|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
75-277 |
2.47e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDD-------LSVMTQ 145
Cdd:COG1131 1 IEVRGLTKRYGDkTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVARDpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 223 GMDLESIDLFWDYLDHVGGSVVTI---THDFNQIDNYFTRVVLLKDGVIKSDESVANI 277
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVllsTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
75-268 |
4.53e-41 |
|
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: 140.23 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDD-------LSVMTQ 145
Cdd:cd03230 1 IEVRNLSKRYgKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIKKEpeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIalslkiydayskiniddllkkfrlteqsevivdQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:cd03230 81 EPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 226 LESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03230 128 PESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
73-269 |
4.26e-39 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 143.28 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQddLSVMTQEnclia 151
Cdd:COG0488 314 KVLELEGLSKSYgDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK--IGYFDQH----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 slkvREQIALSLKIYDAYS-------KINIDDLLKKFRLT-EQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVG 223
Cdd:COG0488 387 ----QEELDPDKTVLDELRdgapggtEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1726007896 224 MDLESIDLFWDYLDHVGGSVVTITHD--FnqIDNYFTRVVLLKDGVIK 269
Cdd:COG0488 463 LDIETLEALEEALDDFPGTVLLVSHDryF--LDRVATRILEFEDGGVR 508
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
75-277 |
1.07e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.44 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLS-----IYGrdriaLLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFN--AQDDL 140
Cdd:COG4555 2 IEVENLSKKYgKVPALKDVSFTakdgeITG-----LLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedVRKEPreARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALSLKIYDAYSKIN---IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 218 DEPTVGMDLESIDLFWDYLDHVGGSVVTI---THDFNQIDNYFTRVVLLKDGVIKSDESVANI 277
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVlfsSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
74-268 |
1.14e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvMTQENCLIA- 151
Cdd:COG1121 6 AIELENLTVSYgGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV--RLFGKP----PRRARRRIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 -----------SLKVREQIALSL-------KIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSK 213
Cdd:COG1121 80 vpqraevdwdfPITVRDVVLMGRygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 214 LLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
76-266 |
1.26e-37 |
|
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: 132.21 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--DLSVM------- 143
Cdd:cd03225 1 ELKNLSFSYPDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV--LVDGKDltKLSLKelrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 -------TQenclIASLKVREQIALSLKIY-DAYSKIN--IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSK 213
Cdd:cd03225 79 lvfqnpdDQ----FFGPTVEEEVAFGLENLgLPEEEIEerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 214 LLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
75-265 |
7.28e-36 |
|
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: 127.60 E-value: 7.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD----------DLSVM 143
Cdd:COG4133 3 LEAENLSCRRgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV--LWNGEPirdaredyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKIY-DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 223 GMDLESIDLFWDYL-DHV--GGSVVTITHDfnQIDNYFTRVVLLKD 265
Cdd:COG4133 161 ALDAAGVALLAELIaAHLarGGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
75-285 |
1.22e-35 |
|
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: 127.83 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF--KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVM 143
Cdd:COG1122 1 IELENLSFSYpgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQ--ENCLIASlKVREQIALSLKIYdAYSKINI----DDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI-KPsKLLI 216
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFGPENL-GLPREEIrervEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAmEP-EVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 217 LDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
75-269 |
2.41e-35 |
|
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: 126.85 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK---NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFN-------AQDDLSVM 143
Cdd:cd03263 1 LQIRNLTKTYKkgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSirtdrkaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALS--LK-IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03263 81 PQFDALFDELTVREHLRFYarLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 221 TVGMDLESIDLFWDYLDHVGG--SVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
76-266 |
3.25e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.97 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDDLSVMTQEncliaslk 154
Cdd:cd00267 1 EIENLSFRYgGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI--LIDGKDIAKLPLEE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VREQIAlslkiydayskiniddllkkfrlteqsevIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWD 234
Cdd:cd00267 71 LRRRIG-----------------------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*
gi 1726007896 235 YLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd00267 122 LLRELaeeGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
75-266 |
7.36e-32 |
|
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: 115.24 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNaqddlsvmtqencliasl 153
Cdd:cd03221 1 IELENLSKTYgGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 154 kvreqialsLKIydAYskiniddllkkfrlteqseviVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFW 233
Cdd:cd03221 63 ---------VKI--GY---------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|...
gi 1726007896 234 DYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
76-268 |
8.20e-32 |
|
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: 117.25 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvMTQENCLIA--- 151
Cdd:cd03235 1 EVEDLTVSYGGhPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI--RVFGKP----LEKERKRIGyvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 ---------SLKVREQIALSL-------KIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:cd03235 75 qrrsidrdfPISVRDVVLMGLyghkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 216 ILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
75-268 |
2.04e-31 |
|
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: 116.23 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-----KHFNAQDDLSVMTQENC 148
Cdd:cd03269 1 LEVENVTKRFGrVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLKVREQIAL--SLKIYD-AYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:cd03269 81 LYPKMKVIDQLVYlaQLKGLKkEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 226 LESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03269 161 PVNVELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
74-273 |
2.63e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.30 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNtILGNII-PDKGSVvkHFNAQdDLSVMT--- 144
Cdd:COG1136 4 LLELRNLTKSYGTgegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDrPTSGEV--LIDGQ-DISSLSere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 -------------QENCLIASLKVREQIALSLKIYDAYSKIN---IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTL 208
Cdd:COG1136 80 larlrrrhigfvfQFFNLLPELTALENVALPLLLAGVSRKERrerARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 209 IKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDfNQIDNYFTRVVLLKDGVIKSDES 273
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
76-269 |
3.58e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.43 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFK--NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFNAQDDLS----VMTQE 146
Cdd:cd03226 1 RIENISFSYKkgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKsigyVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 NCLIASLKVREQIALSLKIYDAYSKInIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQ-AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 227 ESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:cd03226 160 KNMERVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
74-268 |
1.79e-30 |
|
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: 114.76 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVM 143
Cdd:COG1120 1 MLEAENLSVGYgGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdLASLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALS----LKIYDAYSKIN---IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLI 216
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 217 LDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG1120 161 LDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
89-222 |
1.89e-30 |
|
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: 111.97 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDD-----------LSVMTQENCLIASLKVRE 157
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI--LLDGQDLtdderkslrkeIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 158 QIALSLKI---YDAYSKINIDDLLKKFRLTEQSEVIVD----QLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:pfam00005 79 NLRLGLLLkglSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
77-270 |
1.89e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 77 LKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQddLSVMTQENCLIASLKV 155
Cdd:COG0488 1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR--IGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQI---------------ALSLKI----------------------YDAYSKIniDDLLKKFRLT-EQSEVIVDQLSGG 197
Cdd:COG0488 79 LDTVldgdaelraleaeleELEAKLaepdedlerlaelqeefealggWEAEARA--EEILSGLGFPeEDLDRPVSELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 198 QKRRLALLLTLIKPSKLLILDEPTVGMDLESIDlfW--DYLDHVGGSVVTITHD--FnqIDNYFTRVVLLKDGVIKS 270
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPGTVLVVSHDryF--LDRVATRILELDRGKLTL 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
75-268 |
6.89e-30 |
|
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: 112.20 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD----------- 138
Cdd:cd03255 1 IELKNLSKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR--VDGTDisklsekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 ----DLSVMTQENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:cd03255 79 frrrHIGFVFQSFNLLPDLTALENVELPLLLAgvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 212 SKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDfNQIDNYFTRVVLLKDGVI 268
Cdd:cd03255 159 PKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
65-268 |
1.47e-29 |
|
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: 116.93 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 65 AGHTHGDALILELKNLNKSFKN------PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQd 138
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYPVrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI--LFDGK- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 DLSVMTQEN-----------------CLIASLKVREQIALSLKIYDAYSKIN----IDDLLKKFRLTEQsevIVD----Q 193
Cdd:COG1123 328 DLTKLSRRSlrelrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSRAErrerVAELLERVGLPPD---LADryphE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 194 LSGGQKRRLALLLTLI-KPsKLLILDEPTVGMDLeSI-----DLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGV 267
Cdd:COG1123 405 LSGGQRQRVAIARALAlEP-KLLILDEPTSALDV-SVqaqilNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
.
gi 1726007896 268 I 268
Cdd:COG1123 483 I 483
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
74-268 |
2.98e-29 |
|
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: 111.06 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDDLSVMTQE-- 146
Cdd:cd03257 1 LLEVKNLSVSFPTgggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII--FDGKDLLKLSRRLrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 --------------NCLIASLKVREQIALSLKIYDAYSK-----INIDDLLKKFRLTEQsevIVD----QLSGGQKRRLA 203
Cdd:cd03257 79 irrkeiqmvfqdpmSSLNPRMTIGEQIAEPLRIHGKLSKkearkEAVLLLLVGVGLPEE---VLNryphELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 204 LLLTLIKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
71-268 |
1.16e-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: 114.86 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 71 DALILELKNLnkSF-----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNaQDD 139
Cdd:COG4987 330 GGPSLELEDV--SFrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdLRDLD-EDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 L----SVMTQENCLIASlKVREQIALSL------KIYDAYSKINIDDLLKkfRLTEQSEVIVD----QLSGGQKRRLALL 205
Cdd:COG4987 407 LrrriAVVPQRPHLFDT-TLRENLRLARpdatdeELWAALERVGLGDWLA--ALPDGLDTWLGeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 206 LTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDnYFTRVVLLKDGVI 268
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLE-RMDRILVLEDGRI 547
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
75-268 |
1.69e-28 |
|
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: 108.38 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMT 144
Cdd:cd03259 1 LELKGLSKTYgSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL--IDGRDvtgvpperrNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 222 VGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03259 159 SALDAKLreelREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
76-268 |
2.04e-28 |
|
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: 107.52 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvmtqenclIASLK 154
Cdd:cd03214 1 EVENLSVGYgGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--LLDGKD-----------LASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VRE---QIALSLKiydAYSKINIDDLLKKFrlteqseviVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL----E 227
Cdd:cd03214 68 PKElarKIAYVPQ---ALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1726007896 228 SIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
75-268 |
2.05e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdLSVMT--------- 144
Cdd:COG4619 1 LELEGLSFRVGGkPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI--YLDGKP-LSAMPppewrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 ---QENCLIASlKVREQIALSLKIYD-AYSKINIDDLLKKFRLTEqsEVI---VDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:COG4619 78 yvpQEPALWGG-TVRDNLPFPFQLRErKFDRERALELLERLGLPP--DILdkpVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 218 DEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG4619 155 DEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
75-269 |
2.17e-28 |
|
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: 108.05 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKNP-VLKDVNLSIyGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDD----------LSVM 143
Cdd:cd03264 1 LQLENLTKRYGKKrALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIR--IDGQDVlkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQ---IALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03264 78 PQEFGVYPNFTVREFldyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 221 TVGMDLESIDLFWDYLDHVGGSVVTI--THDFNQIDNYFTRVVLLKDGVIK 269
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
74-284 |
7.76e-28 |
|
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: 107.37 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--DLS--------- 141
Cdd:COG1127 5 MIEVRNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI--LVDGQDitGLSekelyelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 ---VMTQENCLIASLKVREQIALSLKIYDAYSKINIDDL----LKKFRLTEQ-----SEvivdqLSGGQKRRLALLLTLI 209
Cdd:COG1127 83 rigMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELvlekLELVGLPGAadkmpSE-----LSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 210 -KPsKLLILDEPTVGMD---LESID-LFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANI-HSNNQT 283
Cdd:COG1127 158 lDP-EILLYDEPTAGLDpitSAVIDeLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELlASDDPW 236
|
.
gi 1726007896 284 I 284
Cdd:COG1127 237 V 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
75-268 |
8.50e-28 |
|
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: 107.20 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD--DLS---------- 141
Cdd:cd03261 1 IELRGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL--IDGEDisGLSeaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 --VMTQENCLIASLKVREQIALSLKIYDAYSKINIDDL----LKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:cd03261 79 mgMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 216 ILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03261 159 LYDEPTAGLDpiasGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-285 |
1.99e-27 |
|
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: 110.76 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF---KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGnIIPDKGSV--VKHFNAQDDLSV------ 142
Cdd:COG1123 4 LLEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgEVLLDGRDLLELsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ----------MTQENCLiaslKVREQIALSLKIYD---AYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI 209
Cdd:COG1123 83 rrigmvfqdpMTQLNPV----TVGDQIAEALENLGlsrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 210 KPSKLLILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:COG1123 159 LDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
75-249 |
6.35e-27 |
|
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: 104.83 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--------------- 138
Cdd:cd03219 1 LEVRGLTKRFGGlVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV--LFDGEDitglppheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 ----------DLSVMtqENCLIASLKVREQIALSLKIYDAYSKIN--IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:cd03219 79 rtfqiprlfpELTVL--ENVMVAAQARTGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 207 TLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHD 249
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELrerGITVLLVEHD 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
74-271 |
6.62e-26 |
|
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: 102.47 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQ------DDL------ 140
Cdd:COG1119 3 LLELRNVTVRRgGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERrggedvWELrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 --SVMTQEncLIASLKVREqIALS-----LKIYDAYSKINI---DDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIK 210
Cdd:COG1119 83 vsPALQLR--FPRDETVLD-VVLSgffdsIGLYREPTDEQReraRELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHVGGS----VVTITHDFNQIDNYFTRVVLLKDGVIKSD 271
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
75-266 |
8.31e-26 |
|
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: 100.34 E-value: 8.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD-------------DL 140
Cdd:cd03229 1 LELKNVSKRYGQkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL--IDGEDltdledelpplrrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALSlkiydayskiniddllkkfrlteqsevivdqLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1726007896 221 TVGMDLESIDLFWDYL----DHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03229 128 TSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-272 |
8.78e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD------------- 138
Cdd:COG2884 1 MIRFENVSKRYPGgrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQV--LVNGQDlsrlkrreipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 -DLSVMTQENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI-KPsK 213
Cdd:COG2884 79 rRIGVVFQDFRLLPDRTVYENVALPLRVTgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVnRP-E 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 214 LLILDEPTVGMDLES----IDLFwDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDE 272
Cdd:COG2884 158 LLLADEPTGNLDPETsweiMELL-EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
75-249 |
1.66e-25 |
|
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: 101.01 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQ------DDLSVM 143
Cdd:cd03293 1 LEVRNVSKTYGGgggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL--VDGEpvtgpgPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKIYDAYSKI---NIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEareRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 1726007896 221 TVGMD----LESIDLFWDYLDHVGGSVVTITHD 249
Cdd:cd03293 159 FSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
75-288 |
2.09e-25 |
|
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: 101.11 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV--------------------- 131
Cdd:cd03256 1 IEVENLSKTYPNgkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 ----KHFNAQDDLSVMtqENCLIASLKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLT 207
Cdd:cd03256 81 gmifQQFNLIERLSVL--ENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 208 LIKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIhsNNQT 283
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL--TDEV 236
|
....*
gi 1726007896 284 IEHWY 288
Cdd:cd03256 237 LDEIY 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
75-268 |
2.12e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.30 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---DLSV-------- 142
Cdd:COG1118 3 IEVRNISKRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV--LNGRDlftNLPPrerrvgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ---------MTqencliaslkVREQIALSLKIYDAySKINI----DDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTL- 208
Cdd:COG1118 81 fqhyalfphMT----------VAENIAFGLRVRPP-SKAEIrarvEELLELVQLEGLADRYPSQLSGGQRQRVALARALa 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 209 IKPsKLLILDEPTVGMD------LESidlfW--DYLDHVGGSVVTITHDfnQ------IDnyftRVVLLKDGVI 268
Cdd:COG1118 150 VEP-EVLLLDEPFGALDakvrkeLRR----WlrRLHDELGGTTVFVTHD--QeealelAD----RVVVMNQGRI 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
75-266 |
3.44e-25 |
|
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: 98.61 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvmtqenclia 151
Cdd:cd03228 1 IEFKNVSFSYPGrpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI--LIDGVD------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 slkvreqialslkiydaYSKINIDDLLKKFRLTEQSEVIVDQ------LSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:cd03228 66 -----------------LRDLDLESLRKNIAYVPQDPFLFSGtireniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1726007896 226 LESIDLFWDYLDHVGG--SVVTITHDFNQIDNyFTRVVLLKDG 266
Cdd:cd03228 129 PETEALILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
75-268 |
8.57e-25 |
|
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: 103.68 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVM 143
Cdd:COG4988 337 IELEDVSFSYPGgrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdLSDLDPASwrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIA-SlkVREQIALSL------KIYDAYSKINIDDLLKKF------RLTEQSEvivdQLSGGQKRRLALLLTLIK 210
Cdd:COG4988 417 PQNPYLFAgT--IRENLRLGRpdasdeELEAALEAAGLDEFVAALpdgldtPLGEGGR----GLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHVGGS--VVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQA-DRILVLDDGRI 549
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-266 |
1.39e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.18 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLS-----IYGrdriaLLGSNGSGKTTIVNTILGNIIPDKGSVvkHFN-------AQDDL 140
Cdd:COG4152 1 MLELKGLTKRFGDkTAVDDVSFTvpkgeIFG-----LLGPNGAGKTTTIRIILGILAPDSGEV--LWDgepldpeDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIA-------LSLKiyDAysKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI-KPs 212
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVylarlkgLSKA--EA--KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLhDP- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 213 KLLILDEPTVGMDLESIDLFWDYL-DHV--GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIrELAakGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
74-249 |
3.56e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVM 143
Cdd:PRK11607 19 LLEIRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM--LDGVDlshvppyqrPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKiYDAYSKINIDD----LLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLK-QDKLPKAEIASrvneMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1726007896 220 PTVGMD--------LESIDLfwdyLDHVGGSVVTITHD 249
Cdd:PRK11607 176 PMGALDkklrdrmqLEVVDI----LERVGVTCVMVTHD 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
75-268 |
4.89e-24 |
|
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: 95.19 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvmtqenclIASL 153
Cdd:cd03216 1 LELRGITKRFgGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI--LVDGKE-----------VSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 154 KVREqiALSLKIYdayskiniddllkkfrlteqsevIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFW 233
Cdd:cd03216 68 SPRD--ARRAGIA-----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 1726007896 234 DYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03216 123 KVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
75-267 |
9.44e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV--------KHFNAQDDLSVMTQ 145
Cdd:PRK13536 42 IDLAGVSKSYGDkAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpaRARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREqialSLKIYDAYSKIN-------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:PRK13536 122 FDNLDLEFTVRE----NLLVFGRYFGMStreieavIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 219 EPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGV 267
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
74-268 |
9.66e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 96.66 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-------------------- 131
Cdd:COG3638 2 MLELRNLSKRYPGgtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 -----KHFNAQDDLSVMTqeNCLIASLKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:COG3638 82 igmifQQFNLVPRLSVLT--NVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 207 TLIKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTarqvMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
75-268 |
1.04e-23 |
|
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: 100.68 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnkSFK-----NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DL 140
Cdd:COG2274 474 IELENV--SFRypgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidLRQIDPASlrrQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIA-SlkVREQIALSL------KIYDAYSKINIDDLLKKF------RLTEQSEvivdQLSGGQKRRLALLLT 207
Cdd:COG2274 552 GVVLQDVFLFSgT--IRENITLGDpdatdeEIIEAARLAGLHDFIEALpmgydtVVGEGGS----NLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 208 LIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGG--SVVTITHDFNQIDNyFTRVVLLKDGVI 268
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
70-249 |
1.68e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 96.31 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 70 GDALILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFNAQD-DL 140
Cdd:COG1116 3 AAAPALELRGVSKRFPTggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgKPVTGPGpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALSLKI---YDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELrgvPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1726007896 218 DEPTVGMD------LEsiDLFWDYLDHVGGSVVTITHD 249
Cdd:COG1116 163 DEPFGALDaltrerLQ--DELLRLWQETGKTVLFVTHD 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
75-268 |
4.03e-23 |
|
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: 94.71 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMTQ 145
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL--LNGKDitnlppekrDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSLKIyDAYSKINIDDllkkfRLTEQSEVI---------VDQLSGGQKRRLALLLTLIKPSKLLI 216
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKK-RKVDKKEIER-----KVLEIAEMLgidhllnrkPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 217 LDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03299 153 LDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
74-289 |
6.16e-23 |
|
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: 94.67 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVK------------------- 132
Cdd:TIGR02315 1 MLEVENLSKVYPNgkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegtditklrgkklrklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 133 ------HFNAQDDLSVMtqENCLIASLKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:TIGR02315 81 igmifqHYNLIERLTVL--ENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 207 TLIKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIhsNNQ 282
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTskqvMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL--DDE 236
|
....*..
gi 1726007896 283 TIEHWYR 289
Cdd:TIGR02315 237 VLRHIYG 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
74-268 |
8.05e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.32 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD---------DLSVM 143
Cdd:COG3842 5 ALELENVSKRYgDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI--LLDGRDvtglppekrNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKIyDAYSK--IN--IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRM-RGVPKaeIRarVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 220 PTVGMDLE-----SIDLFwDYLDHVGGSVVTITHDFNQIdnyFT---RVVLLKDGVI 268
Cdd:COG3842 162 PLSALDAKlreemREELR-RLQRELGITFIYVTHDQEEA---LAladRIAVMNDGRI 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
75-268 |
8.28e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.44 E-value: 8.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDDLSVMTQENCLIAS 152
Cdd:cd03268 1 LKTNDLTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 153 ------LKVREQIALSLKIYDAYSKiNIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:cd03268 81 pgfypnLTARENLRLLARLLGIRKK-RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 227 ESI----DLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03268 160 DGIkelrELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
87-268 |
1.50e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 94.76 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGS-------VVKHFN-AQDDLSVMTQENCLIASLKVREQ 158
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvagydVVREPRkVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 159 IALSLKIYDAYSKI---NIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDY 235
Cdd:TIGR01188 87 LEMMGRLYGLPKDEaeeRAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1726007896 236 LDHVGGSVVTI---THDFNQIDNYFTRVVLLKDGVI 268
Cdd:TIGR01188 167 IRALKEEGVTIlltTHYMEEADKLCDRIAIIDHGRI 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
75-225 |
1.74e-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: 92.99 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFN----AQDDLSVM 143
Cdd:cd03218 1 LRAENLSKRYGKrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqdITKLPmhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
....*
gi 1726007896 221 TVGMD 225
Cdd:cd03218 161 FAGVD 165
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-221 |
1.98e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.61 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF------KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD--------- 138
Cdd:COG1101 1 MLELKNLSKTFnpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL--IDGKDvtklpeykr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 -----------------DLSVmtQENCLIASLKVRE---QIALSLKIYDAYSkinidDLLKKF------RLTEQseviVD 192
Cdd:COG1101 79 akyigrvfqdpmmgtapSMTI--EENLALAYRRGKRrglRRGLTKKRRELFR-----ELLATLglglenRLDTK----VG 147
|
170 180
....*....|....*....|....*....
gi 1726007896 193 QLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
75-268 |
7.24e-22 |
|
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: 91.28 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGS-VVKHFNAQDD-------LSVMTQ 145
Cdd:cd03265 1 IEVENLVKKYgDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREprevrrrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSLKIYD---AYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1726007896 223 GMDLESIDLFWDYL----DHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03265 161 GLDPQTRAHVWEYIeklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
75-287 |
1.31e-21 |
|
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: 91.74 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNL------NKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnaQDDLSVMTQENC 148
Cdd:TIGR04521 1 IKLKNVsyiyqpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT-----IDGRDITAKKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLK------------------VREQIA-------LSLK-----IYDAYSKINIDDLLKkfrltEQSEVivdQLSGGQ 198
Cdd:TIGR04521 76 KLKDLRkkvglvfqfpehqlfeetVYKDIAfgpknlgLSEEeaeerVKEALELVGLDEEYL-----ERSPF---ELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 199 KRRLALLLTL-IKPsKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDES 273
Cdd:TIGR04521 148 MRRVAIAGVLaMEP-EVLILDEPTAGLDPKGrkeiLDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
250
....*....|....
gi 1726007896 274 VANIHSNNQTIEHW 287
Cdd:TIGR04521 227 PREVFSDVDELEKI 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
91-271 |
1.32e-21 |
|
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: 90.24 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 91 DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMTQENCLIASLKVREQIAL 161
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL--INGVDvtaappadrPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 162 SL------------KIYDAYSKINIDDLLKKfrlteqsevIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD---- 225
Cdd:cd03298 94 GLspglkltaedrqAIEVALARVGLAGLEKR---------LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalr 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 226 LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSD 271
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
75-268 |
1.67e-21 |
|
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: 90.01 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMT 144
Cdd:cd03301 1 VELENVTKRFGNvTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY--IGGRDvtdlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIALSLKIYDAySKINID----DLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKV-PKDEIDervrEVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 221 --------TVGMDLESIDLfwdyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03301 158 lsnldaklRVQMRAELKRL----QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
75-268 |
1.76e-21 |
|
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: 90.48 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDDLSVMTQEN------ 147
Cdd:cd03296 3 IEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL--FGGEDATDVPVQERnvgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 148 ---CLIASLKVREQIALSLKIYDAYSKIN-------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:cd03296 81 qhyALFRHMTVFDNVAFGLRVKPRSERPPeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 218 DEPTVGMDLESIDLFWDYL----DHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
75-268 |
2.08e-21 |
|
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: 89.51 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGS------------------------ 129
Cdd:cd03262 1 IEIKNLHKSFgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglkltddkkninelrqkvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 130 VVKHFNAQDDLSVMtqENCLIASLKVR-------EQIALslkiydayskinidDLLKKFRLTEQSEVIVDQLSGGQKRRL 202
Cdd:cd03262 81 VFQQFNLFPHLTVL--ENITLAPIKVKgmskaeaEERAL--------------ELLEKVGLADKADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 203 ALLLTLIKPSKLLILDEPTVGMDLESIDlfwDYLD------HVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVG---EVLDvmkdlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
75-223 |
3.44e-21 |
|
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: 89.42 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDDLSVMT--------- 144
Cdd:cd03224 1 LEVENLNAGYgKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR--FDGRDITGLPPheraragig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 ---QENCLIASLKVREQIALSLKIY-DAYSKINIDDLLKKF-RLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:cd03224 79 yvpEGRRIFPELTVEENLLLGAYARrRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
....
gi 1726007896 220 PTVG 223
Cdd:cd03224 159 PSEG 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
87-248 |
6.88e-21 |
|
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: 87.80 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQENCLIAS----LKVREQIALS 162
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGhlpgLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 LKIYDA---YSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLD-- 237
Cdd:TIGR01189 94 LHFWAAihgGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRah 173
|
170
....*....|..
gi 1726007896 238 -HVGGSVVTITH 248
Cdd:TIGR01189 174 lARGGIVLLTTH 185
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
93-269 |
7.34e-21 |
|
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: 88.38 E-value: 7.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 93 NLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV----VKHFNA---QDDLSVMTQENCLIASLKVREQIALSL-- 163
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkvndQSHTGLapyQRPVSMLFQENNLFAHLTVRQNIGLGLhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 164 ----------KIYDAYSKINIDDLLKkfRLTEQsevivdqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----LESI 229
Cdd:TIGR01277 98 glklnaeqqeKVVDAAQQVGIADYLD--RLPEQ-------LSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1726007896 230 DLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
75-281 |
1.64e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.89 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFkNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD---------DLSVMTQ 145
Cdd:COG3840 2 LRLDDLTYRY-GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI--LWNGQDltalppaerPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIAL----SLKiYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:COG3840 79 ENNLFPHLTVAQNIGLglrpGLK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 222 VGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNN 281
Cdd:COG3840 158 SALDpalrQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
70-262 |
2.64e-20 |
|
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: 90.42 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 70 GDALILELKNLNKSF--KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV------KHFNA---QD 138
Cdd:TIGR02857 317 APASSLEFSGVSVAYpgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvplADADAdswRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 DLSVMTQENCLIASlKVREQIALSLK------IYDAYSKINIDDLLKKFRLTEQSEVIVD--QLSGGQKRRLALLLTLIK 210
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPdasdaeIREALERAGLDEFVAALPQGLDTPIGEGgaGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYFTRVVL 262
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
87-271 |
3.36e-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: 87.00 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV----------KHFNAQDDLsVMTQENCLIASLKVR 156
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrrKKFLRRIGV-VFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIALSLKIYD---AYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL---ESID 230
Cdd:cd03267 114 DSFYLLAAIYDlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1726007896 231 LFWDYL--DHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSD 271
Cdd:cd03267 194 NFLKEYnrER-GTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
74-268 |
3.54e-20 |
|
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: 86.65 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNP-----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGS-------VVKH-FNAQDDL 140
Cdd:cd03266 1 MITADALTKRFRDVkktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEpAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALSLKIY----DAYsKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLI 216
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYglkgDEL-TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 217 LDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
75-269 |
3.58e-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: 85.44 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnaQDDLSVMTQENCLia 151
Cdd:cd03247 1 LSINNVSFSYPEqeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-----LDGVPVSDLEKAL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 slkvREQIA-LSLKIYdAYSKINIDDLLKKFrlteqsevivdqlSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----L 226
Cdd:cd03247 74 ----SSLISvLNQRPY-LFDTTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLDpiteR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1726007896 227 ESIDLFWDYLDhvGGSVVTITHDFNQIDnYFTRVVLLKDGVIK 269
Cdd:cd03247 136 QLLSLIFEVLK--DKTLIWITHHLTGIE-HMDKILFLENGKII 175
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
74-282 |
4.83e-20 |
|
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: 86.48 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV------------KHFNA 136
Cdd:cd03258 1 MIELKNVSKVFGDtggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 137 QDDLSVMTQENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSK 213
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAgvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 214 LLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQ 282
Cdd:cd03258 161 VLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
75-271 |
6.95e-20 |
|
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: 85.72 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSV 142
Cdd:cd03245 3 IEFRNVSFSYPNqeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdIRQLDPADlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASlKVREQIALSL------KIYDAYSKINIDDLLKK------FRLTEQSevivDQLSGGQKRRLALLLTLIK 210
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGApladdeRILRAAELAGVTDFVNKhpngldLQIGERG----RGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHVGG--SVVTITHDfNQIDNYFTRVVLLKDGVIKSD 271
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHR-PSLLDLVDRIIVMDSGRIVAD 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
75-268 |
9.99e-20 |
|
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: 85.15 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD-------------- 138
Cdd:cd03292 1 IEFINVTKTYPNgtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR--VNGQDvsdlrgraipylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 DLSVMTQENCLIASLKVREQIALSLKIYDAYSKI---NIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREirkRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 216 ILDEPTVGMDLES----IDLFWDyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03292 159 IADEPTGNLDPDTtweiMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
75-289 |
1.01e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVMT 144
Cdd:PRK13548 3 LEARNLSVRLgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpLADWSPAElarRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIAL---SLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRR--LALLLTLI----KPSKLL 215
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRvqLARVLAQLwepdGPPRWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 216 ILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSnNQTIEHWYR 289
Cdd:PRK13548 163 LLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT-PETLRRVYG 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-249 |
1.14e-19 |
|
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: 88.57 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-----KHFNAQDDL----SVMTQENCLIASlKVR 156
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpVSSLDQDEVrrrvSVCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIALSLK------IYDAYSKINIDDLLKkfRLTEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:TIGR02868 427 ENLRLARPdatdeeLWAALERVGLADWLR--ALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*..
gi 1726007896 227 ES----IDLFWDYLDhvGGSVVTITHD 249
Cdd:TIGR02868 505 ETadelLEDLLAALS--GRTVVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
74-293 |
1.19e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDK------------------------- 127
Cdd:PRK09984 4 IIRVEKLAKTFnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqregrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 128 -----GSVVKHFNAQDDLSVMtqENCLIASLKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRL 202
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVL--ENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 203 ALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESvaNIH 278
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS--SQQ 239
|
250
....*....|....*
gi 1726007896 279 SNNQTIEHWYRLMNQ 293
Cdd:PRK09984 240 FDNERFDHLYRSINR 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
86-262 |
1.66e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQddLSVMTQENCLIASL--KVREQIALS- 162
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR--VAYVPQRSEVPDSLplTVRDLVAMGr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 ------LKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYL 236
Cdd:NF040873 83 warrglWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|....*....
gi 1726007896 237 DHV---GGSVVTITHDFNQIDNYFTRVVL 262
Cdd:NF040873 163 AEEharGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
75-268 |
2.14e-19 |
|
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: 84.60 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMT 144
Cdd:cd03300 1 IELENVSKFYGGfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL--LDGKDitnlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKklpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 222 VGMDL---ESIDLFWDYL-DHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03300 159 GALDLklrKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
74-225 |
2.37e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 84.70 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--DLSV-------- 142
Cdd:COG1137 3 TLEAENLVKSYGKrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI--FLDGEDitHLPMhkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 --MTQEncliAS----LKVREQIALSL---KIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRL----ALlltLI 209
Cdd:COG1137 81 gyLPQE----ASifrkLTVEDNILAVLelrKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVeiarAL---AT 153
|
170
....*....|....*.
gi 1726007896 210 KPsKLLILDEPTVGMD 225
Cdd:COG1137 154 NP-KFILLDEPFAGVD 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
74-249 |
2.55e-19 |
|
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: 85.88 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNP-----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGnIIP----DKGSVVkhFNAQD------ 138
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPppgiTSGEIL--FDGEDllklse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 ---------DLSVMTQE--NCLIASLKVREQIALSLKIYDAYSKINID----DLLKKFRLTEQSEVIVD---QLSGGQKR 200
Cdd:COG0444 78 kelrkirgrEIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEAReraiELLERVGLPDPERRLDRyphELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 201 R----LALLLtliKPsKLLILDEPTVGMDLeSI-----DLFWDYLDHVGGSVVTITHD 249
Cdd:COG0444 158 RvmiaRALAL---EP-KLLIADEPTTALDV-TIqaqilNLLKDLQRELGLAILFITHD 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
73-266 |
2.72e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSV 142
Cdd:PRK11231 1 MTLRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpISMLSSRQlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASLKVREQIA------LSLkiydaYSKINIDD------LLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIK 210
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAygrspwLSL-----WGRLSAEDnarvnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 211 PSKLLILDEPTVGMDL----ESIDLFWDyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK11231 156 DTPVVLLDEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-285 |
5.74e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 84.01 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF---KnpVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNaQDDLSVMTQENclI 150
Cdd:COG4674 10 ILYVEDLTVSFdgfK--ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVL--FG-GTDLTGLDEHE--I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 151 A---------------SLKVREQIALSLKIY-----------DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLAL 204
Cdd:COG4674 83 ArlgigrkfqkptvfeELTVFENLELALKGDrgvfaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 205 LLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGG--SVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQ 282
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPR 242
|
...
gi 1726007896 283 TIE 285
Cdd:COG4674 243 VIE 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
75-268 |
2.05e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.83 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnkSF----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNaQDDL---- 140
Cdd:COG1132 340 IEFENV--SFsypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdIRDLT-LESLrrqi 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIaSLKVREQIALSLK------IYDAYSKINIDDLLKKF------RLTEQSEvivdQLSGGQKRRLALLLTL 208
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYGRPdatdeeVEEAAKAAQAHEFIEALpdgydtVVGERGV----NLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 209 IKPSKLLILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNyFTRVVLLKDGVI 268
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
74-248 |
2.20e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV--------KHFNAQDDLSVMT 144
Cdd:PRK13537 7 PIDFRNVEKRYgDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREqialSLKIYDAYSKIN-------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:PRK13537 87 QFDNLDPDFTVRE----NLLVFGRYFGLSaaaaralVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1726007896 218 DEPTVGMDLESIDLFWDYLDHV---GGSVVTITH 248
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLlarGKTILLTTH 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
73-268 |
2.56e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 84.56 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-------VKHFnAQD------ 138
Cdd:PRK15064 318 NALEVENLTKGFdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanIGYY-AQDhaydfe 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 -DLSVM------TQENCLIASlkVREQIALSLkiydaYSKiniDDLLKKfrlteqseviVDQLSGGQKRRLAL-LLTLIK 210
Cdd:PRK15064 397 nDLTLFdwmsqwRQEGDDEQA--VRGTLGRLL-----FSQ---DDIKKS----------VKVLSGGEKGRMLFgKLMMQK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 211 PSkLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLK-DGVI 268
Cdd:PRK15064 457 PN-VLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITpDGVV 514
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
73-258 |
2.89e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.62 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSFKNPVL-KDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-------VKHFN----AQD-D 139
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLvKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtkleVAYFDqhraELDpE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 LSVMtqENclIASLKV------REQIALSlkiydaYskinIDDLL---KKFRLTeqseviVDQLSGGQKRRLALLLTLIK 210
Cdd:PRK11147 398 KTVM--DN--LAEGKQevmvngRPRHVLG------Y----LQDFLfhpKRAMTP------VKALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHDFNQIDNYFT 258
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
74-255 |
3.77e-18 |
|
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: 84.22 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF--KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGniipdkgsVVKHFN----AQDDLSV--MTQ 145
Cdd:TIGR03719 4 IYTMNRVSKVVppKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKDFNgearPQPGIKVgyLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSLK-----------IYDAYSKINID-DLLkkfrLTEQSEV------------------------ 189
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAeikdaldrfneISAKYAEPDADfDKL----AAEQAELqeiidaadawdldsqleiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 190 ------IVDQLSGGQKRRLALL-LTLIKPSkLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHDFNQIDN 255
Cdd:TIGR03719 152 cppwdaDVTKLSGGERRRVALCrLLLSKPD-MLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
93-225 |
5.79e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 93 NLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV----VKHFN---AQDDLSVMTQENCLIASLKVREQIAL---- 161
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngQDHTTtppSRRPVSMLFQENNLFSHLTVAQNIGLglnp 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 162 SLKIyDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:PRK10771 99 GLKL-NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
100-271 |
7.22e-18 |
|
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: 80.03 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 100 DRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQ--DD-------------LSVMTQENCLIASLKVREQIALSLK 164
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV--LNGTvlFDsrkkinlppqqrkIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 165 IY-DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLD----HV 239
Cdd:cd03297 102 RKrNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKqikkNL 181
|
170 180 190
....*....|....*....|....*....|..
gi 1726007896 240 GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSD 271
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
74-268 |
9.77e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.21 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---------KHFNAQDDL 140
Cdd:cd03248 11 IVKFQNVTFAYPTrpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqyEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASlKVREQIALSL------KIYDAYSKINIDDLLKKFRLTEQSEV--IVDQLSGGQKRRLALLLTLIKPS 212
Cdd:cd03248 91 SLVGQEPVLFAR-SLQDNIAYGLqscsfeCVKEAAQKAHAHSFISELASGYDTEVgeKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 213 KLLILDEPTVGMDLESIDLFWD--YLDHVGGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
73-225 |
1.01e-17 |
|
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: 80.01 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSFKNP-----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDK---------GSVVKHFNAQD 138
Cdd:cd03234 2 RVLPWWDVGLKAKNWnkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsgqilfnGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 DLSVMTQENCLIASLKVRE------QIALSLKIYDAY-SKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:cd03234 82 CVAYVRQDDILLPGLTVREtltytaILRLPRKSSDAIrKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170
....*....|....
gi 1726007896 212 SKLLILDEPTVGMD 225
Cdd:cd03234 162 PKVLILDEPTSGLD 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
71-277 |
1.17e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 71 DALILELKNLNKSF-KNPVLKDVNLSIYgRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQDDL-- 140
Cdd:COG1129 1 AEPLLEMRGISKSFgGVKALDGVSLELR-PGEVhALLGENGAGKSTLMKILSGVYQPDSGEIlldgepVRFRSPRDAQaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 --SVMTQENCLIASLKVREQIAL-----SLKIYDaYSKINID--DLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:COG1129 80 giAIIHQELNLVPNLSVAENIFLgreprRGGLID-WRAMRRRarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 212 SKLLILDEPTVGMDL-ESIDLFwdylDHV------GGSVVTITHDFNQI----DnyftRVVLLKDGVIKSDESVANI 277
Cdd:COG1129 159 ARVLILDEPTASLTErEVERLF----RIIrrlkaqGVAIIYISHRLDEVfeiaD----RVTVLRDGRLVGTGPVAEL 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
75-249 |
3.14e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.14 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAqdDLSVM 143
Cdd:COG4525 4 LTVRHVSVRYpgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpVTGPGA--DRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIASLKVREQIALSLKIY---DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRgvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190
....*....|....*....|....*....|...
gi 1726007896 221 TVGMDL---ESI-DLFWDYLDHVGGSVVTITHD 249
Cdd:COG4525 162 FGALDAltrEQMqELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
75-268 |
3.53e-17 |
|
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: 77.95 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGN--IIPDKGSVVkhFNAQDDLSVMTQEnclia 151
Cdd:cd03217 1 LEIKDLHVSVgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEIL--FKGEDITDLPPEE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 slKVREQIALSLKIYDAYSKINIDDLLKKfrlteqsevIVDQLSGGQKRRLALL-LTLIKPsKLLILDEPTVGMDLESID 230
Cdd:cd03217 74 --RARLGIFLAFQYPPEIPGVKNADFLRY---------VNEGFSGGEKKRNEILqLLLLEP-DLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1726007896 231 L---FWDYLDHVGGSVVTITHdFNQIDNYF--TRVVLLKDGVI 268
Cdd:cd03217 142 LvaeVINKLREEGKSVLIITH-YQRLLDYIkpDRVHVLYDGRI 183
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
91-279 |
3.55e-17 |
|
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: 80.54 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 91 DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKH----FNA---------QDDLSVMTQENCLIASLKVRE 157
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlFDSrkgiflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 158 QIALSLKIYDA-YSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYL 236
Cdd:TIGR02142 95 NLRYGMKRARPsERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1726007896 237 ----DHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:TIGR02142 175 erlhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
75-268 |
3.79e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.12 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDDLSVMTQE-NclIA- 151
Cdd:COG3839 4 LELENVSKSYgGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI--LIGGRDVTDLPPKDrN--IAm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 ---------SLKVREQIALSLKI--YDAySKIN--IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:COG3839 80 vfqsyalypHMTVYENIAFPLKLrkVPK-AEIDrrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 219 EPT--------VGMDLESIDLFwdylDHVGGSVVTITHDfnQI------DnyftRVVLLKDGVI 268
Cdd:COG3839 159 EPLsnldaklrVEMRAEIKRLH----RRLGTTTIYVTHD--QVeamtlaD----RIAVMNDGRI 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
76-277 |
3.85e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFKN-PVLKDVNLSIyGRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVMT 144
Cdd:COG4604 3 EIKNVSKRYGGkVVLDDVSLTI-PKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldVATTPSRElakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIA----------LSLKIYDAyskinIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKL 214
Cdd:COG4604 82 QENHINSRLTVRELVAfgrfpyskgrLTAEDREI-----IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 215 LILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANI 277
Cdd:COG4604 157 VLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
74-273 |
4.40e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.38 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD-DLSVMTQ 145
Cdd:PRK09452 14 LVELRGISKSFDgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdITHVPAENrHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSL---KIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLrmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 223 GMD--------LEsidlfwdyLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDES 273
Cdd:PRK09452 174 ALDyklrkqmqNE--------LKALqrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
104-279 |
5.37e-17 |
|
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: 79.46 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 104 LLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------DLSVMTQENCLIASLKVREQIALSLKIyDAYSKINI 174
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM--LDGEDvtnvpphlrHINMVFQSYALFPHMTVEENVAFGLKM-RKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 175 D----DLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFW----DYLDHVGGSVVTI 246
Cdd:TIGR01187 78 KprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlelkTIQEQLGITFVFV 157
|
170 180 190
....*....|....*....|....*....|...
gi 1726007896 247 THDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
87-248 |
6.52e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQ------ENCLIASLKVREQIA 160
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAySKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWD-YLDHV 239
Cdd:PRK13539 96 FWAAFLGG-EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAElIRAHL 174
|
170
....*....|.
gi 1726007896 240 --GGSVVTITH 248
Cdd:PRK13539 175 aqGGIVIAATH 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
75-225 |
8.64e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIV-------NTILGNIIPDKGSVVKHFNAQDDLSVMTQE 146
Cdd:PRK11432 7 VVLKNITKRFgSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLrlvagleKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 NCLIASLKVREQIALSLK---IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVG 223
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKmlgVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
..
gi 1726007896 224 MD 225
Cdd:PRK11432 167 LD 168
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
75-268 |
9.05e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 80.15 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSvmtqenclIA 151
Cdd:TIGR02203 331 VEFRNVTFRYPGrdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--------LA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 SLkvREQIAL-------------------------SLKIYDAYSKINIDDLLKKFRLTEQSEVIVD--QLSGGQKRRLAL 204
Cdd:TIGR02203 403 SL--RRQVALvsqdvvlfndtianniaygrteqadRAEIERALAAAYAQDFVDKLPLGLDTPIGENgvLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 205 LLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKA-DRIVVMDDGRI 545
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
75-266 |
9.28e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFkNPV--LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFN-------AQDDLSV 142
Cdd:PRK09700 6 ISMAGIGKSF-GPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinnINYNkldhklaAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASLKVREQIALSLKIYDAYSKINIDD----------LLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPS 212
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDwremrvraamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 213 KLLILDEPTVGMDLESID-LFW--DYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDyLFLimNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
85-268 |
1.13e-16 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 77.27 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVMTQENCLIaSLKV 155
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdVRDYTLASlrrQIGLVSQDVFLF-NDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALSL------KIYDAYSKINIDDLLKkfRLTEQSEVIVD----QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:cd03251 93 AENIAYGRpgatreEVEEAARAANAHEFIM--ELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 226 LESIDLFWDYLDH--VGGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:cd03251 171 TESERLVQAALERlmKNRTTFVIAHRLSTIENA-DRIVVLEDGKI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
75-268 |
1.24e-16 |
|
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: 77.34 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDDLSV---------- 142
Cdd:cd03295 1 IEFENVTKRYGGgkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF--IDGEDIREQdpvelrrkig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 -MTQENCLIASLKVREQIALSLKIyDAYSKINI----DDLLKKFRLTEQS--EVIVDQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:cd03295 79 yVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIreraDELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 216 ILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDfnqIDNYF---TRVVLLKDGVI 268
Cdd:cd03295 158 LMDEPFGALDpitrDQLQEEFKRLQQELGKTIVFVTHD---IDEAFrlaDRIAIMKNGEI 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
77-266 |
1.51e-16 |
|
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: 80.06 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 77 LKNLNKSFK---NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFNAQDD-----LSVMTQ 145
Cdd:TIGR01257 931 VKNLVKIFEpsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggKDIETNLDavrqsLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQI----ALSLKIYDAySKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:TIGR01257 1011 HNILFHHLTVAEHIlfyaQLKGRSWEE-AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1726007896 222 VGMDLESIDLFWDYL--DHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
74-249 |
1.56e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF--KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGniipdkgsVVKHFN----AQDDLSV--MTQ 145
Cdd:PRK11819 6 IYTMNRVSKVVppKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKEFEgearPAPGIKVgyLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSLK-----------IYDAYS--KINIDDLLKKF-RLTEQ------------------------S 187
Cdd:PRK11819 78 EPQLDPEKTVRENVEEGVAevkaaldrfneIYAAYAepDADFDALAAEQgELQEIidaadawdldsqleiamdalrcppW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 188 EVIVDQLSGGQKRRLAL--LLtLIKPSkLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHD 249
Cdd:PRK11819 158 DAKVTKLSGGERRRVALcrLL-LEKPD-MLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
1-66 |
1.76e-16 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 72.72 E-value: 1.76e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 1 MENIFKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAG 66
Cdd:COG1396 4 LKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELLGG 69
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
88-248 |
1.79e-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: 75.99 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQENCL----IASLKVREQIALSL 163
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLylghAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 164 KIYDAY-SKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYL-DHV-- 239
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCar 174
|
....*....
gi 1726007896 240 GGSVVTITH 248
Cdd:cd03231 175 GGMVVLTTH 183
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
76-268 |
2.01e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 76.81 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSF----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQ---DDLSV 142
Cdd:cd03249 2 EFKNVSFRYpsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdIRDLNLRwlrSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASlKVREQIALSLK------IYDAYSKINIDDLLKKfrLTEQSEVIV----DQLSGGQKRRLALLLTLIKPS 212
Cdd:cd03249 82 VSQEPVLFDG-TIAENIRYGKPdatdeeVEEAAKKANIHDFIMS--LPDGYDTLVgergSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 213 KLLILDEPTVGMDLESIDLFWDYLD--HVGGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDraMKGRTTIVIAHRLSTIRNA-DLIAVLQNGQV 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
89-266 |
2.67e-16 |
|
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: 76.35 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQD----DLSVMTQENCLIASLKVREQIALSLK 164
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 165 -----IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTL-IKPsKLLILDEPTVGMDLESIDLFWDYLDH 238
Cdd:TIGR01184 81 rvlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALsIRP-KVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 1726007896 239 V----GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:TIGR01184 160 IweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
85-269 |
2.81e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---------KHFNAQDDLSVMTQENCLIaSLKV 155
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqyDHHYLHRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALSLKIYD------AYSKINIDDLLKKFRLTEQSEV--IVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE 227
Cdd:TIGR00958 572 RENIAYGLTDTPdeeimaAAKAANAHDFIMEFPNGYDTEVgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1726007896 228 SIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:TIGR00958 652 CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
74-223 |
3.00e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.17 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIyGRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD------------D 139
Cdd:COG0410 3 MLEVENLHAGYgGIHVLHGVSLEV-EEGEIvALLGRNGAGKTTLLKAISGLLPPRSGSI--RFDGEDitglpphriarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 LSVMTQENCLIASLKVREQIALSLKIYDAYSKI--NIDDLLKKF-RLTEQSEVIVDQLSGGQKRRLAL---LLTliKPsK 213
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVraDLERVYELFpRLKERRRQRAGTLSGGEQQMLAIgraLMS--RP-K 156
|
170
....*....|
gi 1726007896 214 LLILDEPTVG 223
Cdd:COG0410 157 LLLLDEPSLG 166
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-280 |
4.29e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNPV----------------------LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV- 130
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 131 VKHFNAQDDLS--------VMTQENCLIASLKVREQIALSLKIYD----AYSKiNIDDLLKKFRLTEQSEVIVDQLSGGQ 198
Cdd:COG4586 81 VLGYVPFKRRKefarrigvVFGQRSQLWWDLPAIDSFRLLKAIYRipdaEYKK-RLDELVELLDLGELLDTPVRQLSLGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 199 KRRLALLLTLI-KPsKLLILDEPTVGMDLESIDLFWDYLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDES 273
Cdd:COG4586 160 RMRCELAAALLhRP-KILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
....*..
gi 1726007896 274 VANIHSN 280
Cdd:COG4586 239 LEELKER 245
|
|
| XRE |
COG1476 |
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription]; |
1-66 |
6.67e-16 |
|
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
Pssm-ID: 441085 [Multi-domain] Cd Length: 68 Bit Score: 70.65 E-value: 6.67e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 1 MENIFKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAG 66
Cdd:COG1476 1 MKKKLGNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSL 66
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
75-271 |
8.42e-16 |
|
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: 77.21 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSV 142
Cdd:TIGR03375 464 IEFRNVSFAYPGqetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdIRQIDPADlrrNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASlKVREQIALSlkiyDAYskINIDDLLKKFRLTEQSEVIV--------------DQLSGGQKRRLALLLTL 208
Cdd:TIGR03375 544 VPQDPRLFYG-TLRDNIALG----APY--ADDEEILRAAELAGVTEFVRrhpdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 209 IKPSKLLILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDfNQIDNYFTRVVLLKDGVIKSD 271
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWlaGKTLVLVTHR-TSLLDLVDRIIVMDNGRIVAD 680
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
88-268 |
8.90e-16 |
|
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: 74.83 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-----------KHFNAQddLSVMTQENCLIaSLKVR 156
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdghdlaladpAWLRRQ--VGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIALS------LKIYDAYSKINIDDLLKKfrLTEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:cd03252 94 DNIALAdpgmsmERVIEAAKLAGAHDFISE--LPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1726007896 227 ESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:cd03252 172 ESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNA-DRIIVMEKGRI 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
87-268 |
1.07e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIiPDKGSV-----------VKHFNAQddLSVMTQENCLIASlKV 155
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielreldPESWRKH--LSWVGQNPQLPHG-TL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALS------LKIYDAYSKINIDDLLKKFRLTEQSEvIVDQ---LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:PRK11174 440 RDNVLLGnpdasdEQLQQALENAWVSEFLPLLPQGLDTP-IGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1726007896 227 ESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:PRK11174 519 HSEQLVMQALNAAsrRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
75-282 |
1.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF--KNP----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQENC 148
Cdd:PRK13651 3 IKVKNIVKIFnkKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLKVREQIALSLKiydayskiNIDDLLKK------------FRLTEQSEVI-------------------------V 191
Cdd:PRK13651 83 VLEKLVIQKTRFKKIK--------KIKEIRRRvgvvfqfaeyqlFEQTIEKDIIfgpvsmgvskeeakkraakyielvgL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 192 DQ---------LSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----LESIDLFwDYLDHVGGSVVTITHDFNQIDNYFT 258
Cdd:PRK13651 155 DEsylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTK 233
|
250 260
....*....|....*....|....
gi 1726007896 259 RVVLLKDGVIKSDESVANIHSNNQ 282
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
76-270 |
1.22e-15 |
|
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: 74.18 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSF--KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV---------VKHFNAQDDLSVMT 144
Cdd:cd03254 4 EFENVNFSYdeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENcLIASLKVREQIALSL------KIYDAYSKINIDDLLKKfrLTEQSEVIV----DQLSGGQKRRLALLLTLIKPSKL 214
Cdd:cd03254 84 QDT-FLFSGTIMENIRLGRpnatdeEVIEAAKEAGAHDFIMK--LPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 215 LILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVIKS 270
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNA-DKILVLDDGKIIE 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
75-268 |
1.51e-15 |
|
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: 74.14 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI-----LGNIIPDKGSVvkHFNAQDDLSVMTQENC 148
Cdd:cd03260 1 IELRDLNVYYgDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEV--LLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 L---IA---------SLKVREQIALSLKIYDAYSKINIDDL----LKKFRLTEqsEV----IVDQLSGGQKRRLALLLTL 208
Cdd:cd03260 79 LrrrVGmvfqkpnpfPGSIYDNVAYGLRLHGIKLKEELDERveeaLRKAALWD--EVkdrlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 209 IKPSKLLILDEPTVGMDLES--------IDLFWDYldhvggSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPIStakieeliAELKKEY------TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
74-275 |
1.82e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNP-----------------------VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV 130
Cdd:COG1134 4 MIEVENVSKSYRLYhepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 131 VKH------------FNAqdDLSVMtqENC-LIASL--KVREQIAlslKIYDAyskinIDDL--LKKFrlteqseviVDQ 193
Cdd:COG1134 84 EVNgrvsallelgagFHP--ELTGR--ENIyLNGRLlgLSRKEID---EKFDE-----IVEFaeLGDF---------IDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 194 ----LSGGQKRRLAL-LLTLIKPsKLLILDEPTVGMDLE----SIDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLK 264
Cdd:COG1134 143 pvktYSSGMRARLAFaVATAVDP-DILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|.
gi 1726007896 265 DGVIKSDESVA 275
Cdd:COG1134 221 KGRLVMDGDPE 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
74-268 |
2.13e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLS----------V 142
Cdd:PRK15439 11 LLCARSISKQYSGvEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakahqlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASLKVREQIALSL-KIYDAYSKinIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLpKRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1726007896 222 VGMD-LESIDLFWDY--LDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK15439 169 ASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
70-249 |
2.52e-15 |
|
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: 75.74 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 70 GDaLILELKNLNKSFKNPVL-KDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDDLSVMTQE-N 147
Cdd:TIGR03719 319 GD-KVIEAENLTKAFGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--IGETVKLAYVDQSrD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 148 CLIASLKVREQIALSLKIYD---------AY-SKINiddllkkFRLTEQSEvIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKlgkreipsrAYvGRFN-------FKGSDQQK-KVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|..
gi 1726007896 218 DEPTVGMDLESIDLFWDYLDHVGGSVVTITHD 249
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHD 499
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
75-270 |
2.84e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.56 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNiiPD----KGSVvkHFNAQD--DLSV----- 142
Cdd:COG0396 1 LEIKNLHVSVEGkEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKyevtSGSI--LLDGEDilELSPderar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ---------------MTQENCLIASLKVREQIALSL-----KIYDAYSKINID-DLLKKfrlteqsEVIVDqLSGGQKRR 201
Cdd:COG0396 77 agiflafqypveipgVSVSNFLRTALNARRGEELSAreflkLLKEKMKELGLDeDFLDR-------YVNEG-FSGGEKKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 202 LALL-LTLIKPsKLLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITH-----DFNQIDnyftRVVLLKDG-VIKS 270
Cdd:COG0396 149 NEILqMLLLEP-KLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHyqrilDYIKPD----FVHVLVDGrIVKS 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
75-268 |
3.16e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG------NIIPDKGSVVKHFNAQD-DLSVMTQE 146
Cdd:PRK10851 3 IEIANIKKSFgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsGHIRFHGTDVSRLHARDrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 NCLIASLKVREQIALSLKIY-------DAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVLprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 220 P------TVGMDLESidlfWDYLDH--VGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK10851 163 PfgaldaQVRKELRR----WLRQLHeeLKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
75-274 |
4.22e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKH----FNAQDDLSVMTQENCL 149
Cdd:PRK11247 13 LLLNAVSKRYgERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGtaplAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 IASLKVREQIALSLK------IYDAYSKINIDDllkkfRLTEQSEVivdqLSGGQKRRLALLLTLIKPSKLLILDEPTVG 223
Cdd:PRK11247 93 LPWKKVIDNVGLGLKgqwrdaALQALAAVGLAD-----RANEWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 224 MD----LESIDL---FWdyLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESV 274
Cdd:PRK11247 164 LDaltrIEMQDLiesLW--QQH-GFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTV 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
84-270 |
4.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 84 FKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnaQDDLSVMTQ-ENCLIASlkVREQIALS 162
Cdd:PRK13649 18 FEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR-----VDDTLITSTsKNKDIKQ--IRKKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 LKIydAYSKINIDDLLK----------------------KFRLTEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLI 216
Cdd:PRK13649 91 FQF--PESQLFEETVLKdvafgpqnfgvsqeeaealareKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 217 LDEPTVGMD----LESIDLFwDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG-VIKS 270
Cdd:PRK13649 169 LDEPTAGLDpkgrKELMTLF-KKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGkLVLS 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
62-268 |
4.89e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.86 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 62 FLLAGHTHGDALILELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VK 132
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpIA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 133 HFNAQD---DLSVMTQ----------ENCLIASLKVREQialslKIYDAYSKINIDDLLkkfrlteQSEVIVD------- 192
Cdd:PRK11160 406 DYSEAAlrqAISVVSQrvhlfsatlrDNLLLAAPNASDE-----ALIEVLQQVGLEKLL-------EDDKGLNawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 193 -QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLES----IDLFwdyLDHVGG-SVVTITHDFNQIDNyFTRVVLLKDG 266
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELL---AEHAQNkTVLMITHRLTGLEQ-FDRICVMDNG 549
|
..
gi 1726007896 267 VI 268
Cdd:PRK11160 550 QI 551
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
85-268 |
5.23e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD---DLSVMTQENCLIASLKV 155
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehIQHYASKEvarRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALS----LKIYDAYSKINIDDLLKKFRLTEQSEVI---VDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL-E 227
Cdd:PRK10253 99 QELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLAdqsVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 228 SIDLFwDYLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK10253 179 QIDLL-ELLSELnrekGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
72-266 |
6.78e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 72 ALILELKNLNKSFkNPV--LKDVNLSIYgRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQD--DL 140
Cdd:COG3845 3 PPALELRGITKRF-GGVvaNDDVSLTVR-PGEIhALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpVRIRSPRDaiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SV-MT-QENCLIASLKVREQIALSLKIyDAYSKIN-------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:COG3845 81 GIgMVhQHFMLVPNLTVAENIVLGLEP-TKGGRLDrkaararIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 212 SKLLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
74-271 |
7.65e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.38 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNtILGNIipDKGSVVKHFNAQDDlsVMTQENC 148
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL--DKPTSGTYRVAGQD--VATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLKvREQIALSLKIYDAYSKI----NID------------------DLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:PRK10535 79 ALAQLR-REHFGFIFQRYHLLSHLtaaqNVEvpavyaglerkqrllraqELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 207 TLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDfNQIDNYFTRVVLLKDGVIKSD 271
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLrdrGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
74-285 |
8.45e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKH-----FNAQDDL 140
Cdd:PRK13639 1 ILETRDLKYSYPDgtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepIKYdkkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQ--ENCLIASlKVREQIA---LSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 216 ILDEPTVGMD----LESIDLFWDyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:PRK13639 160 VLDEPTSGLDpmgaSQIMKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
75-268 |
9.99e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIlgNI--IPDKGS---------------------- 129
Cdd:COG4161 3 IQLKNINCFYgSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLleTPDSGQlniaghqfdfsqkpsekairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 130 ------VVKHFNAQDDLSVMtqENCLIASLKVreqialsLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLA 203
Cdd:COG4161 81 rqkvgmVFQQYNLWPHLTVM--ENLIEAPCKV-------LGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 204 LLLTLIKPSKLLILDEPTVGMDLE------SIDLfwdYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEitaqvvEIIR---ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
74-280 |
1.08e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI-------LGNIIPD-----------------KG 128
Cdd:PRK09493 1 MIEFKNVSKHFgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDglkvndpkvderlirqeAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 129 SVVKHFNAQDDLSVMtqENCLIASLKVR-------EQIALslkiydayskinidDLLKKFRLTEQSEVIVDQLSGGQKRR 201
Cdd:PRK09493 81 MVFQQFYLFPHLTAL--ENVMFGPLRVRgaskeeaEKQAR--------------ELLAKVGLAERAHHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 202 LALLLTL-IKPsKLLILDEPTVGMD----LESIDLFWDyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVAN 276
Cdd:PRK09493 145 VAIARALaVKP-KLMLFDEPTSALDpelrHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
....
gi 1726007896 277 IHSN 280
Cdd:PRK09493 223 LIKN 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
74-248 |
1.34e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD---DLSVMTQENCL 149
Cdd:PRK13540 1 MLDVIELDFDYHDqPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI--LFERQSikkDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 IA-------SLKVREQIALSlkIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:PRK13540 79 VGhrsginpYLTLRENCLYD--IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180
....*....|....*....|....*....
gi 1726007896 223 GMDLESIDLFWDYLDH---VGGSVVTITH 248
Cdd:PRK13540 157 ALDELSLLTIITKIQEhraKGGAVLLTSH 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
72-268 |
1.39e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 72 ALILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMT------ 144
Cdd:PRK09536 1 MPMIDVSDLSVEFGDtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasrrva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 ---QENCLIASLKVREQIALSLKIYDA-YSKINIDDLLKKFRLTEQSEVI------VDQLSGGQKRRLALLLTLIKPSKL 214
Cdd:PRK09536 81 svpQDTSLSFEFDVRQVVEMGRTPHRSrFDTWTETDRAAVERAMERTGVAqfadrpVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 215 LILDEPTVGMDL----ESIDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK09536 161 LLLDEPTASLDInhqvRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
74-282 |
1.42e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV----------KHFNAQDDLSV 142
Cdd:PRK10895 3 TLTAKNLAKAYKGrRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllpLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQENCLIASLKVREQIALSLKIYDAYS----KINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSaeqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 219 EPTVGMD-LESIDL--FWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQ 282
Cdd:PRK10895 163 EPFAGVDpISVIDIkrIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
74-266 |
2.49e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLS----VMTQENC 148
Cdd:PRK11248 1 MLQISHLYADYGgKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGaergVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLKVREQIALSLK---IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 226 LESIDLFWDYLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK11248 161 AFTREQMQTLLLKLwqetGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
74-285 |
2.59e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFnaqddlsVMTQENCl 149
Cdd:PRK13635 5 IIRVEHISFRYPDaatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItVGGM-------VLSEETV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 iasLKVREQIALSLKIYD------------AYSKIN-----------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:PRK13635 77 ---WDVRRQVGMVFQNPDnqfvgatvqddvAFGLENigvpreemverVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 207 TLIKPSKLLILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKSDESVANIHSNNQ 282
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEIFKSGH 232
|
...
gi 1726007896 283 TIE 285
Cdd:PRK13635 233 MLQ 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
74-285 |
3.24e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFknP---VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-----KHFNAQDD-----L 140
Cdd:PRK10762 4 LLQLKGIDKAF--PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkeVTFNGPKSsqeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALSLKIYDAYSKIN-------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSK 213
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDwkkmyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 214 LLILDEPTVGM-DLESIDLF--WDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIhSNNQTIE 285
Cdd:PRK10762 162 VIIMDEPTDALtDTETESLFrvIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL-TEDSLIE 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
75-225 |
3.65e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK--NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLS--------VMT 144
Cdd:PRK10790 341 IDIDNVSFAYRddNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrqgvAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIASLKVREQIALSL-----KIYDAYSKINIDDLLKKF------RLTEQSevivDQLSGGQKRRLALLLTLIKPSK 213
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRdiseeQVWQALETVQLAELARSLpdglytPLGEQG----NNLSVGQKQLLALARVLVQTPQ 496
|
170
....*....|..
gi 1726007896 214 LLILDEPTVGMD 225
Cdd:PRK10790 497 ILILDEATANID 508
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
74-266 |
3.85e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD-DLS--------- 141
Cdd:PRK13636 5 ILKVEELNYNYSDgtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL--FDGKPiDYSrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 ----VMTQENCLIASLKVREQI---ALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKL 214
Cdd:PRK13636 83 svgmVFQDPDNQLFSASVYQDVsfgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 215 LILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK13636 163 LVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
75-269 |
3.98e-14 |
|
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: 69.83 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK---NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV------KHFNAQD---DLSV 142
Cdd:cd03244 3 IEFKNVSLRYRpnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiSKIGLHDlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 MTQEnCLIASLKVRE-----QIALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVD--QLSGGQKRRLALLLTLIKPSKLL 215
Cdd:cd03244 83 IPQD-PVLFSGTIRSnldpfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 216 ILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVIK 269
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
75-272 |
4.80e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.87 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKNP-----------------------VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV 131
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 KH--------FNA--QDDLSVMtqEN----CLIASLKVREQIALSLKIYDayskiniddllkkfrLTEQSEVI---VDQL 194
Cdd:cd03220 81 VRgrvssllgLGGgfNPELTGR--ENiylnGRLLGLSRKEIDEKIDEIIE---------------FSELGDFIdlpVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 195 SGGQKRRLALLLTLIKPSKLLILDEPT-VGmD----LESIDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLaVG-DaafqEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
...
gi 1726007896 270 SDE 272
Cdd:cd03220 222 FDG 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
95-266 |
4.94e-14 |
|
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: 70.13 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 95 SIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfnAQDDLSVMTQEncLIASLKVREQIALSLKIYDAYS---- 170
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQY--IKADYEGTVRDLLSSITKDFYThpyf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 171 KINIDDLLKKFRLTEQSeviVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLES-------IDLFwdyLDHVGGSV 243
Cdd:cd03237 96 KTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmaskvIRRF---AENNEKTA 169
|
170 180
....*....|....*....|...
gi 1726007896 244 VTITHDFNQIDnYFTRVVLLKDG 266
Cdd:cd03237 170 FVVEHDIIMID-YLADRLIVFEG 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
75-268 |
8.46e-14 |
|
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: 68.01 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnkSF-----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnaQDDLSVMTqencl 149
Cdd:cd03246 1 LEVENV--SFrypgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----LDGADISQ----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 IASLKVREQIALSLKiydayskiniDDLLKKFRLTEQsevIvdqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESI 229
Cdd:cd03246 69 WDPNELGDHVGYLPQ----------DDELFSGSIAEN---I---LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 230 DLFWDYLDHV---GGSVVTITHD---FNQIDnyftRVVLLKDGVI 268
Cdd:cd03246 133 RALNQAIAALkaaGATRIVIAHRpetLASAD----RILVLEDGRV 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
88-275 |
9.47e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.72 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDdlsvmtqenclIASLKVREQIA----LSL 163
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS--WRGEP-----------LAKLNRAQRKAfrrdIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 164 KIYDAYSKIN---------------IDDLLKKFRLTEQSEVI--VD-----------QLSGGQKRRLALLLTLIKPSKLL 215
Cdd:PRK10419 94 VFQDSISAVNprktvreiireplrhLLSLDKAERLARASEMLraVDlddsvldkrppQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 216 ILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVA 275
Cdd:PRK10419 174 ILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVG 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
73-225 |
1.04e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.35 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIP--DKGSV-VKHFNAQDDLS------VM 143
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlINGRPLDKRSFrkiigyVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 tQENCLIASLKVREQIALSLKIydayskiniddllkkfrlteqsevivDQLSGGQKRRLALLLTLI-KPSkLLILDEPTV 222
Cdd:cd03213 89 -QDDILHPTLTVRETLMFAAKL--------------------------RGLSGGERKRVSIALELVsNPS-LLFLDEPTS 140
|
...
gi 1726007896 223 GMD 225
Cdd:cd03213 141 GLD 143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
74-268 |
1.28e-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: 70.60 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNK---SFKNPVLK---DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDDLSVMT--- 144
Cdd:TIGR03269 279 IIKVRNVSKryiSVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV--NVRVGDEWVDMTkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 ---------------QENCLIASLKVREQI--ALSLKIYDAYSKINIDDLLKKFRLTEQSEVIV-----DQLSGGQKRRL 202
Cdd:TIGR03269 357 pdgrgrakryigilhQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 203 ALLLTLIKPSKLLILDEPTVGMD-------LESIdlfWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSI---LKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
87-270 |
1.63e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV----------------------------------K 132
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarlqqdpprnvegtvydfvaegieeqaE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 133 HFNAQDDLSVMTQENCLIASLKVREQIALSLKIYDAY---SKINidDLLKKFRLTEQSEVivDQLSGGQKRRLALLLTLI 209
Cdd:PRK11147 97 YLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWqleNRIN--EVLAQLGLDPDAAL--SSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 210 KPSKLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
80-279 |
1.87e-13 |
|
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: 68.68 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 80 LNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--------------DLSVMTQ 145
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV--SFRGQDlyqldrkqrrafrrDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 E--NCLIASLKVREQIALSLKIYDAYSKI----NIDDLLKKFRL-TEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:TIGR02769 96 DspSAVNPRMTVRQIIGEPLRHLTSLDESeqkaRIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 219 EPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:TIGR02769 176 EAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| aMBF1 |
COG1813 |
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ... |
5-61 |
2.08e-13 |
|
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441418 [Multi-domain] Cd Length: 70 Bit Score: 64.19 E-value: 2.08e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 5 FKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLD 61
Cdd:COG1813 13 YGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISLA 69
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
59-225 |
2.10e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 59 NLDFLLAGHTHGDALIL----ELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPD-KGSVVKH 133
Cdd:TIGR00955 7 NSDVFGRVAQDGSWKQLvsrlRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 134 FNAQD-DLSVMT-------QENCLIASLKVREQIALS--LKIYDAYSKIN----IDDLLKKFRLTE------QSEVIVDQ 193
Cdd:TIGR00955 87 LNGMPiDAKEMRaisayvqQDDLFIPTLTVREHLMFQahLRMPRRVTKKEkrerVDEVLQALGLRKcantriGVPGRVKG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1726007896 194 LSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
72-268 |
2.29e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 72 ALILELKNLNKSFK--NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSvVKHFNaqddlSVMTQENCl 149
Cdd:PRK13647 2 DNIIEVEDLHFRYKdgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMG-----REVNAENE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 iasLKVREQIAL----------SLKIYD--AYSKIN-----------IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLL 206
Cdd:PRK13647 75 ---KWVRSKVGLvfqdpddqvfSSTVWDdvAFGPVNmgldkdeverrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 207 TLIKPSKLLILDEPTVGMD---LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
75-268 |
2.60e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI-------------------LGNIIPDK------- 127
Cdd:PRK11124 3 IQLNGINCFYgAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniagnhfdFSKTPSDKairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 128 --GSVVKHFNAQDDLSVMtqENCLIASLKVreqialsLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALL 205
Cdd:PRK11124 83 nvGMVFQQYNLWPHLTVQ--QNLIEAPCRV-------LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 206 LTLIKPSKLLILDEPTVGMDLE----SIDLFWDyLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEitaqIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
74-268 |
3.04e-13 |
|
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: 69.71 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG----NIIPDKGSVvkHFNAQDDLSV-- 142
Cdd:COG4172 6 LLSVEDLSVAFGQgggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSI--LFDGQDLLGLse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ------------------MTQENCLiasLKVREQIALSLKIYDAYSKIN----IDDLLKKFRLTEQSEVIVD---QLSGG 197
Cdd:COG4172 84 relrrirgnriamifqepMTSLNPL---HTIGKQIAEVLRLHRGLSGAAararALELLERVGIPDPERRLDAyphQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 198 QKRR----LALLLtliKPsKLLILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:COG4172 161 QRQRvmiaMALAN---EP-DLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
7-63 |
3.27e-13 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 62.96 E-value: 3.27e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 7 SQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFL 63
Cdd:cd00093 2 ERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
88-277 |
3.32e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTT-------IVNTILGNIIPDKGSVVK---HfNAQDDLSVMTQENCLIA-SLKVR 156
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSltlglfrINESAEGEIIIDGLNIAKiglH-DLRFKITIIPQDPVLFSgSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 ---------EQIALSLKIydAYSKINIDDLLKK--FRLTEQSEvivdQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:TIGR00957 1380 ldpfsqysdEEVWWALEL--AHLKTFVSALPDKldHECAEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 226 LESIDLFWDYL--DHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKSDESVANI 277
Cdd:TIGR00957 1454 LETDNLIQSTIrtQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
81-270 |
4.47e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 81 NKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfNAQDDLSVMTQENCLIASLKVREQIA 160
Cdd:PRK13643 14 NSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVGDIVVSSTSKQKEIKPVRKKVGVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAYSKINIDDLL---KKFRLT-EQSEVIVDQ------------------LSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:PRK13643 90 FQFPESQLFEETVLKDVAfgpQNFGIPkEKAEKIAAEklemvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 219 EPTVGMD----LESIDLFwDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK13643 170 EPTAGLDpkarIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
74-283 |
4.78e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.18 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNP-----VLKDVNLS-----IYGrdriaLLGSNGSGKTTIVNTIlgNII--PDKGSVV---------- 131
Cdd:COG1135 1 MIELENLSKTFPTKggpvtALDDVSLTiekgeIFG-----IIGYSGAGKSTLIRCI--NLLerPTSGSVLvdgvdltals 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 ---------------KHFNaqddlsvmtqencLIASLKVREQIALSLKIyDAYSKINI----DDLLKKFRLTEQSEVIVD 192
Cdd:COG1135 74 erelraarrkigmifQHFN-------------LLSSRTVAENVALPLEI-AGVPKAEIrkrvAELLELVGLSDKADAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 193 QLSGGQKRR------LALlltliKPsKLLILDEPTVGMDLE---SI-DLfwdyLDHV----GGSVVTITHDFNQIDNYFT 258
Cdd:COG1135 140 QLSGGQKQRvgiaraLAN-----NP-KVLLCDEATSALDPEttrSIlDL----LKDInrelGLTIVLITHEMDVVRRICD 209
|
250 260
....*....|....*....|....*
gi 1726007896 259 RVVLLKDGVIKSDESVANIHSNNQT 283
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
68-270 |
5.09e-13 |
|
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: 66.67 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 68 THGDaliLELKNLNKSFK---NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD------ 138
Cdd:cd03369 3 EHGE---IEVENLSVRYApdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI--EIDGIDistipl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 -----DLSVMTQENCLIASlkvreQIALSLKIYDAYSKiniDDLLKKFRLTEQSevivDQLSGGQKRRLALLLTLIKPSK 213
Cdd:cd03369 78 edlrsSLTIIPQDPTLFSG-----TIRSNLDPFDEYSD---EEIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 214 LLILDEPTVGMDLESIDLFWDYL--DHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKS 270
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIreEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
87-280 |
5.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.42 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDDLSVMT-----------QENCLIASLk 154
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyVDGLDTSDEENLWDirnkagmvfqnPDNQIVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VREQIAL---SLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----LE 227
Cdd:PRK13633 103 VEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrRE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 228 SIDLFWDYLDHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKSDESVANIHSN 280
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| HTH_3 |
pfam01381 |
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ... |
9-63 |
6.30e-13 |
|
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.
Pssm-ID: 460181 [Multi-domain] Cd Length: 55 Bit Score: 62.17 E-value: 6.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 9 LSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFL 63
Cdd:pfam01381 1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
73-249 |
6.41e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSFKNPVLKDvNLS-------IYGrdriaLLGSNGSGKTTIVNTILGNIIPDKGSV-----VKhfnaqddL 140
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLID-DLSfslppggIVG-----IIGPNGAGKSTLFKMITGQEQPDSGTIkigetVK-------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQE-NCLIASLKVREQIALSLKIYD---------AY-SKINiddllkkFRLTEQSEvIVDQLSGGQKRRLALLLTLI 209
Cdd:PRK11819 390 AYVDQSrDALDPNKTVWEEISGGLDIIKvgnreipsrAYvGRFN-------FKGGDQQK-KVGVLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1726007896 210 KPSKLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHD 249
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
74-266 |
9.10e-13 |
|
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: 66.30 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF--------KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDDL-SVM 143
Cdd:COG4778 4 LLEVENLSKTFtlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDGGWVDLaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQE----------------NCL--IASLKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQsevivdqL--------SGG 197
Cdd:COG4778 84 PREilalrrrtigyvsqflRVIprVSALDVVAEPLLERGVDREEARARARELLARLNLPER-------LwdlppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 198 QKRRLALLLTLIKPSKLLILDEPTVGMDLES----IDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
85-269 |
9.58e-13 |
|
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: 68.14 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNaQDDL--SV--MTQENCLIASlK 154
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadLKQWD-RETFgkHIgyLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VREQIAL------SLKIYDAYSKINIDDLLKKFRLTEQSEVIVD--QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:TIGR01842 408 VAENIARfgenadPEKIIEAAKLAGVHELILRLPDGYDTVIGPGgaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1726007896 227 ESIDLFWDYLDHV---GGSVVTITHD---FNQIDnyftRVVLLKDGVIK 269
Cdd:TIGR01842 488 EGEQALANAIKALkarGITVVVITHRpslLGCVD----KILVLQDGRIA 532
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
74-249 |
1.05e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfNAQDDLSVMTQENCLIAS 152
Cdd:PRK09544 4 LVSLENVSVSFGQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR--NGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 153 LKVREQIALSLKiyDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLF 232
Cdd:PRK09544 82 LPLTVNRFLRLR--PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|.
gi 1726007896 233 WDYLDHV----GGSVVTITHD 249
Cdd:PRK09544 160 YDLIDQLrrelDCAVLMVSHD 180
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
104-267 |
1.12e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 104 LLGSNGSGKTTIVNTILGnIIPDKGSVvkHFNAQD-------DLSVM----TQENCLIASLKVREQIALSL--KIYDAYS 170
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSI--QFAGQPleawsaaELARHraylSQQQTPPFAMPVFQYLTLHQpdKTRTEAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 171 KINIDDLLKKFRLTEQSEVIVDQLSGG--QKRRLALLLTLIKP-----SKLLILDEPTVGMDL---ESIDLFWDYLDHVG 240
Cdd:PRK03695 104 ASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVWPdinpaGQLLLLDEPMNSLDVaqqAALDRLLSELCQQG 183
|
170 180
....*....|....*....|....*..
gi 1726007896 241 GSVVTITHDFNQIDNYFTRVVLLKDGV 267
Cdd:PRK03695 184 IAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
9-63 |
1.86e-12 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 60.99 E-value: 1.86e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 9 LSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFL 63
Cdd:smart00530 2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
74-279 |
2.47e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNPV--LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV--------------VKHFNAQ 137
Cdd:PRK13652 3 LIETRDLCYSYSGSKeaLNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenireVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 ddlsVMTQENCLIASLKVREQIA---LSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKL 214
Cdd:PRK13652 83 ----VFQNPDDQIFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 215 LILDEPTVGMDLESIDLFWDYLDHV----GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLpetyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
68-248 |
3.50e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 68 THGDALILELKNLNKSFKNPV-LKDVNLSIyGRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSVvKHFNAQ---DDLSV 142
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGDFTaVDHVSFRI-RRGEIfGFLGSNGCGKSTTMKMLTGLLPASEGEA-WLFGQPvdaGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ------MTQENCLIASLKVREQIALSLKIYD---AYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI-KPs 212
Cdd:NF033858 338 rrrvgyMSQAFSLYGELTVRQNLELHARLFHlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIhKP- 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 213 KLLILDEPTVGMDLESIDLFWDYL------DHvggsvVTI---TH 248
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLielsreDG-----VTIfisTH 456
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
75-288 |
4.64e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLN------KSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFNAQ-------- 137
Cdd:PRK13641 3 IKFENVDyiyspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPEtgnknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 --DDLSVMTQ--ENCLIAS--LKVREQIALSLKIYDAYSKINIDDLLKKFRLTEQsevIVD----QLSGGQKRRLALLLT 207
Cdd:PRK13641 83 lrKKVSLVFQfpEAQLFENtvLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSED---LISkspfELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 208 LIKPSKLLILDEPTVGMD----LESIDLFWDYlDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQT 283
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDpegrKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEW 238
|
....*
gi 1726007896 284 IEHWY 288
Cdd:PRK13641 239 LKKHY 243
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
75-223 |
5.10e-12 |
|
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: 64.08 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdLSVMT--------- 144
Cdd:TIGR03410 1 LEVSNLNVYYgQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI--RLDGED-ITKLPpheraragi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 ----QENCLIASLKVREQIALSLKIYDAYSKINIDDLLKKFR-LTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:TIGR03410 78 ayvpQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
....
gi 1726007896 220 PTVG 223
Cdd:TIGR03410 158 PTEG 161
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
84-226 |
5.22e-12 |
|
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: 65.92 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 84 FKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQD-DLSVMTQ---------------- 145
Cdd:TIGR01193 485 YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIlLNGFSLKDiDRHTLRQfinylpqepyifsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 -ENCLI-ASLKVREQialslKIYDAYSKINIDDLLKKFRLTEQSEVIVD--QLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:TIGR01193 565 lENLLLgAKENVSQD-----EIWAACEIAEIKDDIENMPLGYQTELSEEgsSISGGQKQRIALARALLTDSKVLILDEST 639
|
....*
gi 1726007896 222 VGMDL 226
Cdd:TIGR01193 640 SNLDT 644
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
86-268 |
6.53e-12 |
|
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: 63.79 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDdLSVMTQEncliaSLkvREQI------ 159
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL--IDGQD-IREVTLD-----SL--RRAIgvvpqd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 160 ------------------ALSLKIYDAYSKINIDDLLKKFRltEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:cd03253 84 tvlfndtigynirygrpdATDEEVIEAAKAAQIHDKIMRFP--DGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 218 DEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDGVI 268
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNA-DKIIVLKDGRI 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
84-288 |
6.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 84 FKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfnAQDDLSVM--TQENCLiasLKVREQIAL 161
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV-----TVDDITIThkTKDKYI---RPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 162 SLKIYDAY----------------SKINIDDLLKK-FRLTEQ---SEVIVD----QLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:PRK13646 90 VFQFPESQlfedtvereiifgpknFKMNLDEVKNYaHRLLMDlgfSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 218 DEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIEHWY 288
Cdd:PRK13646 170 DEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWH 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
76-270 |
8.59e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSF---KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFN---AQDDLSVM 143
Cdd:PRK13632 9 KVENVSFSYpnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitISKENlkeIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQ--ENCLIASlKVREQIALSL------------KIYDAYSKINIDDLLKKfrltEQSEvivdqLSGGQKRRLALLLTLI 209
Cdd:PRK13632 89 FQnpDNQFIGA-TVEDDIAFGLenkkvppkkmkdIIDDLAKKVGMEDYLDK----EPQN-----LSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 210 KPSKLLILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK13632 159 LNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
71-266 |
1.24e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 71 DALILELKNLNKSFK-----NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD------- 138
Cdd:PRK11629 2 NKILLQCDNLCKRYQegsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI--FNGQPmsklssa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 --------DLSVMTQENCLIASLKVREQIALSLKI---YDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLT 207
Cdd:PRK11629 80 akaelrnqKLGFIYQFHHLLPDFTALENVAMPLLIgkkKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 208 LIKPSKLLILDEPTVGMDLESIDLFWDYLDHV----GGSVVTITHDFnQIDNYFTRVVLLKDG 266
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDL-QLAKRMSRQLEMRDG 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
87-248 |
1.61e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV--KHFNAQDD----LSVMTQENCLIASLKVREQIA 160
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidGKTATRGDrsrfMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLD--- 237
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISahl 184
|
170
....*....|.
gi 1726007896 238 HVGGSVVTITH 248
Cdd:PRK13543 185 RGGGAALVTTH 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
89-268 |
2.47e-11 |
|
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: 62.66 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD---------------DLSVMTQENCLIASL 153
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL--IDGQDiaamsrkelrelrrkKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 154 KVREQIALSLKIYDAYSKINID---DLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----L 226
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREEraaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1726007896 227 ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
74-266 |
2.77e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-----KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGniiPDKGSVVKHFNAQDDLSVMTQEN- 147
Cdd:PRK10584 6 IVEVHHLKKSVgqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSSGEVSLVGQPLHQMDEEAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 148 ---------------CLIASLKVREQI---ALSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLI 209
Cdd:PRK10584 83 aklrakhvgfvfqsfMLIPTLNALENVelpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 210 KPSKLLILDEPTVGMDLESIDLFWDYL-----DHvGGSVVTITHDfNQIDNYFTRVVLLKDG 266
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLfslnrEH-GTTLILVTHD-LQLAARCDRRLRLVNG 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
84-284 |
6.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 84 FKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV----------------VKHFNAQDDLSVMTQEN 147
Cdd:PRK13645 22 FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikeVKRLRKEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 148 CLIASlKVREQIA-----LSLKIYDAYSKIniDDLLKKFRLTEQ-SEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:PRK13645 102 QLFQE-TIEKDIAfgpvnLGENKQEAYKKV--PELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 222 VGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTI 284
Cdd:PRK13645 179 GGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
79-269 |
6.07e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 79 NLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfnaqddlsvmTQENCLIAS------ 152
Cdd:PRK13634 13 QYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-------------TIGERVITAgkknkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 153 LK-VREQIALSLKIYD------------AYSKINI----DDLLKKFR----LTEQSEVIVDQ----LSGGQKRRLALLLT 207
Cdd:PRK13634 80 LKpLRKKVGIVFQFPEhqlfeetvekdiCFGPMNFgvseEDAKQKARemieLVGLPEELLARspfeLSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 208 LIKPSKLLILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-279 |
8.04e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 22 LLAQKLFVsrqsISKWEngeSEPNIDKLISISEIFSVNLDFLLAGHTHGDalILELKNLNKSF---KNPVLKDVNLSIYG 98
Cdd:TIGR01257 1894 LLIQHHFF----LSRWI---AEPAKEPIFDEDDDVAEERQRIISGGNKTD--ILRLNELTKVYsgtSSPAVDRLCVGVRP 1964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 99 RDRIALLGSNGSGKTTIVNTILGNIIPDKG-------SVVKHF-NAQDDLSVMTQENCLIASLKVREQIALSLKIYDAYS 170
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagkSILTNIsDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 171 KiNIDDL----LKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV---GGSV 243
Cdd:TIGR01257 2045 E-EIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIireGRAV 2123
|
250 260 270
....*....|....*....|....*....|....*.
gi 1726007896 244 VTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
91-266 |
1.05e-10 |
|
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: 61.66 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 91 DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKH----FNAQDDLSVMT---------QENCLIASLKVRE 157
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlQDSARGIFLPPhrrrigyvfQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 158 QIALSLK-IYDAYSKINIDD---------LLKKFrlteqseviVDQLSGGQKRRLAL---LLTliKPsKLLILDEPTVGM 224
Cdd:COG4148 97 NLLYGRKrAPRAERRISFDEvvellgighLLDRR---------PATLSGGERQRVAIgraLLS--SP-RLLLMDEPLAAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726007896 225 DLESIDLFWDYL----DHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:COG4148 165 DLARKAEILPYLerlrDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
86-226 |
1.20e-10 |
|
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: 61.03 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGsVVKHfnaQDDLSVMTQENCLIASlKVREQIALSLKi 165
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-KIKH---SGRISFSSQFSWIMPG-TIKENIIFGVS- 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 166 YDAYSKINI-------DDLLKkfrLTEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:cd03291 124 YDEYRYKSVvkacqleEDITK---FPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
87-286 |
1.94e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNA------------QDDLSVMTQENCLIASLK 154
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VREQIALSLK---IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDL 231
Cdd:PRK13638 95 IDSDIAFSLRnlgVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 232 FWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIEH 286
Cdd:PRK13638 175 MIAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
66-266 |
2.96e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 66 GHTHGDALILELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGnIIPD-KGSVvkHFNAQDDLSVMT 144
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRI--ARPAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLI-ASLkvREQIAlslkiY----DAYSKINIDDLLKKFRL---TEQSEVIVD---QLSGGQKRRLAL--LLtLIKP 211
Cdd:COG4178 433 QRPYLPlGTL--REALL-----YpataEAFSDAELREALEAVGLghlAERLDEEADwdqVLSLGEQQRLAFarLL-LHKP 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 212 sKLLILDEPTVGMDLESIDLFWDYLDH--VGGSVVTITHDfNQIDNYFTRVVLLKDG 266
Cdd:COG4178 505 -DWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
76-283 |
3.33e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFKNP-----VLKDVNLS-----IYGrdriaLLGSNGSGKTTIVNTIlgNII--PDKGSVV------------ 131
Cdd:PRK11153 3 ELKNISKVFPQGgrtihALNNVSLHipageIFG-----VIGASGAGKSTLIRCI--NLLerPTSGRVLvdgqdltalsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 -------------KHFNaqddlsvmtqencLIASLKVREQIALSLKIyDAYSKINID----DLLKKFRLTEQSEVIVDQL 194
Cdd:PRK11153 76 elrkarrqigmifQHFN-------------LLSSRTVFDNVALPLEL-AGTPKAEIKarvtELLELVGLSDKADRYPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 195 SGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE---SI-DLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSIlELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVE 221
|
250
....*....|...
gi 1726007896 271 DESVANIHSNNQT 283
Cdd:PRK11153 222 QGTVSEVFSHPKH 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
84-285 |
4.28e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.29 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 84 FKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfnaqDDLSVMTQEncliASLK-VREQIALS 162
Cdd:PRK13637 18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-----DGVDITDKK----VKLSdIRKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 LK----------IYD--AYSKINI----DDLLKKFRLTEQS-----EVIVDQ----LSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:PRK13637 89 FQypeyqlfeetIEKdiAFGPINLglseEEIENRVKRAMNIvgldyEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 218 DEPTVGMD-------LESI-DLFWDYldhvGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:PRK13637 169 DEPTAGLDpkgrdeiLNKIkELHKEY----NMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
75-228 |
4.88e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF---KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIL-------GNIIPDkGSVVKHF---NAQDDLS 141
Cdd:PRK11176 342 IEFRNVTFTYpgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEILLD-GHDLRDYtlaSLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 VMTQE----NCLIASlkvreQIALSLKiyDAYSKiniDDLLKKFRLTEQSEVI--VDQ------------LSGGQKRRLA 203
Cdd:PRK11176 421 LVSQNvhlfNDTIAN-----NIAYART--EQYSR---EQIEEAARMAYAMDFInkMDNgldtvigengvlLSGGQRQRIA 490
|
170 180
....*....|....*....|....*
gi 1726007896 204 LLLTLIKPSKLLILDEPTVGMDLES 228
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTES 515
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
74-280 |
5.04e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD------------DL 140
Cdd:PRK11614 5 MLSFDKVSAHYgKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV--FDGKDitdwqtakimreAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 SVMTQENCLIASLKVREQIALS--LKIYDAYSKiNIDDLLKKF-RLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGgfFAERDQFQE-RIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 218 DEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSN 280
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLreqGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
74-270 |
5.83e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.59 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNL----NKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfnaqdDLSVMTQENCL 149
Cdd:PRK13650 4 IIEVKNLtfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII------DGDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 iaslKVREQIALSLKIYD------------AYSKIN--IDDLLKKFRLTEQSEVIVDQ---------LSGGQKRRLALLL 206
Cdd:PRK13650 78 ----DIRHKIGMVFQNPDnqfvgatveddvAFGLENkgIPHEEMKERVNEALELVGMQdfkereparLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 207 TLIKPSKLLILDEPTVGMD----LESIDLFWDYLDHVGGSVVTITHDFNQIdNYFTRVVLLKDGVIKS 270
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
87-249 |
6.15e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKG------------SVVKHFNAQDDLSVMTQENCLIASLK 154
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenipamSRSRLYTVRKRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 155 VREQIALSLKIYDAYSKINIDDL----LKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESID 230
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180
....*....|....*....|...
gi 1726007896 231 L---FWDYLDH-VGGSVVTITHD 249
Cdd:PRK11831 181 VlvkLISELNSaLGVTCVVVSHD 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
89-270 |
6.93e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfnAQDDLSVMTQENcLIASLKVREQIALS------ 162
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI---LGQPTRQALQKN-LVAYVPQSEEVDWSfpvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 -------------LKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLES- 228
Cdd:PRK15056 99 dvvmmgryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTe 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 229 ---IDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK15056 179 ariISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
74-266 |
9.69e-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: 59.07 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNtILGNIIPD---------KGSVVKHFNAQDD---- 139
Cdd:TIGR02633 1 LLEMKGIVKTFGGvKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwdgeiywSGSPLKASNIRDTerag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 LSVMTQENCLIASLKVREQIALSLKIYDAYSKINID-------DLLKKFRLTEQSEV-IVDQLSGGQKRRLALLLTLIKP 211
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamylrakNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 212 SKLLILDEPTVGMDLESIDLFWDY---LDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
74-285 |
1.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVK------------HFNAQD 138
Cdd:PRK13640 5 IVEFKHVSFTYPDskkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdgitltaktVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 DLSVMTQ--ENCLIASlKVREQIALSLK----IYDAYSKInIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPS 212
Cdd:PRK13640 85 KVGIVFQnpDNQFVGA-TVGDDVAFGLEnravPRPEMIKI-VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 213 KLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIdNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:PRK13640 163 KIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
91-248 |
1.52e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 91 DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD----------DLSVMTQENCLIASLKVREQIA 160
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV--LWQGEPirrqrdeyhqDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLD-HV 239
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAqHA 176
|
170
....*....|.
gi 1726007896 240 --GGSVVTITH 248
Cdd:PRK13538 177 eqGGMVILTTH 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
103-266 |
2.03e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 103 ALLGSNGSGKTTIVNTILGNIIPDKGSVV-----------KHFNAQddLSVMTQENCLIASLKVREQIAL-------SLK 164
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqpleswssKAFARK--VAYLPQQLPAAEGMTVRELVAIgrypwhgALG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 165 IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL----ESIDLFWDYLDHVG 240
Cdd:PRK10575 119 RFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERG 198
|
170 180
....*....|....*....|....*.
gi 1726007896 241 GSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK10575 199 LTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-228 |
2.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNT------------ILGNIIPDKGSVVKH--FNAQDD 139
Cdd:PRK14247 4 IEIRDLKVSFGQvEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMdvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 LSVMTQENCLIASLKVREQIALSLKIYD-AYSKINIDD----LLKKFRLTEQSEVIVD----QLSGGQKRRLALLLTLIK 210
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQErvrwALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAF 163
|
170
....*....|....*...
gi 1726007896 211 PSKLLILDEPTVGMDLES 228
Cdd:PRK14247 164 QPEVLLADEPTANLDPEN 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
87-249 |
2.26e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVL-KDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKhfNAQDDLSVMTQENCLIASLKVREQIALSlKI 165
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR--SAKVRMAVFSQHHVDGLDLSSNPLLYMM-RC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 166 YDAYSKINIDDLLKKFRLTEQSEV-IVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGGSVV 244
Cdd:PLN03073 599 FPGVPEQKLRAHLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVL 678
|
....*
gi 1726007896 245 TITHD 249
Cdd:PLN03073 679 MVSHD 683
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
75-283 |
2.93e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---------------------- 131
Cdd:PRK10619 6 LNVIDLHKRYgEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 -------------KHFNAQDDLSVMtqENCLIASLKV--------REQIALSLkiydaySKINIDDllkkfrlTEQSEVI 190
Cdd:PRK10619 86 qlrllrtrltmvfQHFNLWSHMTVL--ENVMEAPIQVlglskqeaRERAVKYL------AKVGIDE-------RAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 191 VDqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE---SIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGV 267
Cdd:PRK10619 151 VH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250
....*....|....*.
gi 1726007896 268 IKSDESVANIHSNNQT 283
Cdd:PRK10619 230 IEEEGAPEQLFGNPQS 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
75-275 |
3.79e-09 |
|
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: 57.12 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG--NIIPDKGSVVKH------------------ 133
Cdd:TIGR03269 1 IEVKNLTKKFDGkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 134 ---------------FNAQDD---------LSVMTQEN-CLIASLKVREQIALSLKIYDAYSKINID---DLLKKFRLTE 185
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDklrrrirkrIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGravDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 186 QSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV----GGSVVTITHDFNQIDNYFTRVV 261
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 1726007896 262 LLKDGVIK----SDESVA 275
Cdd:TIGR03269 241 WLENGEIKeegtPDEVVA 258
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
102-227 |
3.91e-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: 57.10 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfNAQDDLSVMTQENCLIASLKVREqiALSLKIYDAY-SKINIDDLLKK 180
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV----DEDLKISYKPQYISPDYDGTVEE--FLRSANTDDFgSSYYKTEIIKP 442
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1726007896 181 FRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE 227
Cdd:COG1245 443 LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
75-265 |
5.06e-09 |
|
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: 54.47 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnkSFKNP----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGnIIP-DKGSVVKHfnAQDDLSVMTQENCL 149
Cdd:cd03223 1 IELENL--SLATPdgrvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMP--EGEDLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 150 IA-SLkvREQIALSLKiydayskiniddllkkfrlteqsevivDQLSGGQKRRLA---LLLTliKPsKLLILDEPTVGMD 225
Cdd:cd03223 76 PLgTL--REQLIYPWD---------------------------DVLSGGEQQRLAfarLLLH--KP-KFVFLDEATSALD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1726007896 226 LESIDLFWDYLDHVGGSVVTITHDfNQIDNYFTRVVLLKD 265
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
102-221 |
5.57e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNIIPDKGS---------VVKHFNA---QD---DLSvmtqENCLIASLKVR--EQIALSLK 164
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLKRFRGtelQNyfkKLY----NGEIKVVHKPQyvDLIPKVFK 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 165 --IYDAYSKIN----IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:PRK13409 178 gkVRELLKKVDergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
74-227 |
6.80e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfNAQDDLSVMTQEncLIASL 153
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----DPELKISYKPQY--IKPDY 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 154 KVREQIALSlKIYDAY-SKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE 227
Cdd:PRK13409 414 DGTVEDLLR-SITDDLgSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
87-226 |
6.96e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSvVKHfnaQDDLSVMTQENCLIASlKVREQIALSLKiY 166
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-IKH---SGRISFSPQTSWIMPG-TIKDNIIFGLS-Y 513
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 167 DAY---SKINIDDLLKKFRLTEQSEVIV-----DQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:TIGR01271 514 DEYrytSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
88-266 |
8.75e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV-------VKHFnAQDDLSVMTQENCLIASL-----KV 155
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgikLGYF-AQHQLEFLRADESPLQHLarlapQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQialslkiydayskiNIDDLLKKF-----RLTEQSEvivdQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESID 230
Cdd:PRK10636 406 LEQ--------------KLRDYLGGFgfqgdKVTEETR----RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190
....*....|....*....|....*....|....*.
gi 1726007896 231 LFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDG 503
|
|
| HTH_19 |
pfam12844 |
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ... |
9-66 |
1.07e-08 |
|
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.
Pssm-ID: 463728 [Multi-domain] Cd Length: 64 Bit Score: 50.75 E-value: 1.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 9 LSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAG 66
Cdd:pfam12844 4 LRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLYKIAELLGVPANWLLQG 61
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
74-286 |
1.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNL----NKSFKNPVLKDVNLSI-YGRDRI-ALLGSNGSGKTTIVNTILGNIIPDKGSV-VKHFNAQDDLSVMTQE 146
Cdd:PRK13631 21 ILRVKNLycvfDEKQENELVALNNISYtFEKNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIqVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 NCL----IASLK-VREQI-------------------------ALSLKIYDAY--SKINIDDLLKKFRLTEQSEVivdQL 194
Cdd:PRK13631 101 TNPyskkIKNFKeLRRRVsmvfqfpeyqlfkdtiekdimfgpvALGVKKSEAKklAKFYLNKMGLDDSYLERSPF---GL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 195 SGGQKRRLALLLTLIKPSKLLILDEPTVGMD----LESIDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIKS 270
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgeHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|....*.
gi 1726007896 271 DESVANIHSNNQTIEH 286
Cdd:PRK13631 257 TGTPYEIFTDQHIINS 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
86-280 |
1.21e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPD-------KGSVVKHFNAQDDLSVMTQENCLIASLKVREQ 158
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAetssvviRGSVAYVPQVSWIFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 159 IAlslKIYDAYSKINIDDLLKKFRLTEQSEVIVDqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE-SIDLFWDYLD 237
Cdd:PLN03232 710 YW---RAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMK 785
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1726007896 238 H--VGGSVVTIT---HDFNQIDnyftRVVLLKDGVIKSDESVANIHSN 280
Cdd:PLN03232 786 DelKGKTRVLVTnqlHFLPLMD----RIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
75-268 |
1.39e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIlgNII--PDKGSV-VKHFNAQDDLSVMTQENcLI 150
Cdd:PRK11264 4 IEVKNLVKKFHgQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLeqPEAGTIrVGDITIDTARSLSQQKG-LI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 151 ASLkvREQIALSLKIYDAYSKI----NI-------------------DDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLT 207
Cdd:PRK11264 81 RQL--RQHVGFVFQNFNLFPHRtvleNIiegpvivkgepkeeataraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 208 LIKPSKLLILDEPTVGMDLEsidLFWDYLDHVGG------SVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE---LVGEVLNTIRQlaqekrTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
74-266 |
1.42e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVN---------TILGNIIPDkGSVVKHFNAQDD---- 139
Cdd:PRK13549 5 LLEMKNITKTFGGvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlsgvyphgTYEGEIIFE-GEELQASNIRDTerag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 140 LSVMTQENCLIASLKVREQIALSLKI-------YDA-YSKIniDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEItpggimdYDAmYLRA--QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 212 SKLLILDEPTVGMDLESIDLFWDY---LDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
102-221 |
1.55e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNIIPDKGS---------VVKHFN---AQDDLSvMTQENCLIASLKVR--EQI--ALSLKI 165
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLKRFRgteLQDYFK-KLANGEIKVAHKPQyvDLIpkVFKGTV 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 166 YDAYSKIN----IDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPT 221
Cdd:COG1245 181 RELLEKVDergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
102-266 |
1.87e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTI---------LGNIIPDKGSVVKH------FNAQDDLsvmtqencLIASLKVREQIALS--LK 164
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPTKQilkrtgFVTQDDI--------LYPHLTVRETLVFCslLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 165 IYDAYSK----INIDDLLKKFRLTEQSEVIVDQ-----LSGGQKRRLALLL-TLIKPSkLLILDEPTVGMDLES---IDL 231
Cdd:PLN03211 169 LPKSLTKqekiLVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHeMLINPS-LLILDEPTSGLDATAayrLVL 247
|
170 180 190
....*....|....*....|....*....|....*.
gi 1726007896 232 FWDYLDHVGGSVVTITHD-FNQIDNYFTRVVLLKDG 266
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
161-279 |
2.11e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAYSKIniDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV- 239
Cdd:NF000106 114 LDLSRKDARARA--DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMv 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1726007896 240 --GGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHS 279
Cdd:NF000106 192 rdGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
104-266 |
2.18e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 104 LLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD--------------DLSVMTQENCLIASLKVREQIALSLKIYDAY 169
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIW--FSGHDitrlknrevpflrrQIGMIFQDHHLLMDRTVYDNVAIPLIIAGAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 170 S---KINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD---LESIDLFWDYLDHVGGSV 243
Cdd:PRK10908 111 GddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTV 190
|
170 180
....*....|....*....|...
gi 1726007896 244 VTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK10908 191 LMATHDIGLISRRSYRMLTLSDG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
75-249 |
3.07e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.87 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPD---KGSVVkhFNAQD---------DLS 141
Cdd:COG4136 2 LSLENLTITLGGrPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVL--LNGRRltalpaeqrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 VMTQENCLIASLKVREQIALSL--KIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1726007896 220 PTVGMD----LESIDLFWDYLDHVGGSVVTITHD 249
Cdd:COG4136 160 PFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
73-266 |
4.17e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.25 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLN-----KSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVN---------TILGNIIPDKGSVVKHFNAQd 138
Cdd:cd03232 2 SVLTWKNLNytvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvlagrktagVITGEILINGRPLDKNFQRS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 dLSVMTQENCLIASLKVREQIALSLKIYDayskiniddllkkfrlteqsevivdqLSGGQKRRLALLLTLI-KPSkLLIL 217
Cdd:cd03232 81 -TGYVEQQDVHSPNLTVREALRFSALLRG--------------------------LSVEQRKRLTIGVELAaKPS-ILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 218 DEPTVGMDLES---IDLFWDYLDHVGGSVV-TITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03232 133 DEPTSGLDSQAaynIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
71-269 |
4.47e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 71 DALILelKNLNKSFKnpVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHfnaqDDLSVMTQENCLI 150
Cdd:PRK13546 26 DALIP--KHKNKTFF--ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN----GEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 151 ASLKVREQIALSLkIYDAYSKINIDDLLKKF-RLTEQSEVI---VDQLSGGQKRRLALLLTLIKPSKLLILDEP-TVG-- 223
Cdd:PRK13546 98 GQLTGIENIEFKM-LCMGFKRKEIKAMTPKIiEFSELGEFIyqpVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGdq 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1726007896 224 -MDLESIDLFWDYLDHvGGSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:PRK13546 177 tFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
2-64 |
6.94e-08 |
|
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];
Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 49.25 E-value: 6.94e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 2 ENIFKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLL 64
Cdd:COG3620 15 DDTLGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALGKELSAVL 77
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
74-280 |
6.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.68 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQENCLIA 151
Cdd:PRK13644 1 MIRLENVSYSYPDgtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 SL-----------KVREQIAL---SLKIYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLIL 217
Cdd:PRK13644 81 IVfqnpetqfvgrTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 218 DEPTVGMDLESIDLFWD---YLDHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKSDESVANIHSN 280
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLErikKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
92-275 |
7.57e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 92 VNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQddlsVMTQENclIASLkvREQIA-------LSLK 164
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL--LDGQ----PVTADN--REAY--RQLFSavfsdfhLFDR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 165 IYDAYSKIN---IDDLLKKFRLTEQSEVIVD-----QLSGGQKRRLALLLTLI--KPskLLILDE------PTvgmdles 228
Cdd:COG4615 421 LLGLDGEADparARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLedRP--ILVFDEwaadqdPE------- 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 229 idlFWDYLDHV--------GGSVVTITHDfnqiDNYF---TRVVLLKDGVIKSDESVA 275
Cdd:COG4615 492 ---FRRVFYTEllpelkarGKTVIAISHD----DRYFdlaDRVLKMDYGKLVELTGPA 542
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
103-256 |
7.58e-08 |
|
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: 50.82 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 103 ALLGSNGSGKTTIVNTILgniipdkgsvvkhfnaqddlsvmtqENCLIASLKVREQIALSLKIYDAYSKINIddllkkfr 182
Cdd:cd03227 25 IITGPNGSGKSTILDAIG-------------------------LALGGAQSATRRRSGVKAGCIVAAVSAEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 183 lteqsEVIVDQLSGGQKRR--LALLLTL--IKPSKLLILDEPTVGMDLESIDLFWDYLDH--VGGS-VVTITHDFNQIDN 255
Cdd:cd03227 72 -----IFTRLQLSGGEKELsaLALILALasLKPRPLYILDEIDRGLDPRDGQALAEAILEhlVKGAqVIVITHLPELAEL 146
|
.
gi 1726007896 256 Y 256
Cdd:cd03227 147 A 147
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
74-225 |
1.01e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI--LGNIIPD---KGSVVkhFNAQDDLS------ 141
Cdd:PRK14239 5 ILQVSDLSVYYnKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIV--YNGHNIYSprtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 --------VMTQENCLIASlkVREQIALSLKIYDAYSKINIDDLLKKfrlTEQSEVIVDQ-----------LSGGQKRRL 202
Cdd:PRK14239 83 dlrkeigmVFQQPNPFPMS--IYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEvkdrlhdsalgLSGGQQQRV 157
|
170 180
....*....|....*....|...
gi 1726007896 203 ALLLTLIKPSKLLILDEPTVGMD 225
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALD 180
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
74-226 |
1.02e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN----------PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV--KHFNAQDDLS 141
Cdd:PRK15112 4 LLEVRNLSKTFRYrtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLidDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 VMTQENCLI-----ASLKVREQIAlslKIYDAYSKIN-----------IDDLLKKFRL-TEQSEVIVDQLSGGQKRRLAL 204
Cdd:PRK15112 84 YRSQRIRMIfqdpsTSLNPRQRIS---QILDFPLRLNtdlepeqrekqIIETLRQVGLlPDHASYYPHMLAPGQKQRLGL 160
|
170 180
....*....|....*....|..
gi 1726007896 205 LLTLIKPSKLLILDEPTVGMDL 226
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDM 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
67-225 |
1.04e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 67 HTHGDALILELKNLNKsfkNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMT-- 144
Cdd:COG1129 249 AAAPGEVVLEVEGLSV---GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDai 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 -----------QENCLIASLKVREQIALSlkIYDAYSK---IN-------IDDLLKKFRL-TEQSEVIVDQLSGG--QKR 200
Cdd:COG1129 326 ragiayvpedrKGEGLVLDLSIRENITLA--SLDRLSRgglLDrrreralAEEYIKRLRIkTPSPEQPVGNLSGGnqQKV 403
|
170 180
....*....|....*....|....*.
gi 1726007896 201 RLA-LLLTliKPsKLLILDEPTVGMD 225
Cdd:COG1129 404 VLAkWLAT--DP-KVLILDEPTRGID 426
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
74-277 |
1.20e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIL------GNIIPDKGSVVKHFNAQ----- 137
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqaGGLVQCDKMLLRRRSRQviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 ------------DDLSVMTQE--NCLIASLKVREQIALSLKIYDAYSK----INIDDLLKKFRLTEQSEVIV---DQLSG 196
Cdd:PRK10261 92 eqsaaqmrhvrgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASReeamVEAKRMLDQVRIPEAQTILSrypHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 197 GQKRRLALLLTLIKPSKLLILDEPTVGMD-------LESIDLFWDYLDHvggSVVTITHDFNQIDNYFTRVVLLKDGVIK 269
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDvtiqaqiLQLIKVLQKEMSM---GVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 1726007896 270 SDESVANI 277
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
74-249 |
1.53e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.53 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNPVLKD-VNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFNAQDDLSV------- 142
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNnVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgQHIEGLPGHQIarmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ----------MTQ-ENCLIAS-LKVREQIALSLKIYDAYSKINIDDL------LKKFRLTEQSEVIVDQLSGGQKRRLAL 204
Cdd:PRK11300 85 tfqhvrlfreMTViENLLVAQhQQLKTGLFSGLLKTPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1726007896 205 LLTLIKPSKLLILDEPTVGMD-LESIDL--FWDYL-DHVGGSVVTITHD 249
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNpKETKELdeLIAELrNEHNVTVLLIEHD 213
|
|
| YiaG |
COG2944 |
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription]; |
11-52 |
1.55e-07 |
|
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];
Pssm-ID: 442187 [Multi-domain] Cd Length: 64 Bit Score: 47.62 E-value: 1.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1726007896 11 ALRQKKHLSQELLAQKLFVSRQSISKWENGESEPN--IDKLISI 52
Cdd:COG2944 13 ALRERLGLSQAEFAALLGVSVSTVRRWEQGRRKPSgaALKLLRL 56
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
85-266 |
1.70e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.72 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTiLGNIIPDKGSVVK--HFN----------AQDDLSVMTQENCLIAS 152
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKA-LANRTEGNVSVEGdiHYNgipykefaekYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 153 LKVREQIalslkiydayskiniddllkKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD------- 225
Cdd:cd03233 98 LTVRETL--------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDsstalei 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1726007896 226 LESIDLFWDYLDHVggSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03233 158 LKCIRTMADVLKTT--TFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
106-260 |
1.70e-07 |
|
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: 50.68 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 106 GSNGSGKTTIVNTILGNIIPDKgSVVKHFNAQDDLSVMTQENclIASLKVREQIALSLKiYDAYSKINIddlLKKFRLTE 185
Cdd:cd03240 29 GQNGAGKTTIIEALKYALTGEL-PPNSKGGAHDPKLIREGEV--RAQVKLAFENANGKK-YTITRSLAI---LENVIFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 186 QSEV------IVDQLSGGQKR------RLALLLTLIKPSKLLILDEPTVGMDLESI-----DLFWDYLDHVGGSVVTITH 248
Cdd:cd03240 102 QGESnwplldMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNFQLIVITH 181
|
170
....*....|....
gi 1726007896 249 D--FNQIDNYFTRV 260
Cdd:cd03240 182 DeeLVDAADHIYRV 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-225 |
1.89e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI-----LGNIIPDKGSV-----------VKHFNAQ 137
Cdd:PRK14267 5 IETVNLRVYYgSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVrlfgrniyspdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 DDLSVMTQENCLIASLKVREQIALSLKIYD-AYSKINIDDL----LKKFRLTEQSEVIVD----QLSGGQKRRLALLLTL 208
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERvewaLKKAALWDEVKDRLNdypsNLSGGQRQRLVIARAL 164
|
170
....*....|....*..
gi 1726007896 209 IKPSKLLILDEPTVGMD 225
Cdd:PRK14267 165 AMKPKILLMDEPTANID 181
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
64-252 |
2.12e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 64 LAGHTHgdalILELKNLNKSFKNP---VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQ--- 137
Cdd:PRK13648 1 MEDKNS----IIVFKNVSFQYQSDasfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF--YNNQait 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 -DDLSVMTQ---------ENCLIASLkVREQIALSLK----IYDAYSKInIDDLLKKFRLTEQSEVIVDQLSGGQKRRLA 203
Cdd:PRK13648 75 dDNFEKLRKhigivfqnpDNQFVGSI-VKYDVAFGLEnhavPYDEMHRR-VSEALKQVDMLERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 204 LLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGG----SVVTITHDFNQ 252
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHDLSE 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
81-220 |
3.21e-07 |
|
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: 49.78 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 81 NKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhfNAQDDLSVMTQENCLIaSLKVREQIA 160
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV----SVPGSIAYVSQEPWIQ-NGTIRENIL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 161 LSLKIYDAYSKINID------DlLKKFRLTEQSEV----IvdQLSGGQKRRLALLLTLIKPSKLLILDEP 220
Cdd:cd03250 88 FGKPFDEERYEKVIKacalepD-LEILPDGDLTEIgekgI--NLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
73-249 |
3.77e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSF-----------KNPVLK---DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQD 138
Cdd:PRK15079 7 VLLEVADLKVHFdikdgkqwfwqPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--WLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 dLSVMTQENCL-------------IASLKVR----EQIALSLKIYdaYSKINIDDLLKKFR--------LTEQSEVIVDQ 193
Cdd:PRK15079 85 -LLGMKDDEWRavrsdiqmifqdpLASLNPRmtigEIIAEPLRTY--HPKLSRQEVKDRVKammlkvglLPNLINRYPHE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 194 LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHD 249
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
74-266 |
4.07e-07 |
|
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: 49.35 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSfknPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdlsvmtqenclIASL 153
Cdd:cd03215 4 VLEVRGLSVK---GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI--TLDGKP-----------VTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 154 KVREQIA----------------LSLKIYDayskiNIddllkkfrlteqseVIVDQLSGG--QKrrlaLLLT--LIKPSK 213
Cdd:cd03215 68 SPRDAIRagiayvpedrkreglvLDLSVAE-----NI--------------ALSSLLSGGnqQK----VVLArwLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 214 LLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-253 |
4.07e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTiLGNIIPDKGSV-----VKHFNA-----QDDLSVM 143
Cdd:PRK14258 8 IKVNNLSFYYdTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVrvegrVEFFNQniyerRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQENCLIAS------LKVREQIALSLKIYDAYSKINIDDL----LKKFRLTEQSEVIVDQ----LSGGQKRRLALLLTLI 209
Cdd:PRK14258 87 RRQVSMVHPkpnlfpMSVYDNVAYGVKIVGWRPKLEIDDIvesaLKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1726007896 210 KPSKLLILDEPTVGMD-LESIDLfwDYLDHVGG-----SVVTITHDFNQI 253
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDpIASMKV--ESLIQSLRlrselTMVIVSHNLHQV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
91-277 |
4.19e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.64 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 91 DVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKH----FNAQDDLSVMT---------QENCLIASLKVRE 157
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlFDAEKGICLPPekrrigyvfQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 158 QIALSLKIYDA--YSKI----NIDDLLKKFRLTeqsevivdqLSGGQKRRLAL---LLTliKPsKLLILDEPtvgmdLES 228
Cdd:PRK11144 96 NLRYGMAKSMVaqFDKIvallGIEPLLDRYPGS---------LSGGEKQRVAIgraLLT--AP-ELLLMDEP-----LAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 229 IDL-----FWDYL----DHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANI 277
Cdd:PRK11144 159 LDLprkreLLPYLerlaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
75-268 |
4.92e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKNP--VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---------------KHFNAq 137
Cdd:PRK10522 323 LELRNVTFAYQDNgfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILldgkpvtaeqpedyrKLFSA- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 ddlsVMTQENcLIASLKVREQIALSLKIYDAYskinIDDLLKKFRLTEQSEVIVD-QLSGGQKRRLALLLTLIKPSKLLI 216
Cdd:PRK10522 402 ----VFTDFH-LFDQLLGPEGKPANPALVEKW----LERLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726007896 217 LDEPTVGMDLESIDLFWD----YLDHVGGSVVTITHDfnqiDNYFT---RVVLLKDGVI 268
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQvllpLLQEMGKTIFAISHD----DHYFIhadRLLEMRNGQL 527
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
71-249 |
5.96e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 71 DALILELKNLNKSFKNPV-LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------------------- 130
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyalseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 131 ----------VKHFNAQDDL--SVMTQENC---LIAS-----LKVREQ---------IALSlkiydayskiNIDDLLKKF 181
Cdd:PRK11701 83 rrrllrtewgFVHQHPRDGLrmQVSAGGNIgerLMAVgarhyGDIRATagdwlerveIDAA----------RIDDLPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 182 rlteqsevivdqlSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLeSI-----DLFWDYLDHVGGSVVTITHD 249
Cdd:PRK11701 153 -------------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVqarllDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-285 |
6.60e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.71 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIlgNIIPDKGSVVKH-----------FNAQDdlsvmtqencliaSLKVR 156
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL--NRMNDKVSGYRYsgdvllggrsiFNYRD-------------VLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIALSLKIYDAYSKINIDDLL-----------KKFRLTEQS--------EVIVD-------QLSGGQKRRLALLLTLIK 210
Cdd:PRK14271 101 RRVGMLFQRPNPFPMSIMDNVLagvrahklvprKEFRGVAQArltevglwDAVKDrlsdspfRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 211 PSKLLILDEPTVGMDLESIDLFWDYLDHVGG--SVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNNQTIE 285
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
93-265 |
8.69e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 93 NLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDLSVMTQENCLIASLK-----------------V 155
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrnntdmlspgeddtgrtT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALSLK---IYDAYSKI-NIDDLL-KKFRlteqsevivdQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESID 230
Cdd:PRK10938 103 AEIIQDEVKdpaRCEQLAQQfGITALLdRRFK----------YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1726007896 231 LFWDYLD---HVGGSVVTITHDFNQIDNYFTRVVLLKD 265
Cdd:PRK10938 173 QLAELLAslhQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
74-248 |
9.68e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG----NIIpdKGSVVkhFNAQDDLSV------ 142
Cdd:CHL00131 7 ILEIKNLHASVNeNEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpayKIL--EGDIL--FKGESILDLepeera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 143 ----------------MTQENCLIASLKVReQIALSLKIYDAYSKINIddLLKKFRLTEQSEVIV-----DQLSGGQKRR 201
Cdd:CHL00131 83 hlgiflafqypieipgVSNADFLRLAYNSK-RKFQGLPELDPLEFLEI--INEKLKLVGMDPSFLsrnvnEGFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1726007896 202 LALLLTLIKPSKLLILDEPTVGMD---LESIDLFWDYLDHVGGSVVTITH 248
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDidaLKIIAEGINKLMTSENSIILITH 209
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
73-249 |
1.06e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 73 LILELKNLNKSFKNP-----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPD---KGSVvkHFNAQDDLSVMT 144
Cdd:PRK09473 11 ALLDVKDLRVTFSTPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSA--TFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QE-NCLIA------------SL----KVREQIALSLKIYDAYSK-------INIDDLLKKFRLTEQSEVIVDQLSGGQKR 200
Cdd:PRK09473 89 KElNKLRAeqismifqdpmtSLnpymRVGEQLMEVLMLHKGMSKaeafeesVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 201 RLALLLTLIKPSKLLILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHD 249
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
88-277 |
1.18e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIipdKGSVVKH-FNAQDDLSV---------MTQENCLIASLKVRE 157
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRgARVTGDVTLngeplaaidAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 158 QIALSLKIYD--------------AYSKINIDDLLKKFRLTEQSEVI---VDQLSGGQKRRL--ALLLTLIKPS------ 212
Cdd:PRK13547 93 QPAFAFSAREivllgrypharragALTHRDGEIAWQALALAGATALVgrdVTTLSGGELARVqfARVLAQLWPPhdaaqp 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 213 -KLLILDEPTVGMD-------LESI-DLFWDYldHVGgsVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANI 277
Cdd:PRK13547 173 pRYLLLDEPTAALDlahqhrlLDTVrRLARDW--NLG--VLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
90-277 |
2.12e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 90 KDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhFNAQDdLSVMTQENCLIASL----KVREQIALSL-- 163
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM--LNGKE-INALSTAQRLARGLvylpEDRQSSGLYLda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 164 ------------------------KIYDAYSK-INIddllkKFRLTEQSeviVDQLSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:PRK15439 357 plawnvcalthnrrgfwikparenAVLERYRRaLNI-----KFNHAEQA---ARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 219 EPTVGMDLESIDLFWDYLDHV---GGSVVTITHDFNQIDNYFTRVVLLKDGVI-----KSDESVANI 277
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEIsgaltGAAINVDTI 495
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
77-225 |
2.16e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.49 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 77 LKNLNKSFKNPVL-KDVNLSIYGRDRIALLGSNGSGKTTIVNTILG-----------------NIIPDKGSVVKHFnaqd 138
Cdd:PRK11000 6 LRNVTKAYGDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGMVF---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 dlsvmtQENCLIASLKVREQIALSLKIYDAySKINIDDllkkfRLTEQSEVI-----VDQ----LSGGQKRRLALLLTLI 209
Cdd:PRK11000 82 ------QSYALYPHLSVAENMSFGLKLAGA-KKEEINQ-----RVNQVAEVLqlahlLDRkpkaLSGGQRQRVAIGRTLV 149
|
170
....*....|....*.
gi 1726007896 210 KPSKLLILDEPTVGMD 225
Cdd:PRK11000 150 AEPSVFLLDEPLSNLD 165
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
63-268 |
3.42e-06 |
|
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: 48.14 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 63 LLAGHTHGDAL--------ILELKNLNKSFKNP------------VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGn 122
Cdd:COG4172 256 LLAAEPRGDPRpvppdappLLEARDLKVWFPIKrglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 123 IIPDKGSVvkHFNAQDdlsvmtqenclIASLKVREQIALSLKIY----DAYSKIN----IDDLL--------KKFRLTEQ 186
Cdd:COG4172 335 LIPSEGEI--RFDGQD-----------LDGLSRRALRPLRRRMQvvfqDPFGSLSprmtVGQIIaeglrvhgPGLSAAER 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 187 SEVIVDQL-----------------SGGQKRRLALLLTLI-KPsKLLILDEPTVGMDLeSI-----DLFWDYLDHVGGSV 243
Cdd:COG4172 402 RARVAEALeevgldpaarhryphefSGGQRQRIAIARALIlEP-KLLVLDEPTSALDV-SVqaqilDLLRDLQREHGLAY 479
|
250 260
....*....|....*....|....*.
gi 1726007896 244 VTITHDFNQIDnYFT-RVVLLKDGVI 268
Cdd:COG4172 480 LFISHDLAVVR-ALAhRVMVMKDGKV 504
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
87-281 |
4.46e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIL-------GNIIPDKGSVVKhFNAQD---DLSVMTQENCLIaSLKVR 156
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRIMIDDCDVAK-FGLTDlrrVLSIIPQSPVLF-SGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIalslkiyDAYSKINIDDLLKKFRLTEQSEVIV--------------DQLSGGQKRRLALLLTLIKPSKLLILDEPTV 222
Cdd:PLN03232 1328 FNI-------DPFSEHNDADLWEALERAHIKDVIDrnpfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726007896 223 GMDLESIDLFWDYL--DHVGGSVVTITHDFNQIDNyFTRVVLLKDGVIKSDESVANIHSNN 281
Cdd:PLN03232 1401 SVDVRTDSLIQRTIreEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
85-225 |
5.39e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 85 KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG---------------NIIPDKGSVVKHFNAQDDLSvmtqencl 149
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalkgtpvagcvdvpdNQFGREASLIDAIGRKGDFK-------- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 150 iASLKVREQIALSlkiyDAYSkiniddLLKKFrlteqsevivDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:COG2401 114 -DAVELLNAVGLS----DAVL------WLRRF----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
185-261 |
5.73e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 5.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 185 EQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVV 261
Cdd:PRK10636 141 EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
104-226 |
5.98e-06 |
|
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: 46.59 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 104 LLGSNGSGKTTIVNTILGNIIPDKGS---------VVKHFNA---QDDLSVMTQENcLIASLKVR--EQI--ALSLKIYD 167
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILDEFRGselQNYFTKLLEGD-VKVIVKPQyvDLIpkAVKGKVGE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 168 AYSKI----NIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL 226
Cdd:cd03236 110 LLKKKdergKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
75-277 |
8.51e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFknP---VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQDDL----S 141
Cdd:PRK11288 5 LSFDGIGKTF--PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlidgqeMRFASTTAALaagvA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 VMTQENCLIASLKVREQIAL------------SLKIYDAYSK-----INIDDLLKkfrlteqseviVDQLSGGQKRRLAL 204
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLgqlphkggivnrRLLNYEAREQlehlgVDIDPDTP-----------LKYLSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 205 LLTLIKPSKLLILDEPTVGMDLESID-LF--WDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG-VIKSDESVANI 277
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEqLFrvIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQV 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
193-247 |
9.15e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 9.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 193 QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHV-----GGSVVTIT 247
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraerpGMSVLVAT 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
63-225 |
1.72e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 63 LLAGHTHGDAL--------ILELKNLNKSF------------KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILgN 122
Cdd:PRK15134 256 LLNSEPSGDPVplpepaspLLDVEQLQVAFpirkgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-R 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 123 IIPDKGSVVkhFNAQDdLSVMTQEncliASLKVREQIALSLKiyDAYSKIN--------IDDLLKKFRLT------EQ-- 186
Cdd:PRK15134 335 LINSQGEIW--FDGQP-LHNLNRR----QLLPVRHRIQVVFQ--DPNSSLNprlnvlqiIEEGLRVHQPTlsaaqrEQqv 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 187 ----SEVIVD---------QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:PRK15134 406 iavmEEVGLDpetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK04140 |
PRK04140 |
transcriptional regulator; |
9-60 |
1.79e-05 |
|
transcriptional regulator;
Pssm-ID: 235224 [Multi-domain] Cd Length: 317 Bit Score: 45.62 E-value: 1.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 9 LSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNL 60
Cdd:PRK04140 131 LREAREELGLSLGELASELGVSRRTISKYENGGMNASIEVAIKLEEILDVPL 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
194-253 |
1.88e-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: 46.16 E-value: 1.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 194 LSGGQKRRLALLLTLIKPSK---LLILDEPTVGMDLESIDLFWDYLD---HVGGSVVTITHDFNQI 253
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHNLDVI 895
|
|
| PHA01976 |
PHA01976 |
helix-turn-helix protein |
5-66 |
2.02e-05 |
|
helix-turn-helix protein
Pssm-ID: 177330 [Multi-domain] Cd Length: 67 Bit Score: 41.87 E-value: 2.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 5 FKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAG 66
Cdd:PHA01976 3 FAIQLIKARNARAWSAPELSRRAGVRHSLIYDFEADKRLPNLKTLLRLADALGVTLDWLCGR 64
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
67-225 |
2.04e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 67 HTHGDaLILELKNLNksfkNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV------VKHFNAQDDL 140
Cdd:PRK10762 251 KAPGE-VRLKVDNLS----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldgheVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 141 S---VMTQEN----CLIASLKVREQIALS---------LKIYDAYSKINIDDLLKKFRL-TEQSEVIVDQLSGGQKRRLA 203
Cdd:PRK10762 326 AngiVYISEDrkrdGLVLGMSVKENMSLTalryfsragGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVA 405
|
170 180
....*....|....*....|..
gi 1726007896 204 LLLTLIKPSKLLILDEPTVGMD 225
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
76-275 |
2.25e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 76 ELKNLNKSFKN--PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSV---------VKHFNAQDDLSVMT 144
Cdd:PRK13657 336 EFDDVSFSYDNsrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 QENCLIA-----SLKVREQIALSLKIYDAYSKINIDDLLKkfRLTEQSEVIV----DQLSGGQKRRLALLLTLIKPSKLL 215
Cdd:PRK13657 416 QDAGLFNrsiedNIRVGRPDATDEEMRAAAERAQAHDFIE--RKPDGYDTVVgergRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 216 ILDEPTVGMDLESIDLFWDYLDHV--GGSVVTITHDFNQIDNYfTRVVLLKDG-VIKS---DESVA 275
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRNA-DRILVFDNGrVVESgsfDELVA 558
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
74-266 |
3.10e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKN-----PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIL------------GNIIpDKGSVVKHFNA 136
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsppvvypsGDIR-FHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 137 Q-------DDLSVMTQENclIASLK----VREQIA--LSL-----------KIYDAYSKINIDDLLKkfRLTEQSEvivd 192
Cdd:PRK15134 84 QtlrgvrgNKIAMIFQEP--MVSLNplhtLEKQLYevLSLhrgmrreaargEILNCLDRVGIRQAAK--RLTDYPH---- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 193 QLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL----ESIDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
67-271 |
3.74e-05 |
|
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: 44.82 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 67 HTHGDaLILELKNLNK-SFKNPVLK---DVNLSIYGRDRIALLGSNGSGKTTIVNTILG--------NIIPDkGSVVKHF 134
Cdd:TIGR02633 251 HEIGD-VILEARNLTCwDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegNVFIN-GKPVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 135 NAQDDLS---VMTQEN----CLIASLKVREQIALS-LKIYDAYSKIN-------IDDLLKKFRL-TEQSEVIVDQLSGGQ 198
Cdd:TIGR02633 329 NPAQAIRagiAMVPEDrkrhGIVPILGVGKNITLSvLKSFCFKMRIDaaaelqiIGSAIQRLKVkTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1726007896 199 KRRLALLLTLIKPSKLLILDEPTVGMDLES---IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSD 271
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
87-221 |
3.95e-05 |
|
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: 44.81 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQDdLSVMTQencliASLkvREQIAL----- 161
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI--LIDGQD-IRDVTQ-----ASL--RAAIGIvpqdt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 162 -----SL--------------KIYDAYSKINIDDLLKkfRLTEQSEVIVDQ----LSGGQKRRLALLLTLIKPSKLLILD 218
Cdd:COG5265 442 vlfndTIayniaygrpdaseeEVEAAARAAQIHDFIE--SLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
...
gi 1726007896 219 EPT 221
Cdd:COG5265 520 EAT 522
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-266 |
4.80e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 103 ALLGSNGSGKTTIVNTILGNI---IPDKGSVVKHFNAQDD-----LSVMTQENCLIASLKVREQIALS--------LKIY 166
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSsfqrsIGYVQQQDLHLPTSTVRESLRFSaylrqpksVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 167 DAYSKIniDDLLKKFRLTEQSEVIV----DQLSGGQKRRLALLLTLI-KPSKLLILDEPTVGMDLES----IDLFWDYLD 237
Cdd:TIGR00956 873 EKMEYV--EEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTawsiCKLMRKLAD 950
|
170 180
....*....|....*....|....*....
gi 1726007896 238 HVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:TIGR00956 951 HGQAILCTIHQPSAILFEEFDRLLLLQKG 979
|
|
| COG1395 |
COG1395 |
Predicted transcriptional regulator [Transcription]; |
12-56 |
5.77e-05 |
|
Predicted transcriptional regulator [Transcription];
Pssm-ID: 441005 [Multi-domain] Cd Length: 313 Bit Score: 44.06 E-value: 5.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1726007896 12 LRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIF 56
Cdd:COG1395 135 LREERGLSLGELASELGVSRRTISKYERGEMDASIEVALKLEEIL 179
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
67-225 |
7.08e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 67 HTHGDaLILELKNLNK-SFKNPVLK---DVNLSIYGRDRIALLGSNGSGKTTIVNTILG--------NIIPDkGSVVKHF 134
Cdd:PRK13549 253 HTIGE-VILEVRNLTAwDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaypgrwegEIFID-GKPVKIR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 135 NAQDDLS---VMTQEN----CLIASLKVREQIALS-LKIYDAYSKIN-------IDDLLKKFRL-TEQSEVIVDQLSGG- 197
Cdd:PRK13549 331 NPQQAIAqgiAMVPEDrkrdGIVPVMGVGKNITLAaLDRFTGGSRIDdaaelktILESIQRLKVkTASPELAIARLSGGn 410
|
170 180
....*....|....*....|....*....
gi 1726007896 198 -QKRRLALLLtLIKPsKLLILDEPTVGMD 225
Cdd:PRK13549 411 qQKAVLAKCL-LLNP-KILILDEPTRGID 437
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
74-258 |
7.48e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLN-KSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVvkhFNAQDDLSVMTQEnclias 152
Cdd:PRK10247 7 LLQLQNVGyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---LFEGEDISTLKPE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 153 lKVREQIALSLK--------IYDAY------------SKINIDDLLKkFRLTEQS-EVIVDQLSGGQKRRLALLLTLIKP 211
Cdd:PRK10247 78 -IYRQQVSYCAQtptlfgdtVYDNLifpwqirnqqpdPAIFLDDLER-FALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 212 SKLLILDEPTVGMDLESI----DLFWDYLDHVGGSVVTITHDFNQI---DNYFT 258
Cdd:PRK10247 156 PKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEInhaDKVIT 209
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
75-250 |
8.75e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnKSFKNPVLKDVNLSIygrdrIALLGSNGSGKTTIVNTI---LGniipdkGSVVKHFNAQDDLSVMTQENCLI- 150
Cdd:COG0419 5 LRLENF-RSYRDTETIDFDDGL-----NLIVGPNGAGKSTILEAIryaLY------GKARSRSKLRSDLINVGSEEASVe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 151 ------------------------ASLKVREQI---ALSLKIYDAYSK---------------INIDDLLKKFRLTEQSE 188
Cdd:COG0419 73 lefehggkryrierrqgefaefleAKPSERKEAlkrLLGLEIYEELKErlkeleealesaleeLAELQKLKQEILAQLSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726007896 189 VI-VDQLSGGQKRRLALLLTLikpskLLILDepTVGMDLESIDLFWDYLDhvggSVVTITHDF 250
Cdd:COG0419 153 LDpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALE----ELAIITHVI 204
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-254 |
9.94e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnaqddlsvmtqencliaslkvreqialslkiydaysKINIDDLLKKF 181
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 182 RLTEQSEVIV-DQLSGGQKRRLALLLTLIK--PSKLLILDEPT---------VGMDLESIDLFWDYLDHVGGSVVTITHD 249
Cdd:smart00382 46 LDQLLLIIVGgKKASGSGELRLRLALALARklKPDVLILDEITslldaeqeaLLLLLEELRLLLLLKSEKNLTVILTTND 125
|
....*
gi 1726007896 250 FNQID 254
Cdd:smart00382 126 EKDLG 130
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
74-236 |
1.01e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLN--KSFKNPVLKDVNLS-----IYGrdrIAllGSNGSGKTTIVNTILGNIIPDKGSVvkHFNAQD--DLSVMT 144
Cdd:COG3845 257 VLEVENLSvrDDRGVPALKDVSLEvrageILG---IA--GVAGNGQSELAEALAGLRPPASGSI--RLDGEDitGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 145 -------------QENCLIASLKVREQIALslKIYD--AYSK---INID-------DLLKKFRL-TEQSEVIVDQLSGG- 197
Cdd:COG3845 330 rrrlgvayipedrLGRGLVPDMSVAENLIL--GRYRrpPFSRggfLDRKairafaeELIEEFDVrTPGPDTPARSLSGGn 407
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1726007896 198 -QKrrlaLLL--TLIKPSKLLILDEPTVGMDLESIDLFWDYL 236
Cdd:COG3845 408 qQK----VILarELSRDPKLLIAAQPTRGLDVGAIEFIHQRL 445
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
68-252 |
1.02e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.85 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 68 THGDALILELKNLNKSF-KNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTI--LGNIIPD---KGSVV---KHFNAQD 138
Cdd:PRK14243 4 LNGTETVLRTENLNVYYgSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTfhgKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 dlsvmtqenclIASLKVREQIALSLK--------IYD--AYS------KINIDDL----LKKFRLTEQSEVIVDQ----L 194
Cdd:PRK14243 84 -----------VDPVEVRRRIGMVFQkpnpfpksIYDniAYGaringyKGDMDELversLRQAALWDEVKDKLKQsglsL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 195 SGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWDYLDHVGG--SVVTITHDFNQ 252
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHNMQQ 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
194-249 |
1.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 194 LSGGQKRRLALLLTLIKPSK---LLILDEPTVGM---DLESIDLFWDYLDHVGGSVVTITHD 249
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| PRK09706 |
PRK09706 |
transcriptional repressor DicA; Reviewed |
1-66 |
1.43e-04 |
|
transcriptional repressor DicA; Reviewed
Pssm-ID: 182039 [Multi-domain] Cd Length: 135 Bit Score: 40.99 E-value: 1.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 1 MENI-FKSQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAG 66
Cdd:PRK09706 1 MKNLtLGQRIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEPTGKNLFALAKALQCSPTWLLFG 67
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
102-249 |
1.54e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNI-IPDKGSVVK-HFNAQD---------------DLSVMTQE--NCLIASLKVREQIALS 162
Cdd:PRK11022 36 VGIVGESGSGKSVSSLAIMGLIdYPGRVMAEKlEFNGQDlqrisekerrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 163 LKIYDAYSKINID----DLLKKFRLTEQS---EVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDL----ESIDL 231
Cdd:PRK11022 116 IKVHQGGNKKTRRqraiDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIEL 195
|
170
....*....|....*...
gi 1726007896 232 FWDYLDHVGGSVVTITHD 249
Cdd:PRK11022 196 LLELQQKENMALVLITHD 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-266 |
1.63e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.34 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNtILGNIIPDKGSVVK----------------HFNAQDDLSVMTQENCLIA 151
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKvdgkvlyfgkdifqidAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 152 SLKVREQIALSLKIYDAYSKINI----DDLLKKFRLTEQSEVIVD----QLSGGQKRRLALLLTLIKPSKLLILDEPTVG 223
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIkkivEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1726007896 224 MDLESIDLFWDYLDHVGG--SVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
75-225 |
1.99e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.15 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFK---NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTIL------GNIIPDKGS--VVKHFNAQDDLSVM 143
Cdd:cd03289 3 MTVKDLTAKYTeggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIDGVSwnSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 144 TQEnCLIASLKVREQIalslkiyDAYSKINIDDLLKkfrLTEQS--EVIVDQ---------------LSGGQKRRLALLL 206
Cdd:cd03289 83 PQK-VFIFSGTFRKNL-------DPYGKWSDEEIWK---VAEEVglKSVIEQfpgqldfvlvdggcvLSHGHKQLMCLAR 151
|
170
....*....|....*....
gi 1726007896 207 TLIKPSKLLILDEPTVGMD 225
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLD 170
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
89-268 |
2.09e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.33 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV-------KHFNAQ------DDLSVMTQENCLIASLKV 155
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiaKISDAElrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 156 REQIALSLK---IYDAYSKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD----LES 228
Cdd:PRK10070 124 LDNTAFGMElagINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1726007896 229 IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVI 268
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-247 |
2.52e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 138 DDLSVMTQENCLIASLKVREQIALSlKIYDAYSKINIDDLLKKfrLTEQSEVIV----DQLSGGQKRRLALLLTLIKPSK 213
Cdd:PTZ00265 523 NDMSNTTDSNELIEMRKNYQTIKDS-EVVDVSKKVLIHDFVSA--LPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPK 599
|
90 100 110
....*....|....*....|....*....|....
gi 1726007896 214 LLILDEPTVGMDLESIDLFWDYLDHVGGSVVTIT 247
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
195-249 |
2.60e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 2.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 195 SGGQKRRLALLLTLIKPSKLLILDEPTVGMDLeSI-----DLFWDYLDHVGGSVVTITHD 249
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVqaqvlNLMMDLQQELGLSYVFISHD 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
86-219 |
2.61e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 86 NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDD---------LSVMTQENCLIaSLKVR 156
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldswrsrLAVVSQTPFLF-SDTVA 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 157 EQIAL------SLKIYDAYSKINI-DDLLkkfRL-----TEQSEVIVdQLSGGQKRRLALLLTLIKPSKLLILDE 219
Cdd:PRK10789 407 NNIALgrpdatQQEIEHVARLASVhDDIL---RLpqgydTEVGERGV-MLSGGQKQRISIARALLLNAEILILDD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
102-263 |
2.96e-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: 40.63 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 102 IALLGSNGSGKTTIVNTILGNIIPDKGsvvkhfnaqddlsvmtqencliaslkvreqialslkiydayskiniDDLLKKF 181
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGD----------------------------------------------NDEWDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 182 RLTEQSEVIvdQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLE----SIDLFWDYLDHVGGSVVTITHDFNQIDNYF 257
Cdd:cd03222 62 TPVYKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
....*.
gi 1726007896 258 TRVVLL 263
Cdd:cd03222 140 DRIHVF 145
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
74-255 |
2.98e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVKHFNAQDDL-----SVMTQENC 148
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIakpycTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 149 LIASLKVREQIALSLKIYDaySKINIDDLLKKFRLTEQSEVIVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLES 228
Cdd:PRK13541 81 LKLEMTVFENLKFWSEIYN--SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180 190
....*....|....*....|....*....|
gi 1726007896 229 IDLFWDYL---DHVGGSVVTITHDFNQIDN 255
Cdd:PRK13541 159 RDLLNNLIvmkANSGGIVLLSSHLESSIKS 188
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
74-253 |
3.18e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.81 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFKNP-----VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGnIIPDKGSVVK---HFNAQD------- 138
Cdd:COG4170 3 LLDIRNLTIEIDTPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTAdrfRWNGIDllklspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 139 --------DLSVMTQE--NCLIASLKVREQIALSL-------KIYD--AYSKINIDDLLKKFRLTEQSEVIVD---QLSG 196
Cdd:COG4170 82 errkiigrEIAMIFQEpsSCLDPSAKIGDQLIEAIpswtfkgKWWQrfKWRKKRAIELLHRVGIKDHKDIMNSyphELTE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 197 GQKRRLALLLTLIKPSKLLILDEPTVGMdlESID------LFwDYLDHVGG-SVVTITHDFNQI 253
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAM--ESTTqaqifrLL-ARLNQLQGtSILLISHDLESI 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
194-249 |
3.45e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 3.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 194 LSGGQKRRLALLLTLIKPSK---LLILDEPTVGMDLESIDLFWDYLDHV---GGSVVTITHD 249
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvdkGNTVVVIEHN 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
194-253 |
3.53e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 3.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 194 LSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDL----FWDYLDHVGGSVVTITHDFNQI 253
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLiektIVDIKDKADKTIITIAHRIASI 1422
|
|
| CxxCG_CxxCG_HTH |
TIGR03830 |
putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of ... |
7-50 |
6.13e-04 |
|
putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of predicted regulatory proteins with a conserved zinc finger/HTH architecture. The amino-terminal region contains a novel domain, featuring two CXXC motifs and occuring in a number of small bacterial proteins as well as in the present family. The carboxyl-terminal region consists of a helix-turn-helix domain, modeled by pfam01381. The predicted function is DNA binding and transcriptional regulation.
Pssm-ID: 274805 [Multi-domain] Cd Length: 127 Bit Score: 39.15 E-value: 6.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1726007896 7 SQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPN--IDKLI 50
Cdd:TIGR03830 68 PEIRRIRKKLGLSQREAAELLGGGVNAFSRYERGEVRPSkaLDKLL 113
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
88-244 |
6.61e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 88 VLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVVkhfnAQDDLSVMTQEnCLIASLKVREQIALslkiYD 167
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----AERSIAYVPQQ-AWIMNATVRGNILF----FD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 168 AYSKINIDDLLKKFRL------------TEQSEVIVDqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLesidlfwdy 235
Cdd:PTZ00243 746 EEDAARLADAVRVSQLeadlaqlgggleTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDA--------- 815
|
....*....
gi 1726007896 236 ldHVGGSVV 244
Cdd:PTZ00243 816 --HVGERVV 822
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
74-229 |
6.62e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 74 ILELKNLNKSFK-NPVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILG--NIIPDKGSVVkhFNAQDDLSVMTQE---- 146
Cdd:PRK09580 1 MLSIKDLHVSVEdKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVE--FKGKDLLELSPEDrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 147 ----------------------NCLIASLKVREQIALslkiydaySKINIDDLLK-KFRLTEQSEVIVDQ-----LSGGQ 198
Cdd:PRK09580 79 gifmafqypveipgvsnqfflqTALNAVRSYRGQEPL--------DRFDFQDLMEeKIALLKMPEDLLTRsvnvgFSGGE 150
|
170 180 190
....*....|....*....|....*....|.
gi 1726007896 199 KRRLALLLTLIKPSKLLILDEPTVGMDLESI 229
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDAL 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
89-249 |
7.38e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 89 LKDVNLSIYGRDRIALLGSNGSGKTTIVNTilgniipdkgsvvkhfnaqddlsvmtqenCLIASLKVReqIALSLKIYDA 168
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------------------------GLYASGKAR--LISFLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 169 YSKINIDDL--LKKFRLTEQS-EVIVDQLSGGQKRRLALLLTLIKPSK--LLILDEPTVGMDLESIDLFWDYLDHV---G 240
Cdd:cd03238 60 NKLIFIDQLqfLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlG 139
|
....*....
gi 1726007896 241 GSVVTITHD 249
Cdd:cd03238 140 NTVILIEHN 148
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
5-67 |
1.12e-03 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 40.11 E-value: 1.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 5 FKSQLSALRQKKHLSQELLAQKLF-----VSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLAGH 67
Cdd:PRK13355 4 FAERLKQAMKARGLKQEDLVHAAEargvkLGKSHISQYVSGKTGPRRDVLPFLAAILGVSEDWLLGGE 71
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
75-277 |
1.24e-03 |
|
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: 39.51 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKN---PVLKDVNLSIYGRDRIALLGSNGSGKTTI-------VNTILGNIIPDKGSVVK---HfNAQDDLS 141
Cdd:cd03288 20 IKIHDLCVRYENnlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKlplH-TLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 142 VMTQENCLIA-SLKVR---EQIALSLKIYDAYSKINIDDLLKKFR------LTEQSEvivdQLSGGQKRRLALLLTLIKP 211
Cdd:cd03288 99 IILQDPILFSgSIRFNldpECKCTDDRLWEALEIAQLKNMVKSLPggldavVTEGGE----NFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726007896 212 SKLLILDEPTVGMDLESIDLFWDYL--DHVGGSVVTITHDFNQIDNYfTRVVLLKDGVIKSDESVANI 277
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVmtAFADRTVVTIAHRVSTILDA-DLVLVLSRGILVECDTPENL 241
|
|
| couple_hipB |
TIGR03070 |
transcriptional regulator, y4mF family; Members of this family belong to a clade of ... |
7-60 |
1.32e-03 |
|
transcriptional regulator, y4mF family; Members of this family belong to a clade of helix-turn-helix DNA-binding proteins, among the larger family pfam01381 (HTH_3; Helix-turn-helix). Members are similar in sequence to the HipB protein of E. coli. Genes for members of the seed alignment for this protein family were found to be closely linked to genes encoding proteins related to HipA. The HibBA operon appears to have some features in common with toxin-antitoxin post-segregational killing systems. [Regulatory functions, DNA interactions]
Pssm-ID: 213767 [Multi-domain] Cd Length: 58 Bit Score: 36.48 E-value: 1.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1726007896 7 SQLSALRQKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNL 60
Cdd:TIGR03070 5 ILVRARRKALGLTQADLADLAGVGLRFIRDLENGKPTVRLDKVLRVLDALGLEL 58
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
87-225 |
2.46e-03 |
|
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: 39.54 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 87 PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIipDKgsVVKHFNAQDDLSVMTQEnCLIASLKVREQIALSLKIY 166
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM--DK--VEGHVHMKGSVAYVPQQ-AWIQNDSLRENILFGKALN 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726007896 167 DAYSKINID--------DLLKKFRLTEQSEVIVDqLSGGQKRRLALLLTLIKPSKLLILDEPTVGMD 225
Cdd:TIGR00957 727 EKYYQQVLEacallpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-249 |
3.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 169 YSKINI---DDLLKKFRLTEQSEVIVDQLSGGQK------RRLALLLTLIKPSKLLILDEPTVGMDLES----IDLFWDY 235
Cdd:PRK03918 761 YSGVRVkaeENKVKLFVVYQGKERPLTFLSGGERialglaFRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERY 840
|
90
....*....|....
gi 1726007896 236 LDHVgGSVVTITHD 249
Cdd:PRK03918 841 LRKI-PQVIIVSHD 853
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
157-263 |
3.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 157 EQIALSLKIYDAYS-KINIDDLLKKFRLTEQSEV-IVDQLSGGQKRRLALLLTLIKPSKLLILDEPTVGMDLESIDLFWD 234
Cdd:PLN03073 306 EEIYKRLELIDAYTaEARAASILAGLSFTPEMQVkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLET 385
|
90 100
....*....|....*....|....*....
gi 1726007896 235 YLDHVGGSVVTITHDFNQIDNYFTRVVLL 263
Cdd:PLN03073 386 YLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| VapI |
COG3093 |
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ... |
14-65 |
3.91e-03 |
|
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];
Pssm-ID: 442327 [Multi-domain] Cd Length: 87 Bit Score: 35.94 E-value: 3.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1726007896 14 QKKHLSQELLAQKLFVSRQSISKWENGESEPNIDKLISISEIFSVNLDFLLA 65
Cdd:COG3093 19 EPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEFWLN 70
|
|
| HTH_31 |
pfam13560 |
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA. |
8-41 |
4.04e-03 |
|
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
Pssm-ID: 433309 [Multi-domain] Cd Length: 64 Bit Score: 35.20 E-value: 4.04e-03
10 20 30
....*....|....*....|....*....|....
gi 1726007896 8 QLSALRQKKHLSQELLAQKLFVSRQSISKWENGE 41
Cdd:pfam13560 5 RLRRLRERAGLSQEALARRLGVSRSTLSRLETGR 38
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
75-282 |
4.65e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 37.76 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLNKSFKNPVLKDVNLSIYgRDRI-ALLGSNGSGKTTI-----------VNTILGNIIPD---------KGSVV-- 131
Cdd:PRK10418 5 IELRNIALQAAQPLVHGVSLTLQ-RGRVlALVGGSGSGKSLTcaaalgilpagVRQTAGRVLLDgkpvapcalRGRKIat 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 132 ------KHFNAQDDLSVMTQENCLIASLKVREqiALSLKIYDAYSKINIDDLLKKFRLteqsevivdQLSGGQKRRLALL 205
Cdd:PRK10418 84 imqnprSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAARVLKLYPF---------EMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 206 LTLIKPSKLLILDEPTVGMDLES----IDLFWDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDGVIKSDESVANIHSNN 281
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
.
gi 1726007896 282 Q 282
Cdd:PRK10418 233 K 233
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
75-236 |
7.32e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 36.52 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 75 LELKNLnKSFKNPVLKDvnlsiyGRDRI-ALLGSNGSGKTTIVNTIlgniipdkgSVVkhfnaqddLSVMTQEnCLIASL 153
Cdd:cd03239 4 ITLKNF-KSYRDETVVG------GSNSFnAIVGPNGSGKSNIVDAI---------CFV--------LGGKAAK-LRRGSL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 154 KVREQIALSLKIYDAYSKINIDdllKKFRLTEQSEVivDQ-LSGGQKRRLALLLTL----IKPSKLLILDEPTVGMDLES 228
Cdd:cd03239 59 LFLAGGGVKAGINSASVEITFD---KSYFLVLQGKV--EQiLSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTN 133
|
....*...
gi 1726007896 229 IDLFWDYL 236
Cdd:cd03239 134 RRRVSDMI 141
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
102-121 |
7.81e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 7.81e-03
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
77-266 |
8.82e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 77 LKNLNKSFKN-PVLKDVNLSIYGRDRIALLGSNGSGKTTIVNTILGNIIPDKGSVV---KHFN-------AQDDLSVMTQ 145
Cdd:PRK10982 1 MSNISKSFPGvKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqgKEIDfksskeaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726007896 146 ENCLIASLKVREQIALSL-----------KIYDAYSKInIDDLLKKFRLTEQseviVDQLSGGQKRRLALLLTLIKPSKL 214
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRyptkgmfvdqdKMYRDTKAI-FDELDIDIDPRAK----VATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1726007896 215 LILDEPTVGMDLESID-LF--WDYLDHVGGSVVTITHDFNQIDNYFTRVVLLKDG 266
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNhLFtiIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
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