRVLVT 797
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-204 |
5.88e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 5.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 139 NRNIGALSGGQQQRVFIARSLVSepELM----ILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD 537
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
139-199 |
6.27e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.41 E-value: 6.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 139 NRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKLGITLI 199
Cdd:cd03233 113 NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-213 |
6.87e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLklllglfklqkgKI------------EI-FGEDIRRFK---DWQKVGFV--- 84
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLM------------KVlsgvyphgsyegEIlFDGEVCRFKdirDSEALGIViih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 ---------SQKANSF------NSGF---PATVFEVVQsgLTKKIGLfkfagKEDKQ-KVKkalesvdmleyqnrNIGAl 145
Cdd:NF040905 85 qelalipylSIAENIFlgneraKRGVidwNETNRRARE--LLAKVGL-----DESPDtLVT--------------DIGV- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025889903 146 sgGQQQRVFIARSLVSEPELMILDEPTVGV---DSKNVHQFyeMLEMlnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:NF040905 143 --GKQQLVEIAKALSKDVKLLILDEPTAALneeDSAALLDL--LLEL--KAQGITSIIISHklnEIRRVADSIT 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-176 |
7.50e-07 |
|
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: 49.91 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 12 EDISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGE--DIRRFKDWQKV-GFVSQ 86
Cdd:TIGR01271 1221 QGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVswNSVTLQTWRKAfGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSGFpatvfevvqsgltkKIGLFKFAGKEDKQKVKKA----LESV-----DMLEYQNRNIG-ALSGGQQQRVFIA 156
Cdd:TIGR01271 1300 KVFIFSGTF--------------RKNLDPYEQWSDEEIWKVAeevgLKSVieqfpDKLDFVLVDGGyVLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|
gi 1025889903 157 RSLVSEPELMILDEPTVGVD 176
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD 1385
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-213 |
7.95e-07 |
|
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: 49.44 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLF--KLQKGKIEIFGEDI--RRFKDWQKVGFV--SQKANSFNSgfpA 97
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLkaSNIRDTERAGIViiHQELTLVPE---L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 98 TVFEVVQSG--LTKKIGLFKFAgkEDKQKVKKALESVDMLEYQN-RNIGALSGGQQQRVFIARSLVSEPELMILDEPTVG 174
Cdd:TIGR02633 94 SVAENIFLGneITLPGGRMAYN--AMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025889903 175 VDSKNVHQFYEMLEMLNKKlGITLILVTH---DVGTVTDKVT 213
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAH-GVACVYISHklnEVKAVCDTIC 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-203 |
1.44e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 119 KEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITL 198
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATV 197
|
....*
gi 1025889903 199 ILVTH 203
Cdd:NF000106 198 LLTTQ 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-208 |
1.60e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 1.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 140 RNIGALSGGQQQRVFIARSL---VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNkKLGITLILVTHDVGTV 208
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMHVV 875
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-236 |
1.68e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYT---------KDL-----------VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIF 68
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklKDLffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 69 GEdirrfkdwQKVGFVSQKANSFNSGFPATVFEVVQSGLTKkiglfkfagKEDKQKVKKALESVDMLEYQNRNIGALSGG 148
Cdd:PRK13545 85 GS--------AALIAISSGLNGQLTGIENIELKGLMMGLTK---------EKIKEIIPEIIEFADIGKFIYQPVKTYSSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 149 QQQRVFIARSLVSEPELMILDEP-TVGVDSKNVHQFYEMLEMlnKKLGITLILVTHDVGTVTDKVThvaclnKKLHFH-G 226
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEAlSVGDQTFTKKCLDKMNEF--KEQGKTIFFISHSLSQVKSFCT------KALWLHyG 219
|
250
....*....|
gi 1025889903 227 DACEYNELDE 236
Cdd:PRK13545 220 QVKEYGDIKE 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-231 |
1.80e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGkiEIFGEdirrfkdwQKVGFVSQKANSFNsgfpATVFev 102
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--RVWAE--------RSIAYVPQQAWIMN----ATVR-- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 vqsgltkkiGLFKFAGKEDKQKVKKALEsVDMLEYQNRNIGA------------LSGGQQQRVFIARSLVSEPELMILDE 170
Cdd:PTZ00243 739 ---------GNILFFDEEDAARLADAVR-VSQLEADLAQLGGgleteigekgvnLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 171 PTVGVDSKNVHQFYEMLeMLNKKLGITLILVTHDVGTV--TDKVthVACLNKKLHFHGDACEY 231
Cdd:PTZ00243 809 PLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVprADYV--VALGDGRVEFSGSSADF 868
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-229 |
1.89e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGedirrfkdwqKVGFVSQkansFNSGFPATVFEV 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQ----FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 103 VQSGLTkkiglfkFAGKEDKQKVKKALESVDMLEYQNRN---IG----ALSGGQQQRVFIARSLVSEPELMILDEPTVGV 175
Cdd:cd03291 118 IIFGVS-------YDEYRYKSVVKACQLEEDITKFPEKDntvLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 176 DSKNVHQFYEMLE---MLNKklgiTLILvthdvgtVTDKVTHVACLNKKLHFHGDAC 229
Cdd:cd03291 191 DVFTEKEIFESCVcklMANK----TRIL-------VTSKMEHLKKADKILILHEGSS 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-204 |
2.03e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 2 DNVVNPIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIfGEDIrrfkdwqKV 81
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI-------KL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 82 GFVSQKANSFnsgfpatvFEVVQSGLTKkigLFKFAGKEDKQKVKKALESVDMLEYQ-NRNIGALSGGQQQRVFIARSLV 160
Cdd:PRK10636 378 GYFAQHQLEF--------LRADESPLQH---LARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025889903 161 SEPELMILDEPTVGVDsknvhqfYEMLEMLNKKL----GiTLILVTHD 204
Cdd:PRK10636 447 QRPNLLLLDEPTNHLD-------LDMRQALTEALidfeG-ALVVVSHD 486
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-210 |
2.27e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRF--KDWQKVGFV 84
Cdd:PLN03232 1235 IKFEDVHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFglTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 85 SQKANSFNSGfpatvfevvqsglTKKIGLFKFAGKEDKQkVKKALESVDMLEYQNRNIGAL-----------SGGQQQRV 153
Cdd:PLN03232 1315 IPQSPVLFSG-------------TVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLL 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 154 FIARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlgITLILVTHDVGTVTD 210
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID 1435
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-213 |
2.31e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGL--FKLQKGKIEIFGEDIR--RFKDWQKVGFV------------SQK 87
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQasNIRDTERAGIAiihqelalvkelSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSF--NsgfpatvfEVVQSGLTKKIGLFkfagkedkQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPEL 165
Cdd:PRK13549 101 ENIFlgN--------EITPGGIMDYDAMY--------LRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTH---DVGTVTDKVT 213
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHklnEVKAISDTIC 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-176 |
4.19e-06 |
|
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: 46.77 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 13 DISYKYTKD--LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQkGKIEIFGE--DIRRFKDWQKV-GFVSQK 87
Cdd:cd03289 7 DLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVswNSVPLQKWRKAfGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ANSFNSGFPATVfevVQSGLTKKIGLFKFAgkeDKQKVKKALESV-DMLEYQNRNIG-ALSGGQQQRVFIARSLVSEPEL 165
Cdd:cd03289 86 VFIFSGTFRKNL---DPYGKWSDEEIWKVA---EEVGLKSVIEQFpGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKI 159
|
170
....*....|.
gi 1025889903 166 MILDEPTVGVD 176
Cdd:cd03289 160 LLLDEPSAHLD 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
136-227 |
9.74e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 136 EYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVHqfyeMLEMLNKKLGITLILVTHD---VGTVTDKV 212
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVL----WLETYLLKWPKTFIVVSHArefLNTVVTDI 411
|
90
....*....|....*.
gi 1025889903 213 THVAclNKKLH-FHGD 227
Cdd:PLN03073 412 LHLH--GQKLVtYKGD 425
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-178 |
1.00e-05 |
|
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: 45.44 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 29 LEIPR-GAFLAIVGPNGSGKSTLLKLLLGLFKLQKGK------------------IEIFGEDIR--RFKDWQKVGFVSQk 87
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgseLQNYFTKLLegDVKVIVKPQYVDL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 88 ansfnsgFPATVFEVVQSGLTKKiglfkfagkEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMI 167
Cdd:cd03236 99 -------IPKAVKGKVGELLKKK---------DERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170
....*....|.
gi 1025889903 168 LDEPTVGVDSK 178
Cdd:cd03236 163 FDEPSSYLDIK 173
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-203 |
1.26e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRrfkdwqkvgFVSQ 86
Cdd:PRK11288 3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR---------FAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KAnSFNSGF----------PA-TVFEVVQSG-LTKKIGLFKfaGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVF 154
Cdd:PRK11288 74 TA-ALAAGVaiiyqelhlvPEmTVAENLYLGqLPHKGGIVN--RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH 203
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSH 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-192 |
1.40e-05 |
|
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: 44.54 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 6 NPIVKFEDISY----KYTKDLVLEHVSLEIPRGAFLAIVGPNGSGKST--LLKLLLGLFKLQKGKIEIFG----EDIRRF 75
Cdd:cd03232 1 GSVLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTllDVLAGRKTAGVITGEILINGrpldKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 76 kdwqkVGFVSQkansfnsgfpatvFEVVQSGLTkkiglfkfagkedkqkVKKALE-SVdmleyqnrNIGALSGGQQQRVF 154
Cdd:cd03232 81 -----TGYVEQ-------------QDVHSPNLT----------------VREALRfSA--------LLRGLSVEQRKRLT 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVhqfYEMLEMLNK 192
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAA---YNIVRFLKK 153
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-172 |
1.84e-05 |
|
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: 45.55 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 28 SLEIPR-GAFLAIVGPNGSGKSTLLklllglfklqkgKI---EI---FGeDIRRFKDWQKV-----GFVSQkansfnsgf 95
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTAL------------KIlsgELkpnLG-DYDEEPSWDEVlkrfrGTELQ--------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 96 paTVFEVVQSGLTK---KIGLFKFAGKEDKQKVKKALESVD-------------MLEYQNRNIGALSGGQQQRVFIARSL 159
Cdd:COG1245 150 --DYFKKLANGEIKvahKPQYVDLIPKVFKGTVRELLEKVDergkldelaeklgLENILDRDISELSGGELQRVAIAAAL 227
|
170
....*....|...
gi 1025889903 160 VSEPELMILDEPT 172
Cdd:COG1245 228 LRDADFYFFDEPS 240
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-203 |
3.98e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIrRFKDWQK-----VGFVSQKANSFNSgfpAT 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEalengISMVHQELNLVLQ---RS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 99 VFEVVQSGLTKKIGLFKfagKEDK--QKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVD 176
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFV---DQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180
....*....|....*....|....*..
gi 1025889903 177 SKNVHQFYEMLEMLnKKLGITLILVTH 203
Cdd:PRK10982 167 EKEVNHLFTIIRKL-KERGCGIVYISH 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
126-172 |
4.73e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 4.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1025889903 126 KKALESVDMLEYQN---RNIGALSGGQQQRVFIARSLVSEPELMILDEPT 172
Cdd:PRK13409 191 GKLDEVVERLGLENildRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-210 |
6.33e-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: 43.85 E-value: 6.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 145 LSGGQQQRVFIARSL---VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTH--DVGTVTD 210
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHnlDVIKTAD 899
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
140-215 |
8.02e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 8.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025889903 140 RNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKNVhqfyEMLEMLNKKLGITLILVTHD---VGTVTDKVTHV 215
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV----IWLEKWLKSYQGTLILISHDrdfLDPIVDKIIHI 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-176 |
1.22e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 23 VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLL--GLFKLQKGKIEIFGEDIRRFKDWQKVG---FVSQK--------AN 89
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGegiFMAFQypveipgvSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 90 SFnsgFPATVFEVVQSGLTKK-IGLFKFAG-KEDKQKVKKALEsvDMLEyQNRNIGaLSGGQQQRVFIARSLVSEPELMI 167
Cdd:PRK09580 96 QF---FLQTALNAVRSYRGQEpLDRFDFQDlMEEKIALLKMPE--DLLT-RSVNVG-FSGGEKKRNDILQMAVLEPELCI 168
|
....*....
gi 1025889903 168 LDEPTVGVD 176
Cdd:PRK09580 169 LDESDSGLD 177
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-204 |
1.62e-04 |
|
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: 41.19 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 28 SLEIPRGAFLAIVGPNGSGKSTLlklllglfklqkgkieifgedirrFKDwqkVGF-VSQKANSFNSGfpatvfEVVQSG 106
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTI------------------------LDA---IGLaLGGAQSATRRR------SGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 107 LTKkiglfkfagkedkqkvkkALESvdmLEYQNRNIGaLSGGQQQRVFIA-----RSLVSEPeLMILDEPTVGVDSKNVH 181
Cdd:cd03227 62 CIV------------------AAVS---AELIFTRLQ-LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|...
gi 1025889903 182 QFYEMLEMLNKKlGITLILVTHD 204
Cdd:cd03227 119 ALAEAILEHLVK-GAQVIVITHL 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
135-213 |
1.68e-04 |
|
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: 40.82 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 135 LEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSKN-----VHQFYEMLEMLNKKLGITLILVTHDVGTVT 209
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQealllLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
....
gi 1025889903 210 DKVT 213
Cdd:smart00382 131 PALL 134
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
113-178 |
2.07e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 113 LFKFAGKEDKQK-VKKALESVDMLEYQNRNIG-----ALSGGQQQRVFIARSLVSEPELMILDEPTVGVDSK 178
Cdd:PLN03140 982 LPKEVSKEEKMMfVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-234 |
2.20e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 7 PIVKFEDISYKYTKD-LVLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKG--------KIEIFGEdirrfkd 77
Cdd:PLN03073 507 PIISFSDASFGYPGGpLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsakvRMAVFSQ------- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 78 wQKVGFVSQKANSF---NSGFPAtvfeVVQSGLTKKIGLFKFAGkedkqkvKKALESVdmleYqnrnigALSGGQQQRVF 154
Cdd:PLN03073 580 -HHVDGLDLSSNPLlymMRCFPG----VPEQKLRAHLGSFGVTG-------NLALQPM----Y------TLSGGQKSRVA 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 155 IARSLVSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKklGItlILVTHDVGTVTDKVTHVACLN--KKLHFHGDACEYN 232
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSegKVTPFHGTFHDYK 713
|
..
gi 1025889903 233 EL 234
Cdd:PLN03073 714 KT 715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
166-213 |
2.86e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1025889903 166 MILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLIL-VTHD---VGTVTDKVT 213
Cdd:PRK02224 815 LILDEPTVFLDSGHVSQLVDLVESM-RRLGVEQIVvVSHDdelVGAADDLVR 865
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-204 |
2.92e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 139 NRNIGALSGGQQQRVFIARSLVSepELM----ILDEPTVGVDSKNVHQFYEMLEMLnKKLGITLILVTHD 204
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIGS--GLVgvlyVLDEPSIGLHQRDNDRLIETLKRL-RDLGNTVIVVEHD 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-172 |
3.36e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDiRRF---KDWQK--VGFVSQKANSFNSgfpAT 98
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFngpKSSQEagIGIIHQELNLIPQ---LT 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025889903 99 VFEVVQSG--LTKKIGLFKFagKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEPT 172
Cdd:PRK10762 96 IAENIFLGreFVNRFGRIDW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-210 |
3.60e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 9 VKFEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDIRRFkdwqkvgfvsq 86
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 87 KANSFNSGFPATVFEVVQSGLTKKIGLfkfaGKEDKQKVKKALESVDMLEYQNRnIGALSG---------------GQQQ 151
Cdd:cd03288 89 PLHTLRSRLSIILQDPILFSGSIRFNL----DPECKCTDDRLWEALEIAQLKNM-VKSLPGgldavvteggenfsvGQRQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVD--SKNVHQFYEMLEMLNKklgiTLILVTHDVGTVTD 210
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDmaTENILQKVVMTAFADR----TVVTIAHRVSTILD 220
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
145-204 |
3.90e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 3.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 145 LSGGQQQRVFIARSL---VSEPELMILDEPTVGVDSKNVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHN 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
119-178 |
6.15e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 6.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025889903 119 KEDKQKVKKALESVDMLEYQNRNIG----ALSGGQQQRVFIARSLVSEPELMI-LDEPTVGVDSK 178
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-236 |
7.47e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEdirrfkdwqkvgfVSQKAnsFNSGFPATVFEVv 103
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIA--ISAGLSGQLTGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 104 qSGLTKKIGLFKFAGKEDKQKVKKALESVDMLEYQNRNIGALSGGQQQRVFIARSLVSEPELMILDEP-TVGVDS---KN 179
Cdd:PRK13546 104 -ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTfaqKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025889903 180 VHQFYEMlemlnKKLGITLILVTHDVGTVTDKVTHVACLNKklhfhGDACEYNELDE 236
Cdd:PRK13546 183 LDKIYEF-----KEQNKTIFFVSHNLGQVRQFCTKIAWIEG-----GKLKDYGELDD 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-209 |
8.67e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 8.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025889903 145 LSGGQQQRVFIARSLVSEPELMILDEPTVGVDSK---NVHQFYEMLEMLNKKlgiTLILVTHDVGTVT 209
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKK---TALVVEHDLAVLD 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-48 |
1.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 1.86e-03
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-176 |
2.79e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 11 FEDISYKYTKDL--VLEHVSLEIPRGAFLAIVGPNGSGKSTLLKLLLGLFKLQKGKIEIFGEDI---------RRFK--- 76
Cdd:PTZ00243 1311 FEGVQMRYREGLplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgayglrelrRQFSmip 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 77 ------DwqkvGFVSQKANSFNSGFPATVFEVVQsgltkKIGLfkfagkedKQKVKKALESVD--MLEyqnrniGAL--S 146
Cdd:PTZ00243 1391 qdpvlfD----GTVRQNVDPFLEASSAEVWAALE-----LVGL--------RERVASESEGIDsrVLE------GGSnyS 1447
|
170 180 190
....*....|....*....|....*....|.
gi 1025889903 147 GGQQQRVFIARSLVSEPELMIL-DEPTVGVD 176
Cdd:PTZ00243 1448 VGQRQLMCMARALLKKGSGFILmDEATANID 1478
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
27-48 |
3.40e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 3.40e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-49 |
4.45e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 4.45e-03
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
152-204 |
5.03e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 5.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1025889903 152 RVFIARSLVSEPELMILDEPTVGVDsknVHQFYEMLEMLNKKlGITLILVTHD 204
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNER-NSTMIIISHD 211
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-49 |
5.57e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.57e-03
10 20
....*....|....*....|....*.
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKST 49
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-49 |
6.00e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 6.00e-03
10 20
....*....|....*....|....*.
gi 1025889903 24 LEHVSLEIPRGAFLAIVGPNGSGKST 49
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKST 650
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
135-204 |
7.43e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025889903 135 LEY--QNRNIGALSGGQQQRVFIA----RSLVSepELMILDEPTVGvdsknVHQ-----FYEMLEMLnKKLGITLILVTH 203
Cdd:PRK00349 478 LDYltLSRSAGTLSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIG-----LHQrdndrLIETLKHL-RDLGNTLIVVEH 549
|
.
gi 1025889903 204 D 204
Cdd:PRK00349 550 D 550
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-49 |
7.67e-03 |
|
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: 37.47 E-value: 7.67e-03
|
| |
