|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-227 |
1.36e-85 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 254.24 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-----RPVIGWLAQ 83
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprraRRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVM 163
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 164 LDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQRACWGATRAVL 227
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-221 |
1.23e-68 |
|
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: 210.08 E-value: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-----RPVIGWLAQRHALE 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekeRKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 SQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPF 168
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 169 TGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQRACWG 221
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-212 |
6.01e-58 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 182.05 E-value: 6.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 21 GYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPViGWLAQRHALESQFPLNVQDVVS 100
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV-AYVPQRSEVPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELM 180
Cdd:NF040873 80 MGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|..
gi 1119115049 181 DLILEMYRQGQTILAVLHDNQRVADFFPETLL 212
Cdd:NF040873 160 ALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-227 |
1.99e-54 |
|
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: 174.85 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPV-----------IGW 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLaslsrrelarrIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHalESQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAP 160
Cdd:COG1120 80 VPQEP--PAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 161 LVMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHD-NQ--RVADFFpetLLLTPQR-ACWGATRAVL 227
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDlNLaaRYADRL---VLLKDGRiVAQGPPEEVL 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-205 |
4.97e-44 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 148.62 E-value: 4.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGW----LAQRHAL 87
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISMLssrqLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQFPL-----NVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLV 162
Cdd:PRK11231 81 LPQHHLtpegiTVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 163 MLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD-NQ--RVAD 205
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDlNQasRYCD 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-199 |
2.99e-41 |
|
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: 139.92 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVIGWL 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALESQFPL--NVQdvvsqgawpgvsLLRGLGGC--TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:COG4133 81 GHADGLKPELTVreNLR------------FWAALYGLraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-213 |
3.45e-40 |
|
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: 137.21 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHAL--- 87
Cdd:cd03225 1 ELKNLSFSYPDGA-RPALDDIsltIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 -----ESQF-PLNVQDVVSQGawpgvslLRGLGGC---TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQ 158
Cdd:cd03225 80 vfqnpDDQFfGPTVEEEVAFG-------LENLGLPeeeIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 159 APLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-227 |
4.50e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 4.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPV-IgwL 81
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaERPVsM--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALesqFP-LNVQDVVSQGAWPGvslLRgLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAP 160
Cdd:COG3840 77 FQENNL---FPhLTVAQNIGLGLRPG---LK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119115049 161 LVMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHDNQRVADFFPETLLLTPQRACW-GATRAVL 227
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAAdGPTAALL 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-205 |
2.91e-38 |
|
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: 131.40 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGW----LAQRHAles 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK-DLASLspkeLARKIA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 qfplnvqdVVSQgawpgvsllrglggctrrrigaVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:cd03214 77 --------YVPQ----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119115049 170 GIDEATSRELMDLILEMYRQ-GQTILAVLHD-NQ--RVAD 205
Cdd:cd03214 127 HLDIAHQIELLELLRRLARErGKTVVMVLHDlNLaaRYAD 166
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-205 |
1.15e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.34 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV---------IGWLAQ 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQfpLNVQDVVSQGAWpgvslLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLV 162
Cdd:COG1131 81 EPALYPD--LTVRENLRFFAR-----LYGLPRKEAReRIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 163 MLDEPFTGIDEATSRELMDLILEMYRQGQTIL---AVLHDNQRVAD 205
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLlstHYLEEAERLCD 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-227 |
4.04e-37 |
|
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: 129.76 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvaITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---RPVIGWLAQRHA 86
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVslsIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 87 LESQFPLN------VQDVVSQGawpgvslLRGLGGC---TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:COG1122 79 LVFQNPDDqlfaptVEEDVAFG-------PENLGLPreeIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQR-ACWGATRAVL 227
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRiVADGTPREVF 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-199 |
1.13e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.77 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGW----LAQRHAL 87
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG-RPLAAWspweLARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQ-----FPLNVQDVVSQGAWPGvsllRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ----- 157
Cdd:COG4559 80 LPQhsslaFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 158 --QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-199 |
1.53e-34 |
|
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: 122.63 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----RPV----IGWLAQR 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgVPPerrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 85 HALesqFP-LNVQDVVSQGawpgVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVM 163
Cdd:cd03259 81 YAL---FPhLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119115049 164 LDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElGITTIYVTHD 190
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-199 |
1.05e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 121.32 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHAL 87
Cdd:COG3638 1 PMLELRNLSKRYPGG--TPALDDVsleIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ES-------QFPL----NVQDVVSQGAWPGVSLLRGLGGC----TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFA 152
Cdd:COG3638 79 RRrigmifqQFNLvprlSVLTNVLAGRLGRTSTWRSLLGLfppeDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119115049 153 RVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHD 199
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQ 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-199 |
5.30e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 8 GDAAMIELEQLVAGYD-GVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR-----PVI 78
Cdd:COG1116 3 AAAPALELRGVSKRFPtGGGGVTALDDVsltVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALesqFP-LNVQDVVSQGAwpgvsLLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMV 156
Cdd:COG1116 83 GVVFQEPAL---LPwLTVLDNVALGL-----ELRGVPKAERReRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 157 QQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-208 |
5.38e-33 |
|
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: 119.60 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------RPVI 78
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALESQfpLNVQDVVSQGAWPGVSLLRGLGGC----TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARV 154
Cdd:cd03256 81 GMIFQQFNLIER--LSVLENVLSGRLGRRSTWRSLFGLfpkeEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQRVADFFP 208
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYAD 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-199 |
9.34e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.11 E-value: 9.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGW----LAQRHA 86
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLADWspaeLARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 87 LESQ-----FPLNVQDVVSQGAWPGVSLLRGlggcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ---- 157
Cdd:PRK13548 80 VLPQhsslsFPFTVEEVVAMGRAPHGLSRAE----DDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 158 --QAPLVMLDEPFTGIDEATSRELMDLILEM-YRQGQTILAVLHD 199
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHD 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-199 |
1.38e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.97 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPvIG 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppeKRN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHALesqFP-LNVQDVVSQGawpgvslLRGLG---GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVM 155
Cdd:COG3842 81 MVFQDYAL---FPhLTVAENVAFG-------LRMRGvpkAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHD 195
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-207 |
2.03e-32 |
|
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: 117.21 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYD-GVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------- 74
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVslsIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 RPVIGWLAQRHALESQfpLNVQDVVSQGAwpgvsLLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFAR 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPD--LTALENVELPL-----LLAGVPKKERReRAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 154 VMVQQAPLVMLDEPfTG-IDEATSRELMDLILEMYRQ-GQTILAVLHDNqRVADFF 207
Cdd:cd03255 154 ALANDPKIILADEP-TGnLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYA 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
37-199 |
3.54e-32 |
|
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: 116.80 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-----RPVIGWLAQRHALesqFP-LNVQDVVSQGAwpgvsLL 110
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpGPDRGYVFQQDAL---LPwLTVLDNVALGL-----EL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 RGLGGCTRR-RIGAVLERVGLAGLA-KTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR 188
Cdd:cd03293 101 QGVPKAEAReRAEELLELVGLSGFEnAYPHQ-LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWR 179
|
170
....*....|..
gi 1119115049 189 Q-GQTILAVLHD 199
Cdd:cd03293 180 EtGKTVLLVTHD 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-199 |
6.39e-31 |
|
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: 119.49 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------R 75
Cdd:COG4987 330 GGPSLELEDVSFRYPG-AGRPVLDGLsltLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 76 PVIGWLAQRHALesqFPLNVQDvvsqgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPI----EALSGG 144
Cdd:COG4987 409 RRIAVVPQRPHL---FDTTLRE----------NLRLARPDATDEELWAALERVGLGDWLAalpdgldTWLgeggRRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 145 QFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEmYRQGQTILAVLHD 199
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHR 529
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-217 |
1.44e-30 |
|
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: 110.80 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRhalesqfpl 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 94 nvqdvvsqgawpgvsllrglggctRRRIGAVLErvglaglaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDE 173
Cdd:cd00267 72 ------------------------RRRIGYVPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 174 ATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQR 217
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-213 |
1.75e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.44 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQLVAGY-DGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------- 74
Cdd:COG1136 2 SPLLELRNLTKSYgTGEGEVTALRGVslsIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 ---RPVIGWLAQRHALesqFP-LNVQDVVsqgAWPgvSLLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRM 149
Cdd:COG1136 82 rlrRRHIGFVFQFFNL---LPeLTALENV---ALP--LLLAGVSRKERReRARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 150 LFARVMVQQAPLVMLDEPfTG-IDEATSRELMDLILEMYRQ-GQTILAVLHDnQRVADFFPETLLL 213
Cdd:COG1136 154 AIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRL 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-205 |
2.51e-30 |
|
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: 110.57 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVigwlaqRHALEsqfp 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK------KEPEE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 lnvqdvvsqgawpgvsllrglggcTRRRIGAVLERVGL-AGLakTPIE--ALSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:cd03230 71 ------------------------VKRRIGYLPEEPSLyENL--TVREnlKLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119115049 170 GIDEATSRELMDLILEMYRQGQTIL---AVLHDNQRVAD 205
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILlssHILEEAERLCD 163
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-205 |
3.84e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR----PVIGW------LA 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsamPPPEWrrqvayVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 QRHALesqFPLNVQDVVsqgawPGVSLLRGLGGcTRRRIGAVLERVGL-AGLAKTPIEALSGGQFQRMLFARVMVQQAPL 161
Cdd:COG4619 81 QEPAL---WGGTVRDNL-----PFPFQLRERKF-DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119115049 162 VMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDN---QRVAD 205
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPeqiERVAD 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
38-229 |
5.12e-30 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 112.67 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG-------KRPVIGWLAQRHALESQFPLNVQDVVSQGAWPGVSLL 110
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 RGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQG 190
Cdd:PRK15056 113 RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119115049 191 QTILAVLHDNQRVADFFPETLLLTPQRACWGATRAVLPA 229
Cdd:PRK15056 193 KTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTA 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-205 |
8.07e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.93 E-value: 8.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWqGKRPVIGWLAQ-RHALESQ 90
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIGYFDQhQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 91 fpLNVQDVVSQGAwpgvsllrglGGCTRRRIGAVLERVGLAG-LAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPft 169
Cdd:COG0488 394 --KTVLDELRDGA----------PGGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP-- 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 170 gideaT------SRELMDLILEMYrQGqTILAVLHDN---QRVAD 205
Cdd:COG0488 460 -----TnhldieTLEALEEALDDF-PG-TVLLVSHDRyflDRVAT 497
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-199 |
3.66e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDG-VAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLA---- 82
Cdd:COG4525 2 SMLTVRHVSVRYPGgGQPQPALQDVsltIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVTGPGAdrgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 --QRHALesqFP-LNVQDVVSQGawpgvsL-LRGLGGCTRRRI-GAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:COG4525 81 vfQKDAL---LPwLNVLDNVAFG------LrLRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 158 QAPLVMLDEPFTGIDEATsRELM-DLILEMYRQ-GQTILAVLHD 199
Cdd:COG4525 152 DPRFLLMDEPFGALDALT-REQMqELLLDVWQRtGKGVFLITHS 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-227 |
4.50e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.90 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPViGWLA 82
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLT--VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsRRPV-SMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 QRHALesqFP-LNVQDVVSQGAWPGvslLRgLGGCTRRRIGAVLERVGLAG-LAKTPIEaLSGGQFQRMLFARVMVQQAP 160
Cdd:PRK10771 78 QENNL---FShLTVAQNIGLGLNPG---LK-LNAAQREKLHAIARQMGIEDlLARLPGQ-LSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 161 LVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLH---DNQRVAdffPETLLLTPQRACW-GATRAVL 227
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHsleDAARIA---PRSLVVADGRIAWdGPTDELL 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-201 |
5.00e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 109.69 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 16 EQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR----------PVIGWLAQRH 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 86 ALESQfpLNVQDVVSQGAWPGVSLLrglggcTRRR------IGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:PRK10253 91 TTPGD--ITVQELVARGRYPHQPLF------TRWRkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 160 PLVMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHD-NQ 201
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDlNQ 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
38-205 |
5.30e-29 |
|
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: 108.35 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPViGWLAQRHALesqFP-LNVQDVVSQGAWPGV 107
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappaDRPV-SMLFQENNL---FAhLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLlrglGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY 187
Cdd:cd03298 100 KL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180
....*....|....*....|..
gi 1119115049 188 RQ-GQTILAVLH---DNQRVAD 205
Cdd:cd03298 176 AEtKMTVLMVTHqpeDAKRLAQ 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-205 |
6.18e-29 |
|
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: 108.79 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALeSQF 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 PlnvqdvVSQGAWPGVSL---------LRGL-GGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPL 161
Cdd:COG4555 80 P------DERGLYDRLTVreniryfaeLYGLfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 162 VMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVAD 205
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEA 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-205 |
6.34e-29 |
|
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: 113.70 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 5 LVGGDAAMIELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK--------- 74
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpas 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 -RPVIGWLAQRHALesqFPLNVQDVvsqgawpgvsLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPIEA----LS 142
Cdd:COG4988 409 wRRQIAWVPQNPYL---FAGTIREN----------LRLGRPDASDEELEAALEAAGLDEFVAalpdgldTPLGEggrgLS 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 143 GGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLHD--NQRVAD 205
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRlaLLAQAD 539
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-199 |
7.64e-29 |
|
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: 107.44 E-value: 7.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRP---------VIGWLAQ 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrdepheNILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQFplnvqdvvsqGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVM 163
Cdd:TIGR01189 81 LPGLKPEL----------SALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119115049 164 LDEPFTGIDEATSRELMDLILE-MYRQGQTILAVLHD 199
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQD 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
37-198 |
1.34e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.88 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------RPVIGWLAQRHALESQfpLNVQDvvsqgawpGVSL 109
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvAEACHYLGHRNAMKPA--LTVAE--------NLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ 189
Cdd:PRK13539 97 WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQ 176
|
....*....
gi 1119115049 190 GQTILAVLH 198
Cdd:PRK13539 177 GGIVIAATH 185
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-169 |
1.53e-28 |
|
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: 105.42 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWLAQRHALesqFP-LNVQDV 98
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslRKEIGYVFQDPQL---FPrLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 99 VSQGAwpgvsLLRGLGGCTR-RRIGAVLERVGLAGLAKTPIEA----LSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:pfam00005 80 LRLGL-----LLKGLSKREKdARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-199 |
2.03e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.86 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGW----LAQRHAL 87
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL-DVATTpsreLAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ---ESQFP--LNVQDVVSQGAWPgVSllRG-LGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPL 161
Cdd:COG4604 80 lrqENHINsrLTVRELVAFGRFP-YS--KGrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119115049 162 VMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHD 199
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHD 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-199 |
2.18e-28 |
|
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: 107.38 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------RPV 77
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 78 IGWLAQRHALESqfPLNV-QDVV-----SQGAWPGvsLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLF 151
Cdd:TIGR02315 81 IGMIFQHYNLIE--RLTVlENVLhgrlgYKPTWRS--LLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQ 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
37-199 |
2.28e-28 |
|
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: 107.14 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLAQRHA---------LESQFP-LNVQDVV------S 100
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG-EDITGLPPHEIArlgigrtfqIPRLFPeLTVLENVmvaaqaR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELM 180
Cdd:cd03219 104 TGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELA 183
|
170
....*....|....*....
gi 1119115049 181 DLILEMYRQGQTILAVLHD 199
Cdd:cd03219 184 ELIRELRERGITVLLVEHD 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-199 |
7.98e-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: 105.83 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGVAItppLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWL--AQ 83
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVV---LDGVsldVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD--ITGLseKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQF-----------PLNVQDVVsqgAWPgvslLRGLGGCT----RRRIGAVLERVGLAGLA-KTPIEaLSGGQFQ 147
Cdd:COG1127 77 LYELRRRIgmlfqggalfdSLTVFENV---AFP----LREHTDLSeaeiRELVLEKLELVGLPGAAdKMPSE-LSGGMRK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 148 RMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-217 |
9.84e-28 |
|
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: 105.94 E-value: 9.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSG-RLRWQGK----------RPVIG 79
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAqrHALESQFP--LNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:COG1119 82 LVS--PALQLRFPrdETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHDNQRVADFFPETLLLTPQR 217
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-204 |
3.24e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 104.50 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY----DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVigwlaqRHAL 87
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPV------TRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQFPLNVQdVVSQGawPGVSL-------------LRGLG-GCTRRRIGAVLERVGLAG--LAKTPIEaLSGGQFQRMLF 151
Cdd:COG1124 74 RKAFRRRVQ-MVFQD--PYASLhprhtvdrilaepLRIHGlPDREERIAELLEQVGLPPsfLDRYPHQ-LSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQRVA 204
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVA 203
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-198 |
6.59e-27 |
|
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: 101.69 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvigwlaqrhales 89
Cdd:cd03228 1 IEFKNVSFSYPG-RPKPVLKDVsltIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 qfplNVQDvVSQGAWpgvsllrglggctRRRIGAVLERVGLagLAKTpIEA--LSGGQFQRMLFARVMVQQAPLVMLDEP 167
Cdd:cd03228 65 ----DLRD-LDLESL-------------RKNIAYVPQDPFL--FSGT-IREniLSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 168 FTGIDEATSRELMDLILEMyRQGQTILAVLH 198
Cdd:cd03228 124 TSALDPETEALILEALRAL-AKGKTVIVIAH 153
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-215 |
6.66e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.01 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQRHAL---E 88
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAERGVVfqnE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 SQFP-LNVQDVVSQGAWpgvslLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDE 166
Cdd:PRK11248 80 GLLPwRNVQDNVAFGLQ-----LAGVEKMQRLeIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 167 PFTGIDEATSRELMDLILEMY-RQGQTILAVLHDNQRVADFFPETLLLTP 215
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATELVLLSP 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-196 |
1.93e-26 |
|
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: 101.74 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----RPV-------IGWL 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditgLPPheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALesqFP-LNVQDvvsqgawpgvSLLRGLGGCTRRRIGAVLERV-----GLAGLAKTPIEALSGGQfQRML-FARV 154
Cdd:cd03224 81 PEGRRI---FPeLTVEE----------NLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGE-QQMLaIARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLV 188
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-199 |
5.16e-26 |
|
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: 101.04 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------RPVIG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHALESQfpLNVQDVVsqgAWPgvslLRGLGGCTRRRIGAV----LERVGLAGLA-KTPIEaLSGGQFQRMLFARV 154
Cdd:cd03261 81 MLFQSGALFDS--LTVFENV---AFP----LREHTRLSEEEIREIvlekLEAVGLRGAEdLYPAE-LSGGMKKRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-199 |
8.02e-26 |
|
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: 100.39 E-value: 8.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPViGWLAQ 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphKRPV-NTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALesqFP-LNVQDVVSQGAwpgvsLLRGLGGCT-RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPL 161
Cdd:cd03300 80 NYAL---FPhLTVFENIAFGL-----RLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 162 VMLDEPFTGID----EATSRELMDLILEMyrqGQTILAVLHD 199
Cdd:cd03300 152 LLLDEPLGALDlklrKDMQLELKRLQKEL---GITFVFVTHD 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-205 |
1.17e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.53 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-----RPV----IGWLAQ 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnLPPrerrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALesqFP-LNVQDVVSQGawpgvslLRGLGGCT---RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:COG1118 83 HYAL---FPhMTVAENIAFG-------LRVRPPSKaeiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 160 PLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDnQ----RVAD 205
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHD-QeealELAD 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-227 |
1.43e-25 |
|
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: 103.83 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQLVAGYDG--VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKRPV---IGWL 81
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLelsEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALESQFPLNVQDVVSQGAWPGVSLLRGL--GGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 160 PLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQRVADFFPETLLLTPQRACW-GATRAVL 227
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEdGPPEEIL 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-213 |
2.10e-25 |
|
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: 98.89 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------RPVIGWLAQRHALesqFP-LNVQDVVSQGA 103
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaaRNRIGYLPEERGL---YPkMKVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 wpgvsLLRGLGGC-TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDL 182
Cdd:cd03269 96 -----QLKGLKKEeARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 183 ILEMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:cd03269 171 IRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-206 |
2.64e-25 |
|
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: 98.79 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLP-----PVSGRLRWQGK------------R 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKdiydldvdvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 76 PVIGWLAQRHALesqFPLNVQDVVSQGAWpgvslLRG--LGGCTRRRIGAVLERVGLAGLAKTPIEA--LSGGQFQRMLF 151
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNVAYGLR-----LHGikLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLHDNQ---RVADF 206
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQqaaRVADR 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-199 |
3.91e-25 |
|
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: 102.67 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGY-----------DGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV 77
Cdd:COG1123 257 AEPLLEVRNLSKRYpvrgkggvravDDVSLT------LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 78 IGWLAQRHAL-----------ESQF--PLNVQDVVSQGawpgvslLRGLGGCT----RRRIGAVLERVGL-AGLAKTPIE 139
Cdd:COG1123 331 KLSRRSLRELrrrvqmvfqdpYSSLnpRMTVGDIIAEP-------LRLHGLLSraerRERVAELLERVGLpPDLADRYPH 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 140 ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-229 |
7.17e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGW----LAQRH 85
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-DDVEALsaraASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 86 ALESQ-----FPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAP 160
Cdd:PRK09536 80 ASVPQdtslsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 161 LVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQRA-CWGATRAVLPA 229
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVrAAGPPADVLTA 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-199 |
2.33e-24 |
|
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: 95.33 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------RPVIGW 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqfplnvqdvvsqgaWPGVSllrglggctrrrigaVLERVGLaglaktpieALSGGQFQRMLFARVMVQQAP 160
Cdd:cd03229 81 VFQDFAL----------------FPHLT---------------VLENIAL---------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119115049 161 LVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHD 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-172 |
2.37e-24 |
|
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: 96.11 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGsLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVIGWLAQ 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQFPlnVQDVVSQGAWpgvsllrgLGGCT----RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:cd03264 80 EFGVYPNFT--VREFLDYIAW--------LKGIPskevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170
....*....|...
gi 1119115049 160 PLVMLDEPFTGID 172
Cdd:cd03264 150 SILIVDEPTAGLD 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-199 |
2.54e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------R 75
Cdd:COG2884 1 MIRFENVSKRYPGG--REALSDVsleIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 76 PVIG-------WLAQRHALES-QFPLNVQDVVSQGAwpgvsllrglggctRRRIGAVLERVGLAGLAKTPIEALSGGQFQ 147
Cdd:COG2884 79 RRIGvvfqdfrLLPDRTVYENvALPLRVTGKSRKEI--------------RRRVREVLDLVGLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 148 RMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-199 |
2.98e-24 |
|
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: 95.82 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 36 CPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLR-----WQGKR-----PV----IGWLAQRHALesqFP-LNVQDvvs 100
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRkkinlPPqqrkIGLVFQQYAL---FPhLNVRE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 qgawpgvSLLRGLGGCTRR----RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATS 176
Cdd:cd03297 95 -------NLAFGLKRKRNRedriSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180
....*....|....*....|....
gi 1119115049 177 RELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHD 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
37-199 |
6.24e-24 |
|
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: 94.63 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvigWLAQRHALESQFpLNVQDVVSQGAWPGVS--LLRGLG 114
Cdd:cd03226 25 AGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-----PIKAKERRKSIG-YVMQDVDYQLFTDSVReeLLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 115 GCTRR--RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQT 192
Cdd:cd03226 99 ELDAGneQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA 178
|
....*..
gi 1119115049 193 ILAVLHD 199
Cdd:cd03226 179 VIVITHD 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-190 |
1.46e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.72 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGwlAQRHALESQF-----PLNVQDVVSqgAWP 105
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IR--RQRDEYHQDLlylghQPGIKTELT--ALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 GVSLLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK13538 94 NLRFYQRLHGPGDDeALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
....*.
gi 1119115049 185 EMYRQG 190
Cdd:PRK13538 174 QHAEQG 179
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-199 |
1.63e-23 |
|
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: 98.13 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 5 LVGGDAAMIELEQLVAGYDG--VAITPpLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLA 82
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYPGrrPALRP-VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-VPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 ----QRHALESQFPLNVQDVVSQgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPI----EALSGGQFQ 147
Cdd:TIGR02857 392 dswrDQIAWVPQHPFLFAGTIAE------NIRLARPDASDAEIREALERAGLDEFVAalpqgldTPIgeggAGLSGGQAQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 148 RMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEmYRQGQTILAVLHD 199
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHR 516
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-204 |
1.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPV----IGWLAQRHA 86
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIdysrKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 87 LESQFPLNVQDVVSQGAWPGVSL----LRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLV 162
Cdd:PRK13636 84 VGMVFQDPDNQLFSASVYQDVSFgavnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 163 MLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQRVA 204
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVP 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-199 |
3.09e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.43 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 6 VGGDAAMIELEQLVAGYDGVAitPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------- 74
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGYPGAP--PVLDGVsldLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqd 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 --RPVIGWLAQRHALesqFPLNVQDvvsqgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPI----EAL 141
Cdd:TIGR02868 406 evRRRVSVCAQDAHL---FDTTVRE----------NLRLARPDATDEELWAALERVGLADWLRalpdgldTVLgeggARL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 142 SGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLHD 199
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-199 |
3.97e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.53 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR----PV----IGWLA 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlPPkdrnIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 QRHALesqFP-LNVQDVVsqgAWPgvsL-LRGLGGCTR-RRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:COG3839 82 QSYAL---YPhMTVYENI---AFP---LkLRKVPKAEIdRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 160 PLVMLDEPFTGIDeATSRELM-DLILEMYRQ-GQTILAVLHD 199
Cdd:COG3839 153 KVFLLDEPLSNLD-AKLRVEMrAEIKRLHRRlGTTTIYVTHD 193
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-196 |
3.99e-23 |
|
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: 93.51 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQLVAGYDGVAItppLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLAQR-- 84
Cdd:COG0410 1 MPMLEVENLHAGYGGIHV---LHGVsleVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG-EDITGLPPHRia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 85 -----HALESQ--FP-LNVQDVVSQGAWPGVSllrglggctRRRIGAVLERVG-----LAGLAKTPIEALSGGQfQRML- 150
Cdd:COG0410 77 rlgigYVPEGRriFPsLTVEENLLLGAYARRD---------RAEVRADLERVYelfprLKERRRQRAGTLSGGE-QQMLa 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 151 FARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-199 |
1.14e-22 |
|
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: 92.18 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDG----VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------- 74
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 RPVIGWLAQ--------RHALESQF--PLNVQDVVSQGAwpgvslLRglggctRRRIGAVLERVGLAG--LAKTPIEaLS 142
Cdd:cd03257 81 RKEIQMVFQdpmsslnpRMTIGEQIaePLRIHGKLSKKE------AR------KEAVLLLLVGVGLPEevLNRYPHE-LS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 143 GGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHD 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-198 |
1.15e-22 |
|
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: 91.40 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvigwlaqrhALESQFP 92
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-----------PLDFQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 LNVQDVVSQGAWPGV----SLLRGL----GGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:cd03231 70 SIARGLLYLGHAPGIkttlSVLENLrfwhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 1119115049 165 DEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-199 |
1.49e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLAQRHA-----LESQFP----LNVQDVVS 100
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPLESWSSKAFArkvayLPQQLPaaegMTVRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELM 180
Cdd:PRK10575 108 IGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180
....*....|....*....|
gi 1119115049 181 DLILEMYRQ-GQTILAVLHD 199
Cdd:PRK10575 188 ALVHRLSQErGLTVIAVLHD 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-194 |
1.69e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.86 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY------DGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------RPVIG 79
Cdd:COG4152 1 MLELKGLTKRFgdktavDDVSFT------VPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLaqrhalesqfP--------LNVQDVVsqgawpgVSL--LRGLGGCT-RRRIGAVLERVGLAGLAKTPIEALSGGQFQR 148
Cdd:COG4152 75 YL----------PeerglypkMKVGEQL-------VYLarLKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 149 MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVI 183
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-199 |
2.03e-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: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVIGWLAQ 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvreprevRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQFPlNVQDVVSQGAWPGVSllrglGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVM 163
Cdd:cd03265 81 DLSVDDELT-GWENLYIHARLYGVP-----GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119115049 164 LDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHD 199
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHY 191
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
38-205 |
2.98e-22 |
|
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: 90.69 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPViGWLAQRHALESQfpLNVQDVVSQGAWPGVS 108
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqRPV-SMLFQENNLFAH--LTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 LlrglGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR 188
Cdd:TIGR01277 101 L----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180
....*....|....*....|.
gi 1119115049 189 QGQ-TILAVLH---DNQRVAD 205
Cdd:TIGR01277 177 ERQrTLLMVTHhlsDARAIAS 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-213 |
5.46e-22 |
|
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: 89.77 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------RP 76
Cdd:cd03292 1 IEFINVTKTYPNG--TAALDGInisISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 77 VIGWLAQ-------RHALES-QFPLNVQDVVSQGAwpgvsllrglggctRRRIGAVLERVGLAGLAKTPIEALSGGQFQR 148
Cdd:cd03292 79 KIGVVFQdfrllpdRNVYENvAFALEVTGVPPREI--------------RKRVPAALELVGLSHKHRALPAELSGGEQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 149 MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-199 |
6.90e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 6.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 29 PPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---RPVIGWLAQRHALESQFPLNVQ-----D 97
Cdd:PRK13638 15 PVLKGLnldFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldYSKRGLLALRQQVATVFQDPEQqifytD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 98 VVSQGAWPgvslLRGLGGCTR---RRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:PRK13638 95 IDSDIAFS----LRNLGVPEAeitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180
....*....|....*....|....*
gi 1119115049 175 TSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-199 |
7.95e-22 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 90.66 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLP--------PVSGRLRWQGkRPVIGWLAQ 83
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNG-EPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 R---------HALESQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARV 154
Cdd:PRK13547 80 RlarlravlpQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 155 MVQQAP---------LVMLDEPFTGIDEATSRELMDLILEMYRQGQT-ILAVLHD 199
Cdd:PRK13547 160 LAQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHD 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-226 |
1.13e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPvIGWLAQRHALESQF 91
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR-IGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 PLNVQdvvsqgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:PRK09544 83 PLTVN-----------RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 172 DEATSRELMDLILEMYRQ-GQTILAVLHDNQRVADFFPETLLLTPQRACWGATRAV 226
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVV 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-203 |
1.34e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 92.65 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQRHALESQFP 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-ANIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 LNVQDVVSQGAWPG--VSLLRGlggctrrrigaVLERVGLAG-LAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:PRK15064 399 LTLFDWMSQWRQEGddEQAVRG-----------TLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
170 180 190
....*....|....*....|....*....|....
gi 1119115049 170 GIDeATSRELMDLILEMYrQGqTILAVLHDNQRV 203
Cdd:PRK15064 468 HMD-MESIESLNMALEKY-EG-TLIFVSHDREFV 498
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-199 |
4.27e-21 |
|
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: 87.56 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVIGWLAQRHALesqFP-LNVQDVVS 100
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaaRQSLGYCPQFDAL---FDeLTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QgawpgVSLLRGLGGCTRRRIG-AVLERVGLAGLAKTPIEALSGGQfQRML-FARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:cd03263 98 F-----YARLKGLPKSEIKEEVeLLLRVLGLTDKANKRARTLSGGM-KRKLsLAIALIGGPSVLLLDEPTSGLDPASRRA 171
|
170 180
....*....|....*....|.
gi 1119115049 179 LMDLILEMyRQGQTILAVLHD 199
Cdd:cd03263 172 IWDLILEV-RKGRSIILTTHS 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-199 |
4.63e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.15 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKR----PV----IGW 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltalPAeqrrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqFP-LNVqdvvsqGAWPGVSLLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQ 158
Cdd:COG4136 81 LFQDDLL---FPhLSV------GENLAFALPPTIGRAQRRaRVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 159 APLVMLDEPFTGIDEATSRELMDLILEMYRQGQ--TILaVLHD 199
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGipALL-VTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-199 |
6.21e-21 |
|
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: 91.05 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigwLAQ--RHAL 87
Cdd:COG2274 474 IELENVSFRYPG-DSPPVLDNIsltIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-----LRQidPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQFPLNVQDVVsqgawpgvsLLRG-------LG--GCTRRRIGAVLERVGLAGLAK-------TPI----EALSGGQFQ 147
Cdd:COG2274 548 RRQIGVVLQDVF---------LFSGtirenitLGdpDATDEEIIEAARLAGLHDFIEalpmgydTVVgeggSNLSGGQRQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 148 RMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLHD 199
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHR 669
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-201 |
9.25e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPvIGWLA 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyQRP-INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 83 QRHALesqFPlnvQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLV 162
Cdd:PRK11607 98 QSYAL---FP---HMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 163 MLDEPFTGIDEATsRELMDL----ILEmyRQGQTILAVLHDNQ 201
Cdd:PRK11607 172 LLDEPMGALDKKL-RDRMQLevvdILE--RVGVTCVMVTHDQE 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-198 |
1.42e-20 |
|
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: 84.96 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvAITPPLSG---MICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkrpvigwlaqrhales 89
Cdd:cd03246 1 LEVENVSFRYPG-AEPPVLRNvsfSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 qfplnvQDVVSQGawpgvslLRGLGGCtrrrIGAVLERVGLagLAKTPIEA-LSGGQFQRMLFARVMVQQAPLVMLDEPF 168
Cdd:cd03246 64 ------ADISQWD-------PNELGDH----VGYLPQDDEL--FSGSIAENiLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 169 TGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
35-199 |
2.10e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRwQGKRPVigwlaqrHALESQFPLNVQD--------VVSQgawpg 106
Cdd:PRK11247 35 IPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPL-------AEAREDTRLMFQDarllpwkkVIDN----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 107 VSLlrGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEM 186
Cdd:PRK11247 102 VGL--GLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170
....*....|....
gi 1119115049 187 YRQ-GQTILAVLHD 199
Cdd:PRK11247 180 WQQhGFTVLLVTHD 193
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
35-205 |
6.99e-20 |
|
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: 84.70 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----RPV----IGWLAQRHALesqFP-LNVQDVVSQGAWP 105
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdVPVqernVGFVFQHYAL---FRhMTVFDNVAFGLRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 GVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILE 185
Cdd:cd03296 102 KPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR 181
|
170 180
....*....|....*....|....
gi 1119115049 186 MY-RQGQTILAVLHDNQR---VAD 205
Cdd:cd03296 182 LHdELHVTTVFVTHDQEEaleVAD 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-205 |
3.07e-19 |
|
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: 83.12 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIG 79
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLnleIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHALesqFP-LNVQDVVsqGAWPgvSLLRGLGGCTRRRIGAVLERVGL--AGLAKTPIEALSGGQFQRMLFARVMV 156
Cdd:cd03295 79 YVIQQIGL---FPhMTVEENI--ALVP--KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 157 QQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQ---RVAD 205
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDeafRLAD 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
42-199 |
4.01e-19 |
|
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: 82.77 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK--------RPVIGWLAQRHALesqFP-LNVQDVVSQgawpGVSLLRG 112
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppeKRDISYVPQNYAL---FPhMTVYKNIAY----GLKKRKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQ 191
Cdd:cd03299 102 DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGV 181
|
....*...
gi 1119115049 192 TILAVLHD 199
Cdd:cd03299 182 TVLHVTHD 189
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-199 |
4.11e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPvSGRLRWQGkRPVIGW----LAQRHALESQ-----FPLNVQDVVS 100
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNG-RPLSDWsaaeLARHRAYLSQqqsppFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSLlrglgGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ-------QAPLVMLDEPFTGIDE 173
Cdd:COG4138 92 LHQPAGASS-----EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 1119115049 174 ATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-198 |
4.33e-19 |
|
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: 81.21 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPvigwLAQRHALESQFplnvqDVVSQGAWP-GVSL 109
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV----SDLEKALSSLI-----SVLNQRPYLfDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRGLGgctRRrigavlervglaglaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRq 189
Cdd:cd03247 92 RNNLG---RR---------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK- 146
|
....*....
gi 1119115049 190 GQTILAVLH 198
Cdd:cd03247 147 DKTLIWITH 155
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-199 |
1.46e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWLAQRHA-- 86
Cdd:PRK10908 1 MIRFEHVSKAYLGG--RQALQGVtfhMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD--ITRLKNREVpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 87 LESQFPLNVQD---VVSQGAWPGVSLLRGLGGCT----RRRIGAVLERVGLAGLAKT-PIEaLSGGQFQRMLFARVMVQQ 158
Cdd:PRK10908 77 LRRQIGMIFQDhhlLMDRTVYDNVAIPLIIAGASgddiRRRVSAALDKVGLLDKAKNfPIQ-LSGGEQQRVGIARAVVNK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119115049 159 APLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-204 |
1.69e-18 |
|
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: 82.54 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 43 IVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPvIGWLAQRHALesqFP-LNVQDVVSQGAwpgvsLLRG 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphLRH-INMVFQSYAL---FPhMTVEENVAFGL-----KMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATsRELMDLILEM--YRQ 189
Cdd:TIGR01187 72 VPRAEIKpRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKL-RDQMQLELKTiqEQL 150
|
170
....*....|....*
gi 1119115049 190 GQTILAVLHDnQRVA 204
Cdd:TIGR01187 151 GITFVFVTHD-QEEA 164
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
35-199 |
3.25e-18 |
|
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: 80.77 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK--------------RPVIGWLAQRHALesqFP-LNVQDVV 99
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrRKKISMVFQSFAL---LPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 100 SQGawpgvsL-LRGLGGCTRRRIGA-VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:cd03294 124 AFG------LeVQGVPRAEREERAAeALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180
....*....|....*....|...
gi 1119115049 178 ELMDLILEMYR-QGQTILAVLHD 199
Cdd:cd03294 198 EMQDELLRLQAeLQKTIVFITHD 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-198 |
3.30e-18 |
|
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: 82.99 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG----------KRPVIG 79
Cdd:TIGR03375 464 IEFRNVSFAYPG-QETPALDNVsltIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirqidpadLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHALesqFPLNVQDVVSQGAwPGVSllrglggctRRRIGAVLERVGLAGLAKT-------PI----EALSGGQFQR 148
Cdd:TIGR03375 543 YVPQDPRL---FYGTLRDNIALGA-PYAD---------DEEILRAAELAGVTEFVRRhpdgldmQIgergRSLSGGQRQA 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 149 MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDlILEMYRQGQTILAVLH 198
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKD-RLKRWLAGKTLVLVTH 658
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
38-213 |
3.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLR-------WQGKRPVIGWLAQRHALESQFP---LNVQDVVSQGAWPGV 107
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsSTSKQKEIKPVRKKVGVVFQFPesqLFEETVLKDVAFGPQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLlrGLGGCTRRRIGA-VLERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK13643 112 NF--GIPKEKAEKIAAeKLEMVGLADefWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFE 188
|
170 180
....*....|....*....|....*....
gi 1119115049 185 EMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13643 189 SIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
37-205 |
4.24e-18 |
|
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: 79.57 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV--------IGWLAQRHALesqFP-LNVQDVVSQGAwpgv 107
Cdd:cd03268 25 KGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniealrrIGALIEAPGF---YPnLTARENLRLLA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 sLLRGLGgctRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY 187
Cdd:cd03268 98 -RLLGIR---KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR 173
|
170 180
....*....|....*....|.
gi 1119115049 188 RQGQTILA---VLHDNQRVAD 205
Cdd:cd03268 174 DQGITVLIsshLLSEIQKVAD 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-205 |
7.53e-18 |
|
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: 77.47 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWLAQRHALesqfp 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--VSFASPRDAR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 lnvqdvvsqgawpgvsllrglggctRRRIGAVLErvglaglaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:cd03216 74 -------------------------RAGIAMVYQ--------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119115049 173 EATSRELMDLILEMYRQGQTILAV---LHDNQRVAD 205
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFIshrLDEVFEIAD 150
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-172 |
1.23e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVvsqG 102
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADL---S 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 103 AWPGVSLLRGLGGCTRRRI-GAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
37-167 |
1.27e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQ-GKRpvIGWLAQRHALESQFPlnVQDVVSQGAWPGVSLLRGL-- 113
Cdd:COG0488 23 PGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLR--IGYLPQEPPLDDDLT--VLDTVLDGDAELRALEAELee 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 114 -------------------------GGCT-RRRIGAVLERVGLAG-LAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDE 166
Cdd:COG0488 99 leaklaepdedlerlaelqeefealGGWEaEARAEEILSGLGFPEeDLDRPVSELSGGWRRRVALARALLSEPDLLLLDE 178
|
.
gi 1119115049 167 P 167
Cdd:COG0488 179 P 179
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-217 |
1.36e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---RPVIGWLAQRHALE 88
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 SQFPLNvqDVVSQGAWPGVS---LLRGLGGC-TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:PRK13647 85 FQDPDD--QVFSSTVWDDVAfgpVNMGLDKDeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 165 DEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVADFFPETLLLTPQR 217
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-199 |
2.02e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPvSGRLRWQGKrPVIGW----LAQRHALESQ--FPLNVQDVvsqga 103
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQ-PLEAWsaaeLARHRAYLSQqqTPPFAMPV----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WPGVSLLRGLG---GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAP-------LVMLDEPFTGIDE 173
Cdd:PRK03695 87 FQYLTLHQPDKtrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 1119115049 174 ATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-205 |
2.67e-17 |
|
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: 75.56 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWqGKRPVIGWLAQrhalesqfp 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 lnvqdvvsqgawpgvsllrglggctrrrigavlervglaglaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119115049 173 EaTSRELMDLILEMYRqgQTILAVLHDNQ---RVAD 205
Cdd:cd03221 103 L-ESIEALEEALKEYP--GTVILVSHDRYfldQVAT 135
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-203 |
4.82e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALESQfpL 93
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPE--K 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 94 NVQDVVSQGAwPGVSLlrglGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDE 173
Cdd:PRK11147 399 TVMDNLAEGK-QEVMV----NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 174 ATsRELMDLILEMYrQGqTILAVLHDNQRV 203
Cdd:PRK11147 474 ET-LELLEELLDSY-QG-TVLLVSHDRQFV 500
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-206 |
5.46e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRW------QGKRPV-IGWLAQRHALESQFPLN------VQDV 98
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKkLKPLRKKVGIVFQFPEHqlfeetVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 99 VSQGawP---GVSLLRGLggctrRRIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDE 173
Cdd:PRK13634 107 ICFG--PmnfGVSEEDAK-----QKAREMIELVGLpeELLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190
....*....|....*....|....*....|....
gi 1119115049 174 ATSRELMDLILEMYR-QGQTILAVLHDNQRVADF 206
Cdd:PRK13634 179 KGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARY 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-213 |
9.11e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR--PVIG-----WLAQRHALESQFPLN--VQDVVSQGAWPGVs 108
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitPETGnknlkKLRKKVSLVFQFPEAqlFENTVLKDVEFGP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 llRGLGGCTRR-RIGAV--LERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLI 183
Cdd:PRK13641 112 --KNFGFSEDEaKEKALkwLKKVGLSEdlISKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 184 LEMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13641 189 KDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-206 |
1.13e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRW-------QGKRPVIGWLAQRHALESQFPLN-------VQDVVS 100
Cdd:PRK13649 30 IEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitsTSKNKDIKQIRKKVGLVFQFPESqlfeetvLKDVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSllrglggcTRRRIGAVLERVGLAGLA-----KTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEAT 175
Cdd:PRK13649 110 GPQNFGVS--------QEEAEALAREKLALVGISeslfeKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 176 SRELMDLILEMYRQGQTILAVLHDNQRVADF 206
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANY 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-229 |
1.37e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQL-VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRwqgkRPVIG---WLAQR 84
Cdd:COG4178 359 EDGALALEDLtLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA----RPAGArvlFLPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 85 haleSQFPL-NVQDVVsqgAWPGVSllrglGGCTRRRIGAVLERVGLAGLA-KTPIEA-----LSGGQFQRMLFARVMVQ 157
Cdd:COG4178 435 ----PYLPLgTLREAL---LYPATA-----EAFSDAELREALEAVGLGHLAeRLDEEAdwdqvLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGqTILAVLHDnQRVADFFPETLLLTPQRAcWGATRAVLPA 229
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHR-STLAAFHDRVLELTGDGS-WQLLPAEAPA 571
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-199 |
1.38e-16 |
|
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: 75.37 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV--------IGWLAQR 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlppkdrdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 85 HALesqFP-LNVQDVVSQGAwpgvsLLRGLGGCT-RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLV 162
Cdd:cd03301 81 YAL---YPhMTVYDNIAFGL-----KLRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1119115049 163 MLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHD 190
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-201 |
2.24e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 75.16 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQL---VAGYDG-VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWLA--Q 83
Cdd:COG4181 6 APIIELRGLtktVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALDedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQ--------FPLnvqdVVSQGAWPGVSL---LRGLGGCtRRRIGAVLERVGLAGLAK-TPIEaLSGGQFQRMLF 151
Cdd:COG4181 84 RARLRARhvgfvfqsFQL----LPTLTALENVMLpleLAGRRDA-RARARALLERVGLGHRLDhYPAQ-LSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR-QGQTILAVLHDNQ 201
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-205 |
2.35e-16 |
|
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: 75.10 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPP----LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRwqgkrpVIGWLAQRHAL 87
Cdd:cd03266 1 MITADALTKRFRDVKKTVQavdgVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT------VDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQFPLNVqdvVSQG--------AWPGVSLLRGLGGCTRR----RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVM 155
Cdd:cd03266 75 EARRRLGF---VSDStglydrltARENLEYFAGLYGLKGDeltaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTIL---AVLHDNQRVAD 205
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILfstHIMQEVERLCD 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-198 |
3.46e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGWLAQrh 85
Cdd:PRK11160 335 DQVSLTLNNVSFTYPD-QPQPVLKGLslqIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-QPIADYSEA-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 86 ALESQFplnvqDVVSQGawpgV---------SLLRGLGGCTRRRIGAVLERVGLAGLAKT--PIEA--------LSGGQF 146
Cdd:PRK11160 411 ALRQAI-----SVVSQR----VhlfsatlrdNLLLAAPNASDEALIEVLQQVGLEKLLEDdkGLNAwlgeggrqLSGGEQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 147 QRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEmYRQGQTILAVLH 198
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITH 532
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-199 |
3.53e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY-DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------RPVI 78
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALESQFPLNVQDVvsqgAWPGVSLlrGLG-GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDV----AFGPLNL--GLSkEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-206 |
4.99e-16 |
|
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: 75.18 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHAL-----------ESQ-FPLNVQDVVSQGawP 105
Cdd:TIGR04521 31 GEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkvglvfqfpEHQlFEETVYKDIAFG--P 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 ---GVSLLRglggcTRRRIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELM 180
Cdd:TIGR04521 109 knlGLSEEE-----AEERVKEALELVGLdeEYLERSPFE-LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEIL 182
|
170 180
....*....|....*....|....*..
gi 1119115049 181 DLILEMYRQ-GQTILAVLHDNQRVADF 206
Cdd:TIGR04521 183 DLFKRLHKEkGLTVILVTHSMEDVAEY 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-198 |
5.70e-16 |
|
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: 74.15 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY-DGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------- 74
Cdd:cd03258 1 MIELKNVSKVFgDTGGKVTALKDVslsVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 RPVIGWLAQRHALESQ--------FPLNVqdvvsqGAWPGVSLlrglggctRRRIGAVLERVGLAGLAKTPIEALSGGQF 146
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrtvfenvaLPLEI------AGVPKAEI--------EERVLELLELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 147 QRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLH 198
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITH 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-199 |
8.47e-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: 73.65 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK--------RPVIgwlAQRHALesqFP-LNVQDVVsqgAWP 105
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdRMVV---FQNYSL---LPwLTVRENI---ALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 GVSLLRGLGGCTRRRI-GAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIvEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170
....*....|....*.
gi 1119115049 185 EMYRQ-GQTILAVLHD 199
Cdd:TIGR01184 159 QIWEEhRVTVLMVTHD 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-194 |
1.03e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.46 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALesqfplnvqdvvsqgawpGVSLLRGlg 114
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA------------------GIAYVPE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 115 gcTRRRIGAVLER-----VGLAGLaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ 189
Cdd:cd03215 83 --DRKREGLVLDLsvaenIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA 153
|
....*
gi 1119115049 190 GQTIL 194
Cdd:cd03215 154 GKAVL 158
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-198 |
1.22e-15 |
|
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: 72.58 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP--VSGRLRWQGK-------RPVIGWLAQRHALESQfpLNVQDVVSQ 101
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfRKIIGYVPQDDILHPT--LTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 102 GAwpgvsLLRGlggctrrrigavlervglaglaktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:cd03213 106 AA-----KLRG----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170
....*....|....*..
gi 1119115049 182 LILEMYRQGQTILAVLH 198
Cdd:cd03213 153 LLRRLADTGRTIICSIH 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-199 |
1.24e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 22 YDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR-----PV---IGWLAQRHALesqFP- 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvpPAergVGMVFQSYAL---YPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 LNVQDVVSQGawpgVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK11000 90 LSVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180
....*....|....*....|....*...
gi 1119115049 173 EATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK11000 166 AALRVQMRIEISRLHKRlGRTMIYVTHD 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
43-218 |
1.76e-15 |
|
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: 72.96 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 43 IVGL---NGCGKSTLLKTLAGFLPPVSGRLRWQG----KRPV-------IGWLAQRHALESQfpLNVQDVVSqgawpGVS 108
Cdd:cd03218 28 IVGLlgpNGAGKTTTFYMIVGLVKPDSGKILLDGqditKLPMhkrarlgIGYLPQEASIFRK--LTVEENIL-----AVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 LLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY 187
Cdd:cd03218 101 EIRGLSKKEREeKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 188 RQGQTILAVLHdNQRvadffpETLLLTpQRA 218
Cdd:cd03218 181 DRGIGVLITDH-NVR------ETLSIT-DRA 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-198 |
1.85e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP-------VSGRLR------WQGKR 75
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndltLFGRRRgsgetiWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 76 PvIGWLAQRHALESQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIGAVLERVGLAG-LAKTPIEALSGGQfQRM-LFAR 153
Cdd:PRK10938 337 H-IGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQ-QRLaLIVR 414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119115049 154 VMVQQAPLVMLDEPFTGIDeATSRELMDLILE-MYRQGQT-ILAVLH 198
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLD-PLNRQLVRRFVDvLISEGETqLLFVSH 460
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-198 |
2.50e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigwLAQRHALESQ-------------FP-LNVQDVVSQG 102
Cdd:COG1129 29 PGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFRSPRDAQaagiaiihqelnlVPnLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 103 AWPgvsllRGLG----GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:COG1129 104 REP-----RRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180
....*....|....*....|
gi 1119115049 179 LMDLILEMYRQGQTILAVLH 198
Cdd:COG1129 179 LFRIIRRLKAQGVAIIYISH 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
38-199 |
3.39e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-------------RPVIGWLAQRHALESQfpLNVQDVVsqgAW 104
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvRKRMSMLFQSGALFTD--MNVFDNV---AY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 PGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK11831 108 PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170
....*....|....*.
gi 1119115049 185 EM-YRQGQTILAVLHD 199
Cdd:PRK11831 188 ELnSALGVTCVVVSHD 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
35-198 |
3.44e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLP----PVS------------GRLR--WQGKRPVIGWLAQRHALESQfpLNVQ 96
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellgrtvqreGRLArdIRKSRANTGYIFQQFNLVNR--LSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 97 DVVSQGAWPGVSL----LRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK09984 105 ENVLIGALGSTPFwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180
....*....|....*....|....*..
gi 1119115049 173 EATSRELMDLILEMYRQ-GQTILAVLH 198
Cdd:PRK09984 185 PESARIVMDTLRDINQNdGITVVVTLH 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-201 |
5.61e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG--------------KRPVIGWLAQRHALESQFplnvq 96
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelRNQKLGFIYQFHHLLPDF----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 97 dvvsqGAWPGVSLLRGLGGCTR----RRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK11629 103 -----TALENVAMPLLIGKKKPaeinSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 173 EATSRELMDLILEM-YRQGQTILAVLHDNQ 201
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
37-199 |
6.36e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQ---RHALESQFplnvQDV-------------VS 100
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-HIEGLPGHqiaRMGVVRTF----QHVrlfremtvienllVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSLLRGL--GGCTRR-------RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:PRK11300 105 QHQQLKTGLFSGLlkTPAFRRaesealdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180
....*....|....*....|....*....
gi 1119115049 172 DEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK11300 185 NPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-198 |
7.24e-15 |
|
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: 71.08 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAItPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIG 79
Cdd:cd03245 3 IEFRNVSFSYPNQEI-PALDNVsltIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHALesqFPLNVQDvvsqgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPI----EALSGGQFQR 148
Cdd:cd03245 82 YVPQDVTL---FYGTLRD----------NITLGAPLADDERILRAAELAGVTDFVNkhpngldLQIgergRGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 149 MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLiLEMYRQGQTILAVLH 198
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITH 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-204 |
8.35e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIG 79
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVsfsVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 80 WLAQRHalESQF-PLNVQDVVSQGawpgvslLRGlGGCTR----RRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARV 154
Cdd:PRK13635 85 MVFQNP--DNQFvGATVQDDVAFG-------LEN-IGVPReemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHDNQRVA 204
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAA 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
38-199 |
8.92e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG----KRPV----IGWLAQRHALesqFP-LNVQDVVSQGawpgvs 108
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvtHRSIqqrdICMVFQSYAL---FPhMSLGENVGYG------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 lLRGLG---GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILE 185
Cdd:PRK11432 103 -LKMLGvpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
170
....*....|....*
gi 1119115049 186 MYRQ-GQTILAVLHD 199
Cdd:PRK11432 182 LQQQfNITSLYVTHD 196
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
37-205 |
1.25e-14 |
|
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: 70.54 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGR--LRWQGkrpviGW--LAQ---RHALE---------SQFpLNV----- 95
Cdd:COG4778 36 AGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDG-----GWvdLAQaspREILAlrrrtigyvSQF-LRViprvs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 96 -QDVVSQGAwpgvsLLRGLG-GCTRRRIGAVLERVGLAglaktpiEAL--------SGGQFQRMLFARVMVQQAPLVMLD 165
Cdd:COG4778 110 aLDVVAEPL-----LERGVDrEEARARARELLARLNLP-------ERLwdlppatfSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 166 EPFTGIDEATSRELMDLILEMYRQGQTILAVLHDN---QRVAD 205
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEevrEAVAD 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-205 |
2.62e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPViGWLAQ 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKV-GFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQfpLNVQDVVSQGawpgVSLL----RGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:PRK10851 82 HYALFRH--MTVFDNIAFG----LTVLprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 160 PLVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHDNQ---RVAD 205
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEeamEVAD 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-204 |
2.84e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.29 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQL----VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG------------ 73
Cdd:PRK10535 2 TALLELKDIrrsyPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 74 --KRPVIGWLAQRHALESQFPLnVQDVVSQGAWPGVSLLRglggcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLF 151
Cdd:PRK10535 82 qlRREHFGFIFQRYHLLSHLTA-AQNVEVPAVYAGLERKQ-----RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVA 204
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAA 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-199 |
3.50e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.75 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---------KRPViGWLAQ 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaeNRHV-NTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALesqFP-LNVQDVVSQGawpgvslLRgLGGC----TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQ 158
Cdd:PRK09452 94 SYAL---FPhMTVFENVAFG-------LR-MQKTpaaeITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 159 APLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
35-198 |
3.96e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 68.65 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvIGWlaqrhalesqfplnvqdvVSQGAWpgvsLLRG-- 112
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---IAY------------------VSQEPW----IQNGti 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 ----LGGCT--RRRIGAVLERVGL--------AGLaKTPI-E---ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:cd03250 83 reniLFGKPfdEERYEKVIKACALepdleilpDGD-LTEIgEkgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180
....*....|....*....|....*
gi 1119115049 175 TSRELMD-LILEMYRQGQTILAVLH 198
Cdd:cd03250 162 VGRHIFEnCILGLLLNNKTRILVTH 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-224 |
4.23e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGW 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqFPLNVQDVVsqgAWPgvSLLRGLGGcTRRRIGAVLERVGLA-GLAKTPIEALSGGQFQRMLFARvMVQQA 159
Cdd:PRK10247 86 CAQTPTL---FGDTVYDNL---IFP--WQIRNQQP-DPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIR-NLQFM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119115049 160 PLV-MLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHDNQRV--ADffpETLLLTPQRACWGATR 224
Cdd:PRK10247 156 PKVlLLDEITSALDESNKHNVNEIIHRYVREQNiAVLWVTHDKDEInhAD---KVITLQPHAGEMQEAR 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-198 |
4.88e-14 |
|
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: 71.20 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 40 LTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVIGWLAQRHALESQFPLnVQDVVSQGAWPGVSLL 110
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavRQSLGMCPQHNILFHHLTV-AEHILFYAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 RGlggctRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEmYRQG 190
Cdd:TIGR01257 1037 EA-----QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK-YRSG 1110
|
....*...
gi 1119115049 191 QTILAVLH 198
Cdd:TIGR01257 1111 RTIIMSTH 1118
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-204 |
5.26e-14 |
|
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: 68.90 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPvigWlAQRHALESQFPLnVQDVVSQGAW-----PGVSLLRG 112
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVP---W-KRRKKFLRRIGV-VFGQKTQLWWdlpviDSFYLLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGGCTRRRIGAVLERVG----LAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR 188
Cdd:cd03267 122 IYDLPPARFKKRLDELSelldLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNR 201
|
170
....*....|....*..
gi 1119115049 189 Q-GQTILAVLHDNQRVA 204
Cdd:cd03267 202 ErGTTVLLTSHYMKDIE 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-206 |
5.84e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLaGFLPPVSGRLRWQGKRPVIGW------------ 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQniyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 ---LAQRHALESQFPLNVQDVVSQGawpgvslLRGLGGCTRRRIGAVLERVGLAG---------LAKTPIEaLSGGQFQR 148
Cdd:PRK14258 87 rrqVSMVHPKPNLFPMSVYDNVAYG-------VKIVGWRPKLEIDDIVESALKDAdlwdeikhkIHKSALD-LSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 149 MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY-RQGQTILAV---LHDNQRVADF 206
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVshnLHQVSRLSDF 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
42-213 |
6.40e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvIGWLaqrhaLESQFPLN-----VQDVVSQGAwpgvsLLrglgGC 116
Cdd:COG1134 56 GIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSAL-----LELGAGFHpeltgRENIYLNGR-----LL----GL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 117 TRRRIGAVLER-VGLAGLAK---TPIEALSGGQFQRMLFArVMVQQAPLVMLdepftgIDEATS-------RELMDLILE 185
Cdd:COG1134 119 SRKEIDEKFDEiVEFAELGDfidQPVKTYSSGMRARLAFA-VATAVDPDILL------VDEVLAvgdaafqKKCLARIRE 191
|
170 180
....*....|....*....|....*...
gi 1119115049 186 MYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:COG1134 192 LRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-198 |
9.85e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQL-VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLpPVSGRLRWQGK----------RPVIGWL 81
Cdd:PRK11174 350 IEAEDLeILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpeswRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALesqFPLNVQDvvsqgawpgvSLLRGLGGCTRRRIGAVLERVGLA--------GLAkTPIE----ALSGGQFQRM 149
Cdd:PRK11174 429 GQNPQL---PHGTLRD----------NVLLGNPDASDEQLQQALENAWVSeflpllpqGLD-TPIGdqaaGLSVGQAQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119115049 150 LFARVMVQQAPLVMLDEPFTGIDeATSRELMDLILEMYRQGQTILAVLH 198
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLD-AHSEQLVMQALNAASRRQTTLMVTH 542
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
37-205 |
1.03e-13 |
|
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: 67.55 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------RPVIGWLAQRHALesqFP-LNVQDVVSQGa 103
Cdd:cd03262 25 KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkninelRQKVGMVFQQFNL---FPhLTVLENITLA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 wpgVSLLRGLGGCTRRRIG-AVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDL 182
Cdd:cd03262 101 ---PIKVKGMSKAEAEERAlELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDV 177
|
170 180
....*....|....*....|....*.
gi 1119115049 183 ILEMYRQGQTILAVLHD---NQRVAD 205
Cdd:cd03262 178 MKDLAEEGMTMVVVTHEmgfAREVAD 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-199 |
1.08e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 69.89 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 39 SLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvigwlaQRHALESQFPLNVQDVVSQgawPGVSLLRGLGGCTR 118
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--------VRMAVFSQHHVDGLDLSSN---PLLYMMRCFPGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 119 RRIGAVLERVGLAG-LAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID-EATSRELMDLILemyRQGqTILAV 196
Cdd:PLN03073 605 QKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLVL---FQG-GVLMV 680
|
...
gi 1119115049 197 LHD 199
Cdd:PLN03073 681 SHD 683
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-217 |
1.22e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP--VSGRLRWQGKRPV------IGWLAQRHALesqFP-LNVQDVVSq 101
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPTkqilkrTGFVTQDDIL---YPhLTVRETLV- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 102 gawpGVSLLRGLGGCTRRRIGAVLERV-GLAGLAK--------TPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PLN03211 163 ----FCSLLRLPKSLTKQEKILVAESViSELGLTKcentiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119115049 173 EATSRELMDLILEMYRQGQTILAVLHD-NQRVADFFPETLLLTPQR 217
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-198 |
2.30e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 8 GDAAMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------RPVI 78
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarhaRQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALESQFPLnVQDVVSQGAWPGVSllrglGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQ 158
Cdd:PRK13537 83 GVVPQFDNLDPDFTV-RENLLVFGRYFGLS-----AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119115049 159 APLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-198 |
3.60e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVVSQGAWPGVS 108
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 LLRgLGGCT-----RRRIGAVLERVGLAGLAKTPI------EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:TIGR00955 125 HLR-MPRRVtkkekRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180
....*....|....*....|.
gi 1119115049 178 ELMDLILEMYRQGQTILAVLH 198
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-206 |
4.67e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 34 MICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV-IGWLAQRHALESQFPLNVQDVVSQGAwpgvsllRG 112
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrLSFEQLQKLVSDEWQRNNTDMLSPGE-------DD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGGCTRR----------RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDL 182
Cdd:PRK10938 98 TGRTTAEiiqdevkdpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170 180
....*....|....*....|....
gi 1119115049 183 ILEMYRQGQTILAVLHDNQRVADF 206
Cdd:PRK10938 178 LASLHQSGITLVLVLNRFDEIPDF 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-198 |
5.54e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRL---------RWQGKRPVIGWLAQ 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvpaRARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 RHALESQFPLNvQDVVSQGAWPGVSllrglggctRRRIGAV----LERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQA 159
Cdd:PRK13536 122 FDNLDLEFTVR-ENLLVFGRYFGMS---------TREIEAVipslLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119115049 160 PLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-198 |
5.79e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.50 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigwLAQ--RHALESQFplnvqDVVSQGAWpgvsLLRG-- 112
Cdd:COG1132 365 PGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-----IRDltLESLRRQI-----GVVPQDTF----LFSGti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 -----LG--GCTRRRIGAVLERVGLAGLAK-------TPIE----ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:COG1132 431 renirYGrpDATDEEVEEAAKAAQAHEFIEalpdgydTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180
....*....|....*....|....
gi 1119115049 175 TSRELMDLILEMyRQGQTILAVLH 198
Cdd:COG1132 511 TEALIQEALERL-MKGRTTIVIAH 533
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
40-206 |
6.09e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 40 LTAIVGLNGCGKSTLLKT---LAGFLPP--VSGRLRWQGK------------RPVIGWLAQRhalESQFPLNVQDVVSQG 102
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKnlyapdvdpvevRRRIGMVFQK---PNPFPKSIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 103 AwpgvsLLRGLGGCTRRRIGAVLERVGLAGLAKTPIE----ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:PRK14243 115 A-----RINGYKGDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLR 189
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 179 LMDLILEMYRQgQTILAVLHDNQ---RVADF 206
Cdd:PRK14243 190 IEELMHELKEQ-YTIIIVTHNMQqaaRVSDM 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-198 |
6.47e-13 |
|
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: 65.71 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYD-GVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWL 81
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALesqFPLNVQDVVSQGAwPGVSLLRGLGGCTRRRIGAVLER--------VGLAGLAktpieaLSGGQFQRMLFAR 153
Cdd:cd03253 81 PQDTVL---FNDTIGYNIRYGR-PDATDEEVIEAAKAAQIHDKIMRfpdgydtiVGERGLK------LSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 154 VMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLH 198
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-204 |
9.33e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPP----VSGRLRWQGKRPVIGWLAQRH-ALESQFPLNVQDVVSQGAWPGVSLLRG 112
Cdd:PRK10418 29 GRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKiATIMQNPRSAFNPLHTMHTHARETCLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGG-CTRRRIGAVLERVGLAGLAKT----PIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILE-M 186
Cdd:PRK10418 109 LGKpADDATLTAALEAVGLENAARVlklyPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESiV 187
|
170
....*....|....*...
gi 1119115049 187 YRQGQTILAVLHDNQRVA 204
Cdd:PRK10418 188 QKRALGMLLVTHDMGVVA 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
37-199 |
1.05e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLA------QRHALESQFPLNVQD-------VVSQGA 103
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaeRRRLLRTEWGFVHQHprdglrmQVSAGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WPGVSLLrGLG----GCTRRRIGAVLERV--GLAGLAKTPiEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:PRK11701 111 NIGERLM-AVGarhyGDIRATAGDWLERVeiDAARIDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA 188
|
170 180
....*....|....*....|...
gi 1119115049 178 ELMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK11701 189 RLLDLLRGLVRElGLAVVIVTHD 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-201 |
1.05e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.04 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 17 QLVAGY----DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRH------- 85
Cdd:cd03290 2 QVTNGYfswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 86 ALESQFPLNVQDVVSQGAWPGVSLlrglggcTRRRIGAVLERVGL------------AGLAKTPIEaLSGGQFQRMLFAR 153
Cdd:cd03290 82 AYAAQKPWLLNATVEENITFGSPF-------NKQRYKAVTDACSLqpdidllpfgdqTEIGERGIN-LSGGQRQRICVAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 154 VMVQQAPLVMLDEPFTGIDEATSRELMDL-ILEMYRQGQ-TILAVLHDNQ 201
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKrTLVLVTHKLQ 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
42-206 |
1.48e-12 |
|
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: 64.48 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpVIGWLAQRHALESQfpLNVQDVVsqgawpgvsLLRG-LGGCTRRR 120
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLLGLGGGFNPE--LTGRENI---------YLNGrLLGLSRKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 121 IGAVLERV-GLAGLAK---TPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:cd03220 119 IDEKIDEIiEFSELGDfidLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV 198
|
170
....*....|
gi 1119115049 197 LHDNQRVADF 206
Cdd:cd03220 199 SHDPSSIKRL 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-198 |
1.53e-12 |
|
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: 64.55 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGvaITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGwlAQRHALES 89
Cdd:cd03254 3 IEFENVNFSYDE--KKPVLKDInfsIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG-IDIRD--ISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 QFPLNVQDVVsqgawpgvsLLRG-------LGG--CTRRRIGAVLERVGLA--------GLAKTPIEA---LSGGQFQRM 149
Cdd:cd03254 78 MIGVVLQDTF---------LFSGtimenirLGRpnATDEEVIEAAKEAGAHdfimklpnGYDTVLGENggnLSQGERQLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119115049 150 LFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLH 198
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-205 |
1.55e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGY-DGvaiTPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRL-----------RWQGKRP 76
Cdd:PRK13644 1 MIRLENVSYSYpDG---TPALENInlvIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 77 VIGWLAQRHalESQF-PLNVQDVVSQG----AWPGVSLlrglggctRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLF 151
Cdd:PRK13644 78 LVGIVFQNP--ETQFvGRTVEEDLAFGpenlCLPPIEI--------RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVAD 205
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
38-213 |
1.62e-12 |
|
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: 65.21 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVVSQG----------AWPGV 107
Cdd:TIGR02769 37 GETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVnprmtvrqiiGEPLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLLRGLGGCTRRRIGAVLERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILE 185
Cdd:TIGR02769 117 HLTSLDESEQKARIAELLDMVGLRSedADKLPRQ-LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRK 195
|
170 180
....*....|....*....|....*....
gi 1119115049 186 MYRQGQT-ILAVLHDNQRVADFFPETLLL 213
Cdd:TIGR02769 196 LQQAFGTaYLFITHDLRLVQSFCQRVAVM 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-227 |
2.37e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------------RPVIGWLAQRha 86
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqidaiklRKEVGMVFQQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 87 lESQFP-LNVQDVVsqgAWPgvslLRGLGGCTRRRIGAVLE----RVGL----AGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:PRK14246 99 -PNPFPhLSIYDNI---AYP----LKSHGIKEKREIKKIVEeclrKVGLwkevYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQgQTILAVLHDNQ---RVADFFpeTLLLTPQRACWGATRAVL 227
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQqvaRVADYV--AFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
43-213 |
2.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 43 IVGLNGCGKSTLLKTLAGFLPPVSGRLR---------WQGKRPVIGW----------LAQRHALESQFPLN--VQDVVSQ 101
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkKNNHELITNPyskkiknfkeLRRRVSMVFQFPEYqlFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 102 GAWPGVSLLRGLGGCTRRRIGAVLERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSREL 179
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsyLERSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190
....*....|....*....|....*....|....
gi 1119115049 180 MDLILEMYRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
37-207 |
2.89e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTL--AGFLPP---VSGRLRWQGK------------RPVIGWLAQRhalESQFPLNVQDVV 99
Cdd:PRK14239 30 PNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHniysprtdtvdlRKEIGMVFQQ---PNPFPMSIYENV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 100 SQGawpgvslLRGLGGCTRRRIGAVLERvGLAG----------LAKTPIeALSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:PRK14239 107 VYG-------LRLKGIKDKQVLDEAVEK-SLKGasiwdevkdrLHDSAL-GLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 170 GIDEATSRELMDLILEMyRQGQTILAVLHDNQ---RVAD---FF 207
Cdd:PRK14239 178 ALDPISAGKIEETLLGL-KDDYTMLLVTRSMQqasRISDrtgFF 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-205 |
4.29e-12 |
|
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: 64.82 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 18 LVAGYDGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRL------RW----------QGK-RPVIGW 80
Cdd:TIGR03269 296 VVKAVDNVSLE------VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWvdmtkpgpdgRGRaKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqFPL-----NVQDVVsqgawpGVSLLRGLGgctRRRIGAVLERVGLAG------LAKTPIEaLSGGQFQRM 149
Cdd:TIGR03269 370 LHQEYDL---YPHrtvldNLTEAI------GLELPDELA---RMKAVITLKMVGFDEekaeeiLDKYPDE-LSEGERHRV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119115049 150 LFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHDNQRVAD 205
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLD 493
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
35-198 |
5.36e-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: 64.76 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWLAQRHALesqFPLNVQDVVSQGAW 104
Cdd:TIGR01193 497 IKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlRQFINYLPQEPYI---FSGSILENLLLGAK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 PGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEA--LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDL 182
Cdd:TIGR01193 574 ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
170
....*....|....*.
gi 1119115049 183 ILEMyrQGQTILAVLH 198
Cdd:TIGR01193 654 LLNL--QDKTIIFVAH 667
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
35-233 |
5.63e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGW-LAQRHALESQFPLNVQDvvSQGA--------WP 105
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-EPLAKLnRAQRKAFRRDIQMVFQD--SISAvnprktvrEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 GVSLLRGLGGCTRR----RIGAVLERVGLAG--LAKTPiEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSREL 179
Cdd:PRK10419 112 IREPLRHLLSLDKAerlaRASEMLRAVDLDDsvLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 180 MDLILEMYRQGQT-ILAVLHDNQRVADFFPETLLLTPQRACWGATRAVLPAFSHA 233
Cdd:PRK10419 191 IRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSP 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-207 |
6.16e-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: 62.93 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQRHALE----- 88
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE-DITKLPPHERARAgiayv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 SQ----FP-LNVQDvvsqgawpgvSLLRGLGGCTR--RRIGA-------VLE--RVGLAGLaktpieaLSGGQFQRMLFA 152
Cdd:TIGR03410 81 PQgreiFPrLTVEE----------NLLTGLAALPRrsRKIPDeiyelfpVLKemLGRRGGD-------LSGGQQQQLAIA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119115049 153 RVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAV---LHDNQRVADFF 207
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVeqyLDFARELADRY 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-186 |
6.31e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIG---WLAQRHALESQFP---LNVQDVVSQGA 103
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysYRSQRIRMIFQDPstsLNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WPGVSLLRGLGGCTR-RRIGAVLERVGL-AGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:PRK15112 111 DFPLRLNTDLEPEQReKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
....*
gi 1119115049 182 LILEM 186
Cdd:PRK15112 191 LMLEL 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-199 |
6.91e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLR-----WQGKRPV-------- 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTARSLsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 78 -----IGWLAQ-------RHALES--QFPLNVQDVVSQGAwpgVSLLRGLggctrrrigavLERVGLAGLAKTPIEALSG 143
Cdd:PRK11264 82 qlrqhVGFVFQnfnlfphRTVLENiiEGPVIVKGEPKEEA---TARAREL-----------LAKVGLAGKETSYPRRLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 144 GQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
35-199 |
7.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWLAQRHalESQFplnVQDVVSQGAW 104
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklRKHIGIVFQNP--DNQF---VGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 PGVSLLRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170
....*....|....*.
gi 1119115049 185 EMYRQGQ-TILAVLHD 199
Cdd:PRK13648 187 KVKSEHNiTIISITHD 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
37-198 |
8.12e-12 |
|
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: 62.49 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIG----WLAQRHALESQFPL----NVQDVVSQgawpgvs 108
Cdd:cd03248 39 PGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK-PISQyehkYLHSKVSLVGQEPVlfarSLQDNIAY------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 llrGLGGCTRRRIGAVLERVG----LAGLAKTPIEA-------LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDeATSR 177
Cdd:cd03248 111 ---GLQSCSFECVKEAAQKAHahsfISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD-AESE 186
|
170 180
....*....|....*....|.
gi 1119115049 178 ELMDLILEMYRQGQTILAVLH 198
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAH 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-208 |
8.70e-12 |
|
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: 62.67 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVVSQGAWPGV 107
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLLRgLGGCTRRRIGAVL-ERVGLAGLAKTPI-----EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:cd03234 106 AILR-LPRKSSDAIRKKRvEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS 184
|
170 180
....*....|....*....|....*..
gi 1119115049 182 LILEMYRQGQTILAVLHdnQRVADFFP 208
Cdd:cd03234 185 TLSQLARRNRIVILTIH--QPRSDLFR 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-215 |
8.85e-12 |
|
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: 61.40 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQL-VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLrwqgkrpvigwlaQRHALESQF 91
Cdd:cd03223 1 IELENLsLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 plnvqdVVSQGAWPGVSLLRGLggctrrrigavlervglagLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:cd03223 68 ------FLPQRPYLPLGTLREQ-------------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 172 DEATSRELMDLILEMyrqGQTILAVLHdNQRVADFFPETLLLTP 215
Cdd:cd03223 123 DEESEDRLYQLLKEL---GITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-194 |
1.35e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGwlAQRHALE----------SQFP-LNVQDVVSQGA 103
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR--SPRDAIAlgigmvhqhfMLVPnLTVAENIVLGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WPGVSLLRGLGGcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLI 183
Cdd:COG3845 106 EPTKGGRLDRKA-ARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEIL 184
|
170
....*....|.
gi 1119115049 184 LEMYRQGQTIL 194
Cdd:COG3845 185 RRLAAEGKSII 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-198 |
1.40e-11 |
|
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: 61.74 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRP-VIGwlaqRHALESQFPLNVQDVVsqgawpgvsL 109
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIsKIG----LHDLRSRISIIPQDPV---------L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRG--------LGGCTRRRIGAVLERVGLAGLAK-------TPIEA----LSGGQFQRMLFARVMVQQAPLVMLDEPFTG 170
Cdd:cd03244 90 FSGtirsnldpFGEYSDEELWQALERVGLKEFVEslpggldTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180
....*....|....*....|....*...
gi 1119115049 171 IDEATSRELMDLILEMYRqGQTILAVLH 198
Cdd:cd03244 170 VDPETDALIQKTIREAFK-DCTVLTIAH 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-204 |
1.85e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALESQ-----------FP-LNVQDVVSQGAw 104
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhvgfvfqsfmlIPtLNALENVELPA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 pgvsLLRGLG-GCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLI 183
Cdd:PRK10584 114 ----LLRGESsRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180
....*....|....*....|..
gi 1119115049 184 LEMYR-QGQTILAVLHDNQRVA 204
Cdd:PRK10584 190 FSLNReHGTTLILVTHDLQLAA 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-198 |
2.13e-11 |
|
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: 62.81 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGY--DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQrhALESQ 90
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH-DLADYTLA--SLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 91 FPLNVQDVV----SQGAWPGVSLLRGLGgctRRRIGAVLERVGLAGLA-------KTPIEA----LSGGQFQRMLFARVM 155
Cdd:TIGR02203 408 VALVSQDVVlfndTIANNIAYGRTEQAD---RAEIERALAAAYAQDFVdklplglDTPIGEngvlLSGGQRQRLAIARAL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDlILEMYRQGQTILAVLH 198
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQA-ALERLMQGRTTLVIAH 526
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-232 |
2.58e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFL-----PPVSGRLRWQG----KRPVIGwL 81
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGqdifKMDVIE-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 82 AQRHALESQFP-----LNVQDVVSQGawPGVSLLRGLGGCTRRRIGAVLERVGLAGLAK----TPIEALSGGQFQRMLFA 152
Cdd:PRK14247 81 RRRVQMVFQIPnpipnLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 153 RVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLHDNQ---RVADFFpeTLLLTPQRACWGATRAVLPA 229
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQqaaRISDYV--AFLYKGQIVEWGPTREVFTN 235
|
...
gi 1119115049 230 FSH 232
Cdd:PRK14247 236 PRH 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-199 |
4.59e-11 |
|
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: 61.22 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGK----------RPV----IGWLAQ-- 83
Cdd:COG0444 22 DGVSFD------VRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklsekelRKIrgreIQMIFQdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 ------RHALESQF--PLNVQDVVSQGAWpgvsllrglggctRRRIGAVLERVGLAG----LAKTPIEaLSGGQFQRMLF 151
Cdd:COG0444 96 mtslnpVMTVGDQIaePLRIHGGLSKAEA-------------RERAIELLERVGLPDperrLDRYPHE-LSGGMRQRVMI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHD 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-204 |
5.88e-11 |
|
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: 61.28 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 41 TAIVGLNGCGKSTLLKTLAGFLPPVSGRLR-----WQGKRPVIGWLAQRHAL------ESQFP-LNVQDVVSQGAWpgvs 108
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRKGIFLPPEKRRIgyvfqeARLFPhLSVRGNLRYGMK---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 llRGLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR 188
Cdd:TIGR02142 102 --RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170
....*....|....*..
gi 1119115049 189 Q-GQTILAVLHDNQRVA 204
Cdd:TIGR02142 180 EfGIPILYVSHSLQEVL 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-212 |
6.13e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPpvsgrlrwqgKRPVIGWlaqrhalesqfplnvqDVVSQGAWP-GVSLLRGL 113
Cdd:COG2401 53 IEPGEIVLIVGASGSGKSTLLRLLAGALK----------GTPVAGC----------------VDVPDNQFGrEASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 114 GgcTRRRIGAVLERVGLAGLA-----KTPIEALSGGQFQRMLFARVMVQQAPLVMLDEpFT-GIDEATSRELMDLILEMY 187
Cdd:COG2401 107 G--RKGDFKDAVELLNAVGLSdavlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCsHLDRQTAKRVARNLQKLA 183
|
170 180
....*....|....*....|....*.
gi 1119115049 188 RQ-GQTILAVLHDNQRVADFFPETLL 212
Cdd:COG2401 184 RRaGITLVVATHHYDVIDDLQPDLLI 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-198 |
6.59e-11 |
|
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: 60.32 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGY--DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK--RPVigwlaQRHALE 88
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvRDY-----TLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 SQFPLNVQDV------VSQgawpgvSLLRGLGGCTRRRIGAVLERVGLAGLAK-------TPIE----ALSGGQFQRMLF 151
Cdd:cd03251 76 RQIGLVSQDVflfndtVAE------NIAYGRPGATREEVEEAARAANAHEFIMelpegydTVIGergvKLSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119115049 152 ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYrQGQTILAVLH 198
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-215 |
7.31e-11 |
|
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: 59.18 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAG----------FLppVSGRLRWQGKRPVIGWLAQRHALESQfpLNVQDVVSQ 101
Cdd:cd03232 27 SGYVKPGTLTALMGESGAGKTTLLDVLAGrktagvitgeIL--INGRPLDKNFQRSTGYVEQQDVHSPN--LTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 102 GAWpgvslLRGLGGCTRRRIGAVLErvglagLAKTPIealsggqfqrmlfarvmvqqapLVMLDEPFTGIDEATSRELMD 181
Cdd:cd03232 103 SAL-----LRGLSVEQRKRLTIGVE------LAAKPS----------------------ILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1119115049 182 LILEMYRQGQTILAVLHD-NQRVADFFPETLLLTP 215
Cdd:cd03232 150 FLKKLADSGQAILCTIHQpSASIFEKFDRLLLLKR 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-206 |
7.82e-11 |
|
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: 59.46 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFlP---PVSGRLRWQGK-----------RPVI 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKGEditdlppeeraRLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GwlaqrhaLESQFPLNVqdvvsqgawPGVSL---LRGLGgctrrrigavlervglaglaktpiEALSGGQFQRMLFARVM 155
Cdd:cd03217 80 F-------LAFQYPPEI---------PGVKNadfLRYVN------------------------EGFSGGEKKRNEILQLL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHdNQRVADF 206
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH-YQRLLDY 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
38-199 |
8.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIgwlaqRHALESQFPLNVQDVVSQGAWPGVSLLRGLggct 117
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKN-----KKKTKEKEKVLEKLVIQKTRFKKIKKIKEI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 118 RRRIGAV--------------------------------------LERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQ 157
Cdd:PRK13651 104 RRRVGVVfqfaeyqlfeqtiekdiifgpvsmgvskeeakkraakyIELVGLdeSYLQRSPFE-LSGGQKRRVALAGILAM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 158 QAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
43-172 |
1.36e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 59.27 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 43 IVGL---NGCGKSTLLKTLAGFLPPVSGRLRWQGKR----PV-------IGWLAQRHaleSQF-PLNVQD---VVSQgaw 104
Cdd:COG1137 31 IVGLlgpNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlPMhkrarlgIGYLPQEA---SIFrKLTVEDnilAVLE--- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119115049 105 pgvslLRGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:COG1137 105 -----LRKLSKKEREeRLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-167 |
1.56e-10 |
|
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: 60.08 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGfLPPVSGRLRWQGkRPVIGW-----LAQRHALESQF------ 91
Cdd:COG4172 303 DGVSLT------LRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDG-QDLDGLsrralRPLRRRMQVVFqdpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 --P-LNVQDVVSQGawpgvslLR----GLGGCTRR-RIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQAPL 161
Cdd:COG4172 375 lsPrMTVGQIIAEG-------LRvhgpGLSAAERRaRVAEALEEVGLdpAARHRYPHE-FSGGQRQRIAIARALILEPKL 446
|
....*.
gi 1119115049 162 VMLDEP 167
Cdd:COG4172 447 LVLDEP 452
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
39-198 |
1.73e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 39 SLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGW----LAQRHALESQFPLnvqdVVSQGAWPGVSLLRglg 114
Cdd:PRK10790 368 GFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-RPLSSLshsvLRQGVAMVQQDPV----VLADTFLANVTLGR--- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 115 GCTRRRIGAVLERVGLAGLAKTPIEA-----------LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDlI 183
Cdd:PRK10790 440 DISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ-A 518
|
170
....*....|....*
gi 1119115049 184 LEMYRQGQTILAVLH 198
Cdd:PRK10790 519 LAAVREHTTLVVIAH 533
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-198 |
1.77e-10 |
|
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: 60.05 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITPP---------LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR----------PVIGWLAQ 83
Cdd:TIGR01842 320 ENVTIVPPggkkptlrgISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADlkqwdretfgKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 84 rhalesqfplnvqdvvsqgawpGVSLLRGLGGCTRRRIG------AVLERVGLAG----LAKTPI----------EALSG 143
Cdd:TIGR01842 400 ----------------------DVELFPGTVAENIARFGenadpeKIIEAAKLAGvhelILRLPDgydtvigpggATLSG 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 144 GQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-206 |
2.74e-10 |
|
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: 58.19 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYdGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGwLAQRHALES 89
Cdd:cd03369 7 IEVENLSVRY-APDLPPVLKNVsfkVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID--IS-TIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 QFPLNVQDVVsqgawpgvsLLRG--------LGGCTRRRIGAVLeRVGLAGLAktpieaLSGGQFQRMLFARVMVQQAPL 161
Cdd:cd03369 83 SLTIIPQDPT---------LFSGtirsnldpFDEYSDEEIYGAL-RVSEGGLN------LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 162 VMLDEPFTGIDEATSRELMDLILEMYrQGQTILAVLHDNQRVADF 206
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-185 |
2.76e-10 |
|
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: 59.56 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWqGKRPVIGWLAQ-RHALESQf 91
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQsRDALDPN- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 pLNVQDVVSQGAwpgvSLLRgLGGctrRRIG--AVLERVGLAGLAK-TPIEALSGGQFQRMLFARVMVQQAPLVMLDEPF 168
Cdd:TIGR03719 401 -KTVWEEISGGL----DIIK-LGK---REIPsrAYVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170
....*....|....*..
gi 1119115049 169 TGIDEATSRELMDLILE 185
Cdd:TIGR03719 472 NDLDVETLRALEEALLN 488
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-186 |
3.26e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 16 EQLVAGYDGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALES------ 89
Cdd:PRK11308 25 ERLVKALDGVSFT------LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQkiqivf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 QFP---LNVQDVVSQGAWPGVSLLRGLGGCTRR-RIGAVLERVGL-AGLAKTPIEALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:PRK11308 99 QNPygsLNPRKKVGQILEEPLLINTSLSAAERReKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180
....*....|....*....|....*.
gi 1119115049 165 DEPFTGIDEATSRE----LMDLILEM 186
Cdd:PRK11308 179 DEPVSALDVSVQAQvlnlMMDLQQEL 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-206 |
4.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.52 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG-----KRPVIGWLAQRHALESQFP---LNVQDVVSQGAWPGVSL 109
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIRKKVGLVFQYPeyqLFEETIEKDIAFGPINL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 lrGLG-GCTRRRIGAVLERVGLAG---LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILE 185
Cdd:PRK13637 113 --GLSeEEIENRVKRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKE 189
|
170 180
....*....|....*....|..
gi 1119115049 186 MYRQ-GQTILAVLHDNQRVADF 206
Cdd:PRK13637 190 LHKEyNMTIILVSHSMEDVAKL 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-213 |
4.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG-------KRPVIGWLAQRHALESQFP------------------ 92
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPVRKRIGMVFQFPesqlfedtvereiifgpk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 ---LNVQDVVSQGawpgVSLLRGLGgcTRRRIgavlervglagLAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFT 169
Cdd:PRK13646 113 nfkMNLDEVKNYA----HRLLMDLG--FSRDV-----------MSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 170 GIDEATSRELMDLILEM-YRQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-198 |
4.22e-10 |
|
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: 59.26 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 7 GGDAAMIELEQLVAGYDGVaiTPPLSGMIC----PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPV--IGW 80
Cdd:TIGR01257 1932 GNKTDILRLNELTKVYSGT--SSPAVDRLCvgvrPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALESQFPLnVQDVVSqgAWPGVSLLRGLGGCTRRRIGAV----LERVGLAGLAKTPIEALSGGQFQRMLFARVMV 156
Cdd:TIGR01257 2010 VHQNMGYCPQFDA-IDDLLT--GREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 157 QQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-198 |
4.65e-10 |
|
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: 57.88 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGY--DGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGW 80
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqFPLNVQDVVSQGAwPGVSLLRglggctrrrigaVLERVGLAG----LAKTPI----------EALSGGQF 146
Cdd:cd03252 81 VLQENVL---FNRSIRDNIALAD-PGMSMER------------VIEAAKLAGahdfISELPEgydtivgeqgAGLSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 147 QRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDlilEMYR--QGQTILAVLH 198
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMR---NMHDicAGRTVIIIAH 195
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-205 |
5.14e-10 |
|
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: 58.66 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITP-----PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWlAQRHAL 87
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgftlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP--VTA-DNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ESQF------------PLNVQDVVSqgawpgvsllrglggctRRRIGAVLERVGLAGlaKTPIE-------ALSGGQFQR 148
Cdd:COG4615 405 RQLFsavfsdfhlfdrLLGLDGEAD-----------------PARARELLERLELDH--KVSVEdgrfsttDLSQGQRKR 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 149 --MLFArvMVQQAPLVMLDE-------PFtgideatsREL--MDLILEMYRQGQTILAVLHDNQ--RVAD 205
Cdd:COG4615 466 laLLVA--LLEDRPILVFDEwaadqdpEF--------RRVfyTELLPELKARGKTVIAISHDDRyfDLAD 525
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
38-198 |
5.89e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.79 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---KRPVIGW-LAQRHALESQFPLN--VQDVVSQGAWPGVSLLR 111
Cdd:PRK13633 36 GEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWdIRNKAGMVFQNPDNqiVATIVEEDVAFGPENLG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 112 GLGGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQ-G 190
Cdd:PRK13633 116 IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyG 195
|
....*...
gi 1119115049 191 QTILAVLH 198
Cdd:PRK13633 196 ITIILITH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
31-199 |
7.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---------VSG-----RLRWQgKRPVIGWLAQRHalESQF-PLNV 95
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGitltaKTVWD-IREKVGIVFQNP--DNQFvGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 96 QDVVSQGAWPgvsllRGLGGCTRRRIGA-VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:PRK13640 103 GDDVAFGLEN-----RAVPRPEMIKIVRdVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180
....*....|....*....|....*.
gi 1119115049 175 TSRELMDLILE-MYRQGQTILAVLHD 199
Cdd:PRK13640 178 GKEQILKLIRKlKKKNNLTVISITHD 203
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-167 |
8.77e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.82 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 23 DGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPVIGwlAQRHALES---------QFP- 92
Cdd:COG4608 35 DGVSFD------IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG-QDITG--LSGRELRPlrrrmqmvfQDPy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 --LN----VQDVVS-----QGAWPGVSLlrglggctRRRIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQA 159
Cdd:COG4608 106 asLNprmtVGDIIAeplriHGLASKAER--------RERVAELLELVGLrpEHADRYPHE-FSGGQRQRIGIARALALNP 176
|
....*...
gi 1119115049 160 PLVMLDEP 167
Cdd:COG4608 177 KLIVCDEP 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-199 |
9.41e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRL----RWQGkrpVIGWLAQRhALESQFPLNVQDVVSQGAWPG-VSLL- 110
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE---ILDEFRGS-ELQNYFTKLLEGDVKVIVKPQyVDLIp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 RGLGGCTRRRIGA---------VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:cd03236 101 KAVKGKVGELLKKkdergkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170
....*....|....*...
gi 1119115049 182 LILEMYRQGQTILAVLHD 199
Cdd:cd03236 181 LIRELAEDDNYVLVVEHD 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
43-194 |
1.03e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 43 IVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGwlaqrhalesqfplNVQDVVSQGawpgvsllrgLGGCT--RRR 120
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR--------------SPRDAIRAG----------IAYVPedRKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 121 IG-------------AVLERVGLAGL-----------------------AKTPIEALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:COG1129 339 EGlvldlsirenitlASLDRLSRGGLldrrreralaeeyikrlriktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 165 DEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-199 |
1.10e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpVIG-----WLAQRHALESQF--PL-------NVQDVVS--- 100
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD-LLGmkddeWRAVRSDIQMIFqdPLaslnprmTIGEIIAepl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 101 QGAWPGVSllrglGGCTRRRIGAVLERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:PRK15079 126 RTYHPKLS-----RQEVKDRVKAMMLKVGLLPnlINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180
....*....|....*....|..
gi 1119115049 179 LMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK15079 200 VVNLLQQLQREmGLSLIFIAHD 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-204 |
1.35e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.05 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 10 AAMIELEQLVAGYDGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG----------KRP 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVsfhVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 77 VIGWLAQRHalESQF-PLNVQDVVSQGAW-PGVSLLRglggcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARV 154
Cdd:PRK13650 82 KIGMVFQNP--DNQFvGATVEDDVAFGLEnKGIPHEE-----MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHDNQRVA 204
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVA 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-196 |
1.72e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 19 VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGwlAQRHALESQFPLNVQDV 98
Cdd:PRK11288 260 LDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR--SPRDAIRAGIMLCPEDR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 99 VSQGAWPGVSLLRGLGGCTRR---RIGAVLERVGLAGLA---------KTP-----IEALSGGQFQRMLFARVMVQQAPL 161
Cdd:PRK11288 338 KAEGIIPVHSVADNINISARRhhlRAGCLINNRWEAENAdrfirslniKTPsreqlIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190
....*....|....*....|....*....|....*
gi 1119115049 162 VMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV 452
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-206 |
1.92e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKSTLLKTLAGFL-----PPVSGRLRWQGK------------RPVIGWLAQrhaLESQFP-LNVQDVVSQGA 103
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRniyspdvdpievRREVGMVFQ---YPNPFPhLTIYDNVAIGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 wpgvsllrGLGGCTRRRiGAVLERVGLAgLAKTPI------------EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:PRK14267 111 --------KLNGLVKSK-KELDERVEWA-LKKAALwdevkdrlndypSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1119115049 172 DEATSRELMDLILEMyRQGQTILAVLHD---NQRVADF 206
Cdd:PRK14267 181 DPVGTAKIEELLFEL-KKEYTIVLVTHSpaqAARVSDY 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-199 |
2.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIG--W-LAQRH 85
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvWnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 86 ALESQFPLN------VQDVVSQG----AWPGVSLLRglggctrrRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVM 155
Cdd:PRK13642 84 GMVFQNPDNqfvgatVEDDVAFGmenqGIPREEMIK--------RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQ-TILAVLHD 199
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHD 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-198 |
2.64e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGwlAQRHALES------------------------QFP 92
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTAALAAgvaiiyqelhlvpemtvaenlylgQLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 93 lnvqdvvSQGAWPGVSLLrglggctRRRIGAVLERVGLAGLAKTPIEALSGGQFQrmlfarvMVQQAPLVMLDEPFTGID 172
Cdd:PRK11288 107 -------HKGGIVNRRLL-------NYEAREQLEHLGVDIDPDTPLKYLSIGQRQ-------MVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|...
gi 1119115049 173 EATS----RE---LMDLILEMYRQGQTILAVLH 198
Cdd:PRK11288 166 EPTSslsaREieqLFRVIRELRAEGRVILYVSH 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
42-205 |
2.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWLAQRHALESQFPLNVQDVvsqgAWPGVSLlr 111
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevRKFVGLVFQNPDDQIFSPTVEQDI----AFGPINL-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 112 GLGGCT-RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEM-YRQ 189
Cdd:PRK13652 108 GLDEETvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETY 187
|
170
....*....|....*.
gi 1119115049 190 GQTILAVLHDNQRVAD 205
Cdd:PRK13652 188 GMTVIFSTHQLDLVPE 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-215 |
3.05e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.48 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpVIGWLAQRHALE--- 88
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-VNDPKVDERLIRqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 ----SQFPLNVQDVVSQGAWPGVSLLRGLGGCTRRRIG-AVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVM 163
Cdd:PRK09493 80 gmvfQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 164 LDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH---------------DNQRVA-DFFPETLLLTP 215
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHeigfaekvasrlifiDKGRIAeDGDPQVLIKNP 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-172 |
3.20e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWqGKRPVIGWLAQrHALE--- 88
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQ-HQLEflr 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 89 -SQFPLnvQDVVSQGAWPGVSLLRG-LGGctrrrigavlerVGLAGLAKT-PIEALSGGQFQRMLFARVMVQQAPLVMLD 165
Cdd:PRK10636 390 aDESPL--QHLARLAPQELEQKLRDyLGG------------FGFQGDKVTeETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
....*..
gi 1119115049 166 EPFTGID 172
Cdd:PRK10636 456 EPTNHLD 462
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-199 |
3.87e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 9 DAAMIELEQLVAGYDGVaiTPP----LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK---------- 74
Cdd:PRK13632 4 KSVMIKVENVSFSYPNS--ENNalknVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkei 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 RPVIGWLAQRHalESQF-PLNVQDVVSqgawpgvsllRGLGG--CTRRRIGAVLE----RVGLAGLAKTPIEALSGGQFQ 147
Cdd:PRK13632 82 RKKIGIIFQNP--DNQFiGATVEDDIA----------FGLENkkVPPKKMKDIIDdlakKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 148 RMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQG-QTILAVLHD 199
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHD 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
35-207 |
4.45e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTL-------AGFLppVSGRLRWQGK-------RPV-----IGWLAQRHALesqFPLNV 95
Cdd:COG1117 34 IPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEdiydpdvDVVelrrrVGMVFQKPNP---FPKSI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 96 QDVVSQGawpgvslLRgLGGCTRRRI--GAV---LERVGL----------AGLaktpieALSGGQFQRMLFARVMVQQAP 160
Cdd:COG1117 109 YDNVAYG-------LR-LHGIKSKSEldEIVeesLRKAALwdevkdrlkkSAL------GLSGGQQQRLCIARALAVEPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 161 LVMLDEPFTGID-EATSR-ElmDLILEMyRQGQTILAVLHDNQ---RVAD---FF 207
Cdd:COG1117 175 VLLMDEPTSALDpISTAKiE--ELILEL-KKDYTIVIVTHNMQqaaRVSDytaFF 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-236 |
7.06e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 18 LVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGrLRWQGK-----------------RPVIGW 80
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDvllggrsifnyrdvlefRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRhalESQFPLNVQDVVSQGAWPGVSL----LRGLGGCTRRRIG---AVLERvglagLAKTPIEaLSGGQFQRMLFAR 153
Cdd:PRK14271 106 LFQR---PNPFPMSIMDNVLAGVRAHKLVprkeFRGVAQARLTEVGlwdAVKDR-----LSDSPFR-LSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 154 VMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQgQTILAVLHD-------NQRVADFFPETLLLTpqracwGATRAV 226
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNlaqaariSDRAALFFDGRLVEE------GPTEQL 249
|
250
....*....|
gi 1119115049 227 LPAFSHARSA 236
Cdd:PRK14271 250 FSSPKHAETA 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-199 |
1.14e-08 |
|
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: 54.94 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQ-GKRpvIGWLAQRHALESQfpLNVQDVVSQGAWPGVSLLRGL-- 113
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIK--VGYLPQEPQLDPT--KTVRENVEEGVAEIKDALDRFne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 114 ------------------GGCTRRRIGAV----LER-VGLAGLA------KTPIEALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:TIGR03719 106 isakyaepdadfdklaaeQAELQEIIDAAdawdLDSqLEIAMDAlrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170 180 190
....*....|....*....|....*....|....*
gi 1119115049 165 DEPFTGIDeATSRELMDLILEMYrQGqTILAVLHD 199
Cdd:TIGR03719 186 DEPTNHLD-AESVAWLERHLQEY-PG-TVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-167 |
1.44e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvIGWLAQRhaLESQFPLNVQDVVSQ------GAWP 105
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---ISYKPQY--IKPDYDGTVEDLLRSitddlgSSYY 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 106 GVSLLRGLGgctrrrIGAVLERvglaglaktPIEALSGGQFQRMLFARVMVQQAPLVMLDEP 167
Cdd:PRK13409 434 KSEIIKPLQ------LERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-213 |
1.63e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGflpPVSGRLRWQGKRPVIGwlaqrHALESQFPLNV-----QDVVSQGAWPG 106
Cdd:TIGR00956 783 DGWVKPGTLTALMGASGAGKTTLLNVLAE---RVTTGVITGGDRLVNG-----RPLDSSFQRSIgyvqqQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 107 VSL-----LRGLGGCTR----RRIGAVLERVGLAGLAK----TPIEALSGGQFQRMLFARVMVQQ-APLVMLDEPFTGID 172
Cdd:TIGR00956 855 ESLrfsayLRQPKSVSKsekmEYVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKpKLLLFLDEPTSGLD 934
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 173 EATSRELMDLILEMYRQGQTILAVLHdnQRVADFFPE--TLLL 213
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHGQAILCTIH--QPSAILFEEfdRLLL 975
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-198 |
1.77e-08 |
|
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: 53.31 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 24 GVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---KRPVIGWLAQRHALESQ----FPLNVQ 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWLRSQIGLVSQepvlFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 97 DVVSQGAWPGV--------------SLLRGL--GGCTrrrigavleRVGLAGLaktpieALSGGQFQRMLFARVMVQQAP 160
Cdd:cd03249 95 ENIRYGKPDATdeeveeaakkanihDFIMSLpdGYDT---------LVGERGS------QLSGGQKQRIAIARALLRNPK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1119115049 161 LVMLDEPFTGIDeATSRELMDLILEMYRQGQTILAVLH 198
Cdd:cd03249 160 ILLLDEATSALD-AESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
38-198 |
1.89e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG---KRPVIGWLAQRHALESQFPLNVQDVVSQGAWPGVSLLRGLG 114
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsiKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 115 GctrrrIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:PRK13540 107 G-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVL 181
|
....
gi 1119115049 195 AVLH 198
Cdd:PRK13540 182 LTSH 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-199 |
1.92e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDG-VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLrWQGKRPV---------IGW 80
Cdd:PRK11650 2 AGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVnelepadrdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LAQRHALesqFP-LNVQDVVSQGawpgvsL-LRGLGGCT-RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQ 157
Cdd:PRK11650 81 VFQNYAL---YPhMSVRENMAYG------LkIRGMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119115049 158 QAPLVMLDEPFTGIDeATSRELMDL-ILEMYRQ-GQTILAVLHD 199
Cdd:PRK11650 152 EPAVFLFDEPLSNLD-AKLRVQMRLeIQRLHRRlKTTSLYVTHD 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-205 |
2.34e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGR------------LRWQGKRPvI 78
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRG-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALESQfpLNVQDVVSqgawpGVSLLRGLGGCTRR--RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMV 156
Cdd:PRK10895 81 GYLPQEASIFRR--LSVYDNLM-----AVLQIRDDLSAEQRedRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119115049 157 QQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVAD 205
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLA 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-198 |
2.74e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWLAQRHALES-------QFPLNVQDVVSQGAWPGVSL 109
Cdd:PRK10982 23 PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE--IDFKSSKEALENgismvhqELNLVLQRSVMDNMWLGRYP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRGL---GGCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEM 186
Cdd:PRK10982 101 TKGMfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL 180
|
170
....*....|..
gi 1119115049 187 YRQGQTILAVLH 198
Cdd:PRK10982 181 KERGCGIVYISH 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-198 |
2.83e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigWLAQRHALESQF 91
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN----YNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 -------PLNVQDVVS--QGAWPGVSLLRGLGGCT-------RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVM 155
Cdd:PRK09700 81 gigiiyqELSVIDELTvlENLYIGRHLTKKVCGVNiidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 156 VQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH 198
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-205 |
3.00e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVS--GRLRWQGKRP-------------VIgwLAQRHAL-------ESQFPLN 94
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdirdsealgiVI--IHQELALipylsiaENIFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 95 VQdvVSQGA--WPGvsllrglggcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:NF040905 104 ER--AKRGVidWNE----------TNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119115049 173 EATSRELMDLILEMYRQGQTILAVLHD-NQ--RVAD 205
Cdd:NF040905 172 EEDSAALLDLLLELKAQGITSIIISHKlNEirRVAD 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-205 |
3.36e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 11 AMIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWLAQRHALESq 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-DITDWQTAKIMREA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 91 fplnvQDVVSQG----AWPGVSLLRGLGGC------TRRRIGAVLE--------RVGLAGlaktpieALSGGQFQRMLFA 152
Cdd:PRK11614 82 -----VAIVPEGrrvfSRMTVEENLAMGGFfaerdqFQERIKWVYElfprlherRIQRAG-------TMSGGEQQMLAIG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 153 RVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD-NQ--RVAD 205
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNaNQalKLAD 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-204 |
3.40e-08 |
|
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: 53.29 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLP--PVSGRLRWQG-----------KRPVI 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGsplkasnirdtERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLAQRHALESQfpLNVQDVVSQG---AWPGVSLLRGLggcTRRRIGAVLERVGLAGLAKT-PIEALSGGQFQRMLFARV 154
Cdd:TIGR02633 81 VIIHQELTLVPE--LSVAENIFLGneiTLPGGRMAYNA---MYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 155 MVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQRVA 204
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-204 |
3.94e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 25 VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLA----GFLPPVSGRLRWQG------KRPVIGWLAQRHALESQFP-L 93
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpeeiKKHYRGDVVYNAETDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 94 NVQDVVSQGAwpgvsLLRGLG----GCTRRRIGAVLERVGLA--GLAKTP--------IEALSGGQFQRMLFARVMVQQA 159
Cdd:TIGR00956 154 TVGETLDFAA-----RCKTPQnrpdGVSREEYAKHIADVYMAtyGLSHTRntkvgndfVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119115049 160 PLVMLDEPFTGIDEATSrelmdliLEMYRQGQTILAVLHDNQRVA 204
Cdd:TIGR00956 229 KIQCWDNATRGLDSATA-------LEFIRALKTSANILDTTPLVA 266
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
38-199 |
4.76e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLagflppvsgrLRWQGKRPVIGWLaqrhaleSQFPLNVQDVVSQgawpgVSLLRGLGgct 117
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEG----------LYASGKARLISFL-------PKFSRNKLIFIDQ-----LQFLIDVG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 118 rrrIGAV-LERvglaglaktPIEALSGGQFQRMLFARVMVQQAP--LVMLDEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:cd03238 76 ---LGYLtLGQ---------KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVI 143
|
....*
gi 1119115049 195 AVLHD 199
Cdd:cd03238 144 LIEHN 148
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-199 |
4.81e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.73 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG--------------KRPVIGWLAQRHALESQfpLNVQDVVSQGA 103
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevRRKKIAMVFQSFALMPH--MTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WpgvslLRGLGGCTRRRIGA-VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDL 182
Cdd:PRK10070 132 E-----LAGINAEERREKALdALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170
....*....|....*...
gi 1119115049 183 ILEMYRQGQ-TILAVLHD 199
Cdd:PRK10070 207 LVKLQAKHQrTIVFISHD 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-199 |
5.10e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.39 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQL----------VAGYDGVAITpplsgmICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------- 74
Cdd:COG1135 1 MIELENLsktfptkggpVTALDDVSLT------IEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 ---RPV---IGW-------LAQRHALEsqfplNVqdvvsqgAWP----GVSllrglGGCTRRRIGAVLERVGLAGLAKTP 137
Cdd:COG1135 75 relRAArrkIGMifqhfnlLSSRTVAE-----NV-------ALPleiaGVP-----KAEIRKRVAELLELVGLSDKADAY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 138 IEALSGGQFQRMLFARVMVQQaPLVML-DEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANN-PKVLLcDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-181 |
5.72e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkrpvigwlaqRHALESQFPLNVQDVVSQGAWPGVSLlrglggcT 117
Cdd:cd03291 63 GEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQFSWIMPGTIKENIIFGVSY-------D 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 118 RRRIGAVLERVGLA-GLAKTPIE----------ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:cd03291 126 EYRYKSVVKACQLEeDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-167 |
5.89e-08 |
|
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: 51.64 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 33 GMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQgkRPVIGWLAQRhaLESQFPLNVQDVVSqgawpgvSLLRG 112
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--LDTVSYKPQY--IKADYEGTVRDLLS-------SITKD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 113 LGGCTRRRIgAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEP 167
Cdd:cd03237 89 FYTHPYFKT-EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-190 |
6.60e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLP--PVSGRLRWQGK-----------RPVIGWLAQRHALESQfpLNVQDVVSQGA 103
Cdd:PRK13549 30 AGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEelqasnirdteRAGIAIIHQELALVKE--LSVLENIFLGN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 104 WPGVsllrglGGCTR-----RRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:PRK13549 108 EITP------GGIMDydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAV 181
|
170
....*....|..
gi 1119115049 179 LMDLILEMYRQG 190
Cdd:PRK13549 182 LLDIIRDLKAHG 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-199 |
6.98e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHALESQFPLNVQD---VVSQGAWPGVSLLRGL 113
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyaSLDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 114 -------GGCTRRRIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK10261 429 rvhgllpGKAAAARVAWLLERVGLlpEHAWRYPHE-FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170
....*....|....*.
gi 1119115049 185 EMYRQ-GQTILAVLHD 199
Cdd:PRK10261 508 DLQRDfGIAYLFISHD 523
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-210 |
7.27e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 29 PPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPvigwlaqrhalesqfplnvqdVVSQGAWP 105
Cdd:TIGR00957 652 PTLNGItfsIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---------------------YVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 106 GVSLLRG--LGGC--TRRRIGAVLERVG-------LAGLAKTPIEA----LSGGQFQRMLFARVMVQQAPLVMLDEPFTG 170
Cdd:TIGR00957 711 QNDSLREniLFGKalNEKYYQQVLEACAllpdleiLPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 171 IDEATSRELMDLIL--EMYRQGQTILAVLHDnqrvADFFPET 210
Cdd:TIGR00957 791 VDAHVGKHIFEHVIgpEGVLKNKTRILVTHG----ISYLPQV 828
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
38-199 |
7.75e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK-----RPVIGWLA-----QRHALESQFPLNVQDVvsqGAWPGV 107
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvRDKDGQLKvadknQLRLLRTRLTMVFQHF---NLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLLR----------GLGGC-TRRRIGAVLERVGLAGLA--KTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:PRK10619 108 TVLEnvmeapiqvlGLSKQeARERAVKYLAKVGIDERAqgKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*
gi 1119115049 175 TSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-167 |
8.22e-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: 52.09 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrpvIGWLAQRhaLESQFPLNVQDVvsqgawpgvsllr 111
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---ISYKPQY--ISPDYDGTVEEF------------- 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 112 gLGGCTRRRIGA------VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEP 167
Cdd:COG1245 422 -LRSANTDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-181 |
1.12e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkrpvigwlaqRHALESQFPLNVQDVVSQGAWPGVSLlrglggcT 117
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQTSWIMPGTIKDNIIFGLSY-------D 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 118 RRRIGAVLERVGL-------AGLAKTPIE----ALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:TIGR01271 515 EYRYTSVIKACQLeedialfPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
31-198 |
1.42e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.65 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGWlaQRHALESQFPLNVQDVVSQGAWPGVSLL 110
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-PLVQY--DHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 RGLGGCTRRRIGAVLERVG----LAGLAK---TPI----EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSREL 179
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANahdfIMEFPNgydTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170
....*....|....*....
gi 1119115049 180 MDLileMYRQGQTILAVLH 198
Cdd:TIGR00958 657 QES---RSRASRTVLLIAH 672
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-194 |
1.63e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119115049 118 RRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-196 |
2.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigwLAQRHALES---QFPLNVQDVVSQGAWPGVSL----- 109
Cdd:PRK10982 274 GEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK-----INNHNANEAinhGFALVTEERRSTGIYAYLDIgfnsl 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 -------LRGLGGCTRRRIGAVLERVGLAGLAKTP-----IEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:PRK10982 349 isnirnyKNKVGLLDNSRMKSDTQWVIDSMRVKTPghrtqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF 428
|
170
....*....|....*....
gi 1119115049 178 ELMDLILEMYRQGQTILAV 196
Cdd:PRK10982 429 EIYQLIAELAKKDKGIIII 447
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-199 |
2.15e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.08 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGW-LAQRHALESQ-FplnvQDvVSQGAWPGVSLL---- 110
Cdd:COG1101 31 EGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLpEYKRAKYIGRvF----QD-PMMGTAPSMTIEenla 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 111 --------RGLG-GCTRRRIGAV---LERVGLaGLA---KTPIEALSGGqfQRMLFARVM--VQQAPLVMLDEPFTGIDE 173
Cdd:COG1101 105 layrrgkrRGLRrGLTKKRRELFrelLATLGL-GLEnrlDTKVGLLSGG--QRQALSLLMatLTKPKLLLLDEHTAALDP 181
|
170 180
....*....|....*....|....*..
gi 1119115049 174 ATSRELMDLILEMYRQGQ-TILAVLHD 199
Cdd:COG1101 182 KTAALVLELTEKIVEENNlTTLMVTHN 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-198 |
3.06e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.18 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDG----VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK------------- 74
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 75 RPVIGWLAQRHALESqfplnvqdvvSQGAWPGVSLLRGLGGCTRRRIGA----VLERVGLAGLAKTPIEALSGGQFQRML 150
Cdd:PRK11153 81 RRQIGMIFQHFNLLS----------SRTVFDNVALPLELAGTPKAEIKArvteLLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119115049 151 FARVMVQQaPLVML-DEPFTGIDEATSRELMDLILEMYRQ-GQTILAVLH 198
Cdd:PRK11153 151 IARALASN-PKVLLcDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-213 |
3.26e-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: 49.18 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 21 GYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKRPVIgwLAQRHALESQFplnvqd 97
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKE--FAEKYPGEIIY------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 98 vVSQGAWPGVSLLrglggcTRRRIGAVLERVGLAGlaktpIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:cd03233 88 -VSEEDVHFPTLT------VRETLDFALRCKGNEF-----VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1119115049 178 ELMDLILEMYRQ--GQTILAVLHDNQRVADFFPETLLL 213
Cdd:cd03233 156 EILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVL 193
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
38-206 |
3.78e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVI----GWLAQRHALES-QFPLnvqdvvsqgawpgvsLLRG 112
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIaisaGLSGQLTGIENiEFKM---------------LCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LggcTRRRIGA----VLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYR 188
Cdd:PRK13546 115 F---KRKEIKAmtpkIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170
....*....|....*...
gi 1119115049 189 QGQTILAVLHDNQRVADF 206
Cdd:PRK13546 192 QNKTIFFVSHNLGQVRQF 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-199 |
3.93e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRL---------RWQGKRP-----------------VIGWLAQRHAL- 87
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivaRLQQDPPrnvegtvydfvaegieeQAEYLKRYHDIs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 88 ------ESQFPLN----VQDVVS-QGAWPGVSllrglggctrrRIGAVLERVGLAglAKTPIEALSGGQFQRMLFARVMV 156
Cdd:PRK11147 106 hlvetdPSEKNLNelakLQEQLDhHNLWQLEN-----------RINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 157 QQAPLVMLDEPFTGIDEATSRELMDLILEMyrQGqTILAVLHD 199
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHD 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-172 |
5.65e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 45 GLNGCGKSTLLKTLAGFLPPVSGRLRWQGkRPV----------IGWLAQRHALESQfpLNV-QDVVsqgawpgvsL---L 110
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVdagdiatrrrVGYMSQAFSLYGE--LTVrQNLE---------LharL 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 111 RGLGGCTRR-RIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:NF033858 367 FHLPAAEIAaRVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
40-213 |
7.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 40 LTAIVGLNGCGKSTLLKTLAGFLPPVSGR-LRWQGKRPV-------IGWLAQRHALESQFPLN--VQDVVSQGAWPGVSL 109
Cdd:PRK13645 39 VTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPAnlkkikeVKRLRKEIGLVFQFPEYqlFQETIEKDIAFGPVN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRGLGGCTRRRIGAVLERVGLAG--LAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY 187
Cdd:PRK13645 119 LGENKQEAYKKVPELLKLVQLPEdyVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLN 197
|
170 180
....*....|....*....|....*..
gi 1119115049 188 R-QGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13645 198 KeYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-183 |
8.26e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGrlrwqgkrpvigwlaqrhalesqfplnvqdvvsqgawpGVSLLRGlggc 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDG---- 38
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119115049 117 trRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLI 183
Cdd:smart00382 39 --EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-205 |
1.03e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 35 ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvIGWLAQRHALESQFPLNVQDVVSQG-------AWPGV 107
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE--INALSTAQRLARGLVYLPEDRQSSGlyldaplAWNVC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 SLLRGLGG--CTRRRIGAVLERVGLA-GL----AKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELM 180
Cdd:PRK15439 364 ALTHNRRGfwIKPARENAVLERYRRAlNIkfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIY 443
|
170 180
....*....|....*....|....*...
gi 1119115049 181 DLILEMYRQGQTILAV---LHDNQRVAD 205
Cdd:PRK15439 444 QLIRSIAAQNVAVLFIssdLEEIEQMAD 471
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-87 |
1.04e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIGWLAQRHAL 87
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-198 |
1.17e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG------KRPVIGWLAqrHALESQFPLNVQDVVSqgAW 104
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniAKPYCTYIG--HNLGLKLEMTVFENLK--FW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 PGVSllrglggCTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLIL 184
Cdd:PRK13541 95 SEIY-------NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
170
....*....|....
gi 1119115049 185 EMYRQGQTILAVLH 198
Cdd:PRK13541 168 MKANSGGIVLLSSH 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-199 |
1.73e-06 |
|
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: 47.22 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 40 LTAIVGLNGCGKSTLLK----TLAGFLPPvsGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVVSqgawpgvsllrglgg 115
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPP--NSKGGAHDPKLIREGEVRAQVKLAFENANGKKYT--------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 116 CTRRRigAVLERV------GLAGLAKTPIEALSGGQfqRMLF--------ARVMVQQAPLVMLDEPFTGIDEATSRE-LM 180
Cdd:cd03240 87 ITRSL--AILENVifchqgESNWPLLDMRGRCSGGE--KVLAsliirlalAETFGSNCGILALDEPTTNLDEENIEEsLA 162
|
170 180
....*....|....*....|.
gi 1119115049 181 DLILEMYRQG--QTILaVLHD 199
Cdd:cd03240 163 EIIEERKSQKnfQLIV-ITHD 182
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-198 |
1.82e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 3 SNLVGG------DAAMIELEQL-VAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLP--------PVSG 67
Cdd:TIGR00954 436 SNLVPGrgiveyQDNGIKFENIpLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvyggrltkPAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 68 RLRWQGKRPVIGwlaqRHALESQ--FPLNVQDVVSqgawpgvsllRGLGGCTRRRI------GAVLERVGLAGLAKTPIE 139
Cdd:TIGR00954 516 KLFYVPQRPYMT----LGTLRDQiiYPDSSEDMKR----------RGLSDKDLEQIldnvqlTHILEREGGWSAVQDWMD 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 140 ALSGGQFQRMLFARVMVQQAPLVMLdepftgiDEATSRELMDLILEMYRQGQ----TILAVLH 198
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAIL-------DECTSAVSVDVEGYMYRLCRefgiTLFSVSH 637
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
37-199 |
1.84e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 47.32 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRpvigWLAQRHALESQFPLNVQDV--VSQ--GAWPGVSLLRG 112
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ----FDFSQKPSEKAIRLLRQKVgmVFQqyNLWPHLTVMEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 L--GGC---------TRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMD 181
Cdd:COG4161 103 LieAPCkvlglskeqAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVE 182
|
170
....*....|....*...
gi 1119115049 182 LILEMYRQGQTILAVLHD 199
Cdd:COG4161 183 IIRELSQTGITQVIVTHE 200
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-213 |
1.94e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVI----GWLAQRHALEsqfplNVQdvvsqgawpgvslLRGL 113
Cdd:PRK13545 50 GEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIaissGLNGQLTGIE-----NIE-------------LKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 114 -GGCTRRRIGAVLERV-GLAGLAK---TPIEALSGGQFQRMLFArVMVQQAP-LVMLDEPFTGIDEATSRELMDLILEMY 187
Cdd:PRK13545 112 mMGLTKEKIKEIIPEIiEFADIGKfiyQPVKTYSSGMKSRLGFA-ISVHINPdILVIDEALSVGDQTFTKKCLDKMNEFK 190
|
170 180
....*....|....*....|....*.
gi 1119115049 188 RQGQTILAVLHDNQRVADFFPETLLL 213
Cdd:PRK13545 191 EQGKTIFFISHSLSQVKSFCTKALWL 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-206 |
2.77e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFlpP----VSGRLRWQGK---------RPVI 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGEsildlepeeRAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 79 GWLaqrhaLESQFPLNVqdvvsqgawPGVS---LLRgLGGCTRRR---------------IGAVLERVGLAG--LAKTPI 138
Cdd:CHL00131 85 GIF-----LAFQYPIEI---------PGVSnadFLR-LAYNSKRKfqglpeldplefleiINEKLKLVGMDPsfLSRNVN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 139 EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHdNQRVADF 206
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-YQRLLDY 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-199 |
4.53e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkrpviGW------------------LAQ---RHALESQF---- 91
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP-----SWdevlkrfrgtelqnyfkkLYNgeiKVVHKPQYvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 PLNVQDVVSQgawpgvsLLRGLGgcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:PRK13409 173 PKVFKGKVRE-------LLKKVD--ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 172 DeatSRELM---DLILEMyRQGQTILAVLHD 199
Cdd:PRK13409 244 D---IRQRLnvaRLIREL-AEGKYVLVVEHD 270
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-199 |
5.01e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.16 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 36 CP-GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRwqgkrpvigwLAQRHALESQFP---------LNVQDVVSQ-GAW 104
Cdd:PRK11124 25 CPqGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLN----------IAGNHFDFSKTPsdkairelrRNVGMVFQQyNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 PGVSLLRGLGGCTRRRIG-----------AVLERVGLAGLA-KTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK11124 95 PHLTVQQNLIEAPCRVLGlskdqalaraeKLLERLRLKPYAdRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180
....*....|....*....|....*..
gi 1119115049 173 EATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:PRK11124 174 PEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
37-201 |
5.02e-06 |
|
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: 45.04 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTlagflppvsgrlrwqgkrpvIGWLAqrhaLESQFPLNVQDVVSQGawpgvsllrglGGC 116
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDA--------------------IGLAL----GGAQSATRRRSGVKAG-----------CIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 117 TRRRIGAVLERVGLaglaktpiealSGGQFQR----MLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQT 192
Cdd:cd03227 65 AAVSAELIFTRLQL-----------SGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ 133
|
....*....
gi 1119115049 193 ILAVLHDNQ 201
Cdd:cd03227 134 VIVITHLPE 142
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-198 |
5.18e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPV------------IGWLAQRhalesqfpLNV--QDVVSQG 102
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK-EVtfngpkssqeagIGIIHQE--------LNLipQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 103 AWPGVSLLRGLGGCTRRRI----GAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:PRK10762 100 IFLGREFVNRFGRIDWKKMyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
|
170 180
....*....|....*....|
gi 1119115049 179 LMDLILEMYRQGQTILAVLH 198
Cdd:PRK10762 180 LFRVIRELKSQGRGIVYISH 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-201 |
5.32e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 22 YDGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPP-------VSGRLRWQgkrPVIGWLAQRHALESqf 91
Cdd:PLN03232 624 WDSKTSKPTLSDInleIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetssvvIRGSVAYV---PQVSWIFNATVREN-- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 PLNVQDVVSQGAWPGVSL------LRGLGGCTRRRIGavlERvglaGLAktpieaLSGGQFQRMLFARVMVQQAPLVMLD 165
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVtalqhdLDLLPGRDLTEIG---ER----GVN------ISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119115049 166 EPFTGIDEATSRELMDLILEMYRQGQTilAVLHDNQ 201
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKT--RVLVTNQ 799
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-199 |
6.18e-06 |
|
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: 46.70 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLrwqgKRPViGW------------------LAQ---RHALESQF---- 91
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY----DEEP-SWdevlkrfrgtelqdyfkkLANgeiKVAHKPQYvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 PLNVQDVVSQgawpgvsLLRGLGgcTRRRIGAVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:COG1245 173 PKVFKGTVRE-------LLEKVD--ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 1119115049 172 DeatSRELM---DLILEMYRQGQTILAVLHD 199
Cdd:COG1245 244 D---IYQRLnvaRLIRELAEEGKYVLVVEHD 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-199 |
6.82e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQ-GKRpvIGWLAQRHALESQfpLNVQDVVSQGAWPGVSLLrglgg 115
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIK--VGYLPQEPQLDPE--KTVRENVEEGVAEVKAAL----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 116 ctrRRIGAVLERVGLAG-----LAK----------------------------------TPIEALSGGQFQRMLFARVMV 156
Cdd:PRK11819 103 ---DRFNEIYAAYAEPDadfdaLAAeqgelqeiidaadawdldsqleiamdalrcppwdAKVTKLSGGERRRVALCRLLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119115049 157 QQAPLVMLDEPFTGIDeATSRELMDLILEMYrQGqTILAVLHD 199
Cdd:PRK11819 180 EKPDMLLLDEPTNHLD-AESVAWLEQFLHDY-PG-TVVAVTHD 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-185 |
1.13e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 13 IELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRwQGKRPVIGWLAQ-RHALESQf 91
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVKLAYVDQsRDALDPN- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 92 pLNVQDVVSQGAwpgvSLLRgLGGctrRRIG--AVLERVGLAGL-AKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPF 168
Cdd:PRK11819 403 -KTVWEEISGGL----DIIK-VGN---REIPsrAYVGRFNFKGGdQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
170
....*....|....*..
gi 1119115049 169 TGIDEATSRELMDLILE 185
Cdd:PRK11819 474 NDLDVETLRALEEALLE 490
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-199 |
1.24e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLP--PV---SGRLRWQGK-------RPVIGWLAQRHALESQFP---LNV 95
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGEsllhaseQTLRGVRGNKIAMIFQEPmvsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 96 QDVVSQGAWPGVSLLRGLGG-CTRRRIGAVLERVGLAGLAKT----PiEALSGGQFQRMLFARVMVQQAPLVMLDEPFTG 170
Cdd:PRK15134 108 LHTLEKQLYEVLSLHRGMRReAARGEILNCLDRVGIRQAAKRltdyP-HQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190
....*....|....*....|....*....|
gi 1119115049 171 IDEATSRELMDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQElNMGLLFITHN 216
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-172 |
1.74e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 12 MIELEQLVAGYDGVAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGF--LPPVSGRLRWQGKRpVIGWLAQRHALES 89
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD-LLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 90 -----QFPLNVqdvvsqgawPGVS----LLRGLGGCTRRRIGAVLERVGLAGLAKTPIEAL---------------SGGQ 145
Cdd:PRK09580 80 ifmafQYPVEI---------PGVSnqffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGE 150
|
170 180
....*....|....*....|....*..
gi 1119115049 146 FQRMLFARVMVQQAPLVMLDEPFTGID 172
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-203 |
1.82e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKST----LLKTLAGflppvSGRLRWQGKrPVIGW-----LAQRHALESQFP---------LNVQDV 98
Cdd:PRK15134 311 PGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQ-PLHNLnrrqlLPVRHRIQVVFQdpnsslnprLNVLQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 99 VSQGawpgvslLR----GLGGCTR-RRIGAVLERVGL--AGLAKTPIEaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGI 171
Cdd:PRK15134 385 IEEG-------LRvhqpTLSAAQReQQVIAVMEEVGLdpETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190
....*....|....*....|....*....|....*
gi 1119115049 172 DEATSRELMDLILEMYRQGQtiLAVL---HDNQRV 203
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQ--LAYLfisHDLHVV 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-199 |
2.39e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 33 GMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVIgwlaqrhalesqfplnvqdvvsqgawpgvsllrg 112
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY---------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 lggctrrrigavlervglaglaKTPIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDE----ATSRELMDLILEmyr 188
Cdd:cd03222 66 ----------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEE--- 120
|
170
....*....|.
gi 1119115049 189 QGQTILAVLHD 199
Cdd:cd03222 121 GKKTALVVEHD 131
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-196 |
2.64e-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: 44.43 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPvsgrlRWQGK-----RPV-IGWLAQrhALESQFPLNVQDVVSQGAWP--GV-- 107
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPG-----KFEGNvfingKPVdIRNPAQ--AIRAGIAMVPEDRKRHGIVPilGVgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 108 ----SLLRGLggCTRRRIGAVLE----RVGLAGLA-KT-----PIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDE 173
Cdd:TIGR02633 359 nitlSVLKSF--CFKMRIDAAAElqiiGSAIQRLKvKTaspflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180
....*....|....*....|...
gi 1119115049 174 ATSRELMDLILEMYRQGQTILAV 196
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVV 459
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-199 |
4.70e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 30 PLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGwlAQRHALESQFPLNVQDVvsqgaWPGVSL 109
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-PVTA--EQPEDYRKLFSAVFTDF-----HLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 110 LRGLGGCTRRRIGAV-LERVGLAglAKTPIE-------ALSGGQFQR--MLFArvMVQQAPLVMLDEPFTGIDEATSREL 179
Cdd:PRK10522 413 LGPEGKPANPALVEKwLERLKMA--HKLELEdgrisnlKLSKGQKKRlaLLLA--LAEERDILLLDEWAADQDPHFRREF 488
|
170 180
....*....|....*....|.
gi 1119115049 180 MDLILEMYRQ-GQTILAVLHD 199
Cdd:PRK10522 489 YQVLLPLLQEmGKTIFAISHD 509
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-208 |
5.92e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 123 AVLERVGLAGLakTP---IEALSGGQFQRMLFARVMVQQAPLVM--LDEPFTGIDEATSRELMDLILEMYRQGQTILAVL 197
Cdd:PRK00635 458 SILIDLGLPYL--TPeraLATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90
....*....|....*..
gi 1119115049 198 HDNQ------RVADFFP 208
Cdd:PRK00635 536 HDEQmisladRIIDIGP 552
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-201 |
7.36e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 22 YDGVAITPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVS-GRLRWQGK---RPVIGWLaqrhalesqFPLN 94
Cdd:PLN03130 624 WDSKAERPTLSNInldVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTvayVPQVSWI---------FNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 95 VQDVVSQGA-------WPGV---SLLRGLGGCTrrriGAVLERVGLAGLaktpieALSGGQFQRMLFARVMVQQAPLVML 164
Cdd:PLN03130 695 VRDNILFGSpfdperyERAIdvtALQHDLDLLP----GGDLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119115049 165 DEPFTGIDEATSRELMDLILEMYRQGQTilAVLHDNQ 201
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKCIKDELRGKT--RVLVTNQ 799
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-209 |
9.14e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 9.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 137 PIEALSGGQFQRMLFARVMVQQAP---LVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQ--RVADFFPE 209
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHvvKVADYVLE 883
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-206 |
9.25e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 125 LERVGLAGLA-KTPIEALSGGQFQRMLFARVMVQQAPLVM--LDEPFTGIDEATSRELMDLILEMYRQGQTILAVLHDNQ 201
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
....*..
gi 1119115049 202 --RVADF 206
Cdd:TIGR00630 552 tiRAADY 558
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-172 |
1.29e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 32 SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPvIGWLAQ------RHALE---------SQFPLNVQ 96
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ-LAWVNQetpalpQPALEyvidgdreyRQLEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 97 DVVSQGAWPGVSLLRGL-----GGCTRRRIGAVLERVGLAGLAKT-PIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTG 170
Cdd:PRK10636 100 DANERNDGHAIATIHGKldaidAWTIRSRAASLLHGLGFSNEQLErPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
..
gi 1119115049 171 ID 172
Cdd:PRK10636 180 LD 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-198 |
1.47e-04 |
|
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: 42.50 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 5 LVGGDAAmIELEQLVAGYD-------GVAITPPlsgmicPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGkrpv 77
Cdd:COG5265 351 LVVGGGE-VRFENVSFGYDperpilkGVSFEVP------AGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 78 igwlaqrhalesqfplnvQDV--VSQgawpgVSLLRGLG----------------------GCTRRRIGAVLE------- 126
Cdd:COG5265 420 ------------------QDIrdVTQ-----ASLRAAIGivpqdtvlfndtiayniaygrpDASEEEVEAAARaaqihdf 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 127 ----------RVGLAGLaKtpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAV 196
Cdd:COG5265 477 ieslpdgydtRVGERGL-K-----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVI 549
|
..
gi 1119115049 197 LH 198
Cdd:COG5265 550 AH 551
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
123-199 |
1.67e-04 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 41.71 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 123 AVLERVGLAGLAKTPIEALSGGQFQRMLFARVMVQQaPLVML-DEPFTGIDEATSRELMDLILEMYRQGQTILAVLHD 199
Cdd:COG4598 137 ALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAME-PEVMLfDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
118-206 |
1.94e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 118 RRRIGaVLERVGLAGLAKT-PIEALSGGQFQRMLFARVMVQQAPLVM--LDEPFTGIDEATSRELMDLILEMYRQGQTIL 194
Cdd:cd03270 115 RERLG-FLVDVGLGYLTLSrSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
|
90
....*....|....
gi 1119115049 195 AVLHDNQ--RVADF 206
Cdd:cd03270 194 VVEHDEDtiRAADH 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
42-199 |
2.23e-04 |
|
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: 41.59 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 42 AIVGLNGCGKS-TLLKTLaGFLPP----VSGRLRWQGK----------RPVIGwlaQRHALESQFP---LN-VQDVVSQG 102
Cdd:COG4172 40 ALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQdllglserelRRIRG---NRIAMIFQEPmtsLNpLHTIGKQI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 103 AWPgVSLLRGLGG-CTRRRIGAVLERVGLAGlAKTPIEA----LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:COG4172 116 AEV-LRLHRGLSGaAARARALELLERVGIPD-PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQA 193
|
170 180
....*....|....*....|...
gi 1119115049 178 ELMDLILEMYRQ-GQTILAVLHD 199
Cdd:COG4172 194 QILDLLKDLQRElGMALLLITHD 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-198 |
4.12e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.10 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGK----------RPVIGWLAQRHALesqFPLNVQDVVSQGAwPG 106
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslRRNIAVVFQDAGL---FNRSIEDNIRVGR-PD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 107 VSLLRGLGGCTR--------RRIGAVLERVGLAGLAktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRE 178
Cdd:PRK13657 436 ATDEEMRAAAERaqahdfieRKPDGYDTVVGERGRQ------LSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170 180
....*....|....*....|
gi 1119115049 179 LMDLILEMyRQGQTILAVLH 198
Cdd:PRK13657 510 VKAALDEL-MKGRTTFIIAH 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
44-102 |
4.64e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 4.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 44 VGLNGCGKSTLLKTLAGFLPPVSGRLRWQ-GKRpvIGWLAQ-RHALESQfplNVQDVVSQG 102
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNER--LGKLRQdQFAFEEF---TVLDTVIMG 88
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
138-196 |
7.60e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 7.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119115049 138 IEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
37-198 |
9.27e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 37 PGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKR-PVI---GWLAqRHALESQFPLNVQDVVSQgawpgvSLLRG 112
Cdd:PRK10789 340 PGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPlTKLqldSWRS-RLAVVSQTPFLFSDTVAN------NIALG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 113 LGGCTRRRIGAV-----------------LERVGLAGLAktpieaLSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEAT 175
Cdd:PRK10789 413 RPDATQQEIEHVarlasvhddilrlpqgyDTEVGERGVM------LSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180
....*....|....*....|...
gi 1119115049 176 SRELMDlILEMYRQGQTILAVLH 198
Cdd:PRK10789 487 EHQILH-NLRQWGEGRTVIISAH 508
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
40-70 |
9.56e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 9.56e-04
10 20 30
....*....|....*....|....*....|.
gi 1119115049 40 LTAIVGLNGCGKSTLLKTLAGFLPPVSGRLR 70
Cdd:COG3950 27 LTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-196 |
1.13e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 137 PIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
141-205 |
1.18e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.34 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119115049 141 LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVL-HDNQRVAD 205
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLItHDLALVAE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-196 |
1.26e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.62 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 14 ELEQL-VAGYDGVaitPPLSGM---ICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKrPVIGW--------- 80
Cdd:COG3845 259 EVENLsVRDDRGV---PALKDVsleVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE-DITGLsprerrrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 81 LA------QRHALESQFPL--NVqdVVSQGAWPGVS---LLRglggctRRRIGAVLER------VGLAGlAKTPIEALSG 143
Cdd:COG3845 335 VAyipedrLGRGLVPDMSVaeNL--ILGRYRRPPFSrggFLD------RKAIRAFAEElieefdVRTPG-PDTPARSLSG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119115049 144 GQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAV 196
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-196 |
1.91e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 38 GSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQGKRPVI-----GwLAQRHALESQ--------FPLNVQDVVSQGAw 104
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdG-LANGIVYISEdrkrdglvLGMSVKENMSLTA- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 105 pgVSLLRGLGGCTRRR--IGAVLERVGLAGLaKTP-----IEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSR 177
Cdd:PRK10762 356 --LRYFSRAGGSLKHAdeQQAVSDFIRLFNI-KTPsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKK 432
|
170
....*....|....*....
gi 1119115049 178 ELMDLILEMYRQGQTILAV 196
Cdd:PRK10762 433 EIYQLINQFKAEGLSIILV 451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-206 |
2.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119115049 137 PIEALSGGQFQRMLFARVMVQQA---PLVMLDEPFTGIDEATSRELMDLILEMYRQGQTILAVLH--DNQRVADF 206
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHnlDVIKTADY 900
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-198 |
2.27e-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: 38.35 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 3 SNLVGgDAAMIELEQLVAGYDGvAITPPL---SGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPPVSGRLRWQG----KR 75
Cdd:cd03288 11 SGLVG-LGGEIKIHDLCVRYEN-NLKPVLkhvKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 76 PVigwlaqrHALESQFPLNVQD-VVSQGawpgvSLLRGLG---GCTRRRIGAVLERVGLaglaKTPIEALSGG------- 144
Cdd:cd03288 89 PL-------HTLRSRLSIILQDpILFSG-----SIRFNLDpecKCTDDRLWEALEIAQL----KNMVKSLPGGldavvte 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119115049 145 ------QFQRMLF--ARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQgQTILAVLH 198
Cdd:cd03288 153 ggenfsVGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAH 213
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-183 |
2.31e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.06 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119115049 140 ALSGGQFQRM----LFA--RVMVQQAP-------LVMLDEPFTGIDEATSRELMDLI 183
Cdd:pfam13558 32 GLSGGEKQLLaylpLAAalAAQYGSAEgrppaprLVFLDEAFAKLDEENIRTALELL 88
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
141-198 |
2.61e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 38.46 E-value: 2.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119115049 141 LSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMyRQGQTILAVLH 198
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH 537
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-198 |
2.74e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 2.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119115049 139 EALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMY-RQGQTILAVLH 198
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1417
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-213 |
3.60e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 31 LSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP--VSGRLRWQGKRPVIGWLAQRHALESQFPLNVQDVVSQGAWPGVS 108
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119115049 109 LLRGLGGCTR----RRIGAVLER----------VGLAGlaktpIEALSGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEA 174
Cdd:PLN03140 979 FLRLPKEVSKeekmMFVDEVMELveldnlkdaiVGLPG-----VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119115049 175 TSRELMDLILEMYRQGQTILAVLHdnQRVADFFP---ETLLL 213
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIH--QPSIDIFEafdELLLM 1093
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
142-204 |
4.01e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 37.78 E-value: 4.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 142 SGGQFQRMLFARVMVQQAPLVMLDEPFTGIDEATSRELMDLILEMYRQGQT-ILAVLHDNQRVA 204
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVA 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-75 |
5.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 5.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1119115049 25 VAITPPLSGMICPGSLTAIVGLNGCGKSTLLKTLAGFLPP---VSGRLRWQGKR 75
Cdd:PLN03140 178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGYR 231
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
40-68 |
6.35e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.29 E-value: 6.35e-03
10 20
....*....|....*....|....*....
gi 1119115049 40 LTAIVGLNGCGKSTLLKTLAGFLPPVSGR 68
Cdd:COG3593 25 LTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| |
